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1
Kuczak, Michał, and Ewa Kurczyńska. "Cell Wall Composition as a Marker of the Reprogramming of the Cell Fate on the Example of a Daucus carota (L.) Hypocotyl in Which Somatic Embryogenesis Was Induced." International Journal of Molecular Sciences 21, no. 21 (October 30, 2020): 8126. http://dx.doi.org/10.3390/ijms21218126.
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Changes in the composition of the cell walls are postulated to accompany changes in the cell’s fate. We check whether there is a relationship between the presence of selected pectic, arabinogalactan proteins (AGPs), and extensins epitopes and changes in cell reprogramming in order to answer the question of whether they can be markers accompanying changes of cell fate. Selected antibodies were used for spatio-temporal immunolocalization of wall components during the induction of somatic embryogenesis. Based on the obtained results, it can be concluded that (1) the LM6 (pectic), LM2 (AGPs) epitopes are positive markers, but the LM5, LM19 (pectic), JIM8, JIM13 (AGPs) epitopes are negative markers of cells reprogramming to the meristematic/pluripotent state; (2) the LM8 (pectic), JIM8, JIM13, LM2 (AGPs) and JIM11 (extensin) epitopes are positive markers, but LM6 (pectic) epitope is negative marker of cells undergoing detachment; (3) JIM4 (AGPs) is a positive marker, but LM5 (pectic), JIM8, JIM13, LM2 (AGPs) are negative markers for pericycle cells on the xylem pole; (4) LM19, LM20 (pectic), JIM13, LM2 (AGPs) are constitutive wall components, but LM6, LM8 (pectic), JIM4, JIM8, JIM16 (AGPs), JIM11, JIM12 and JIM20 (extensins) are not constitutive wall components; (5) the extensins do not contribute to the cell reprogramming.
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Larsen, Nadja, Mette Boye, Henrik Siegumfeldt, and Mogens Jakobsen. "Differential Expression of Proteins and Genes in the Lag Phase of Lactococcus lactis subsp. lactis Grown in Synthetic Medium and Reconstituted Skim Milk." Applied and Environmental Microbiology 72, no. 2 (February 2006): 1173–79. http://dx.doi.org/10.1128/aem.72.2.1173-1179.2006.
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ABSTRACT We investigated protein and gene expression in the lag phase of Lactococcus lactis subsp. lactis CNRZ 157 and compared it to the exponential and stationary phases. By means of two-dimensional polyacrylamide gel electrophoresis, 28 highly expressed lag-phase proteins, implicated in nucleotide metabolism, glycolysis, stress response, translation, transcription, cell division, amino acid metabolism, and coenzyme synthesis, were identified. Among the identified proteins, >2-fold induction and down-regulation in the lag phase were determined for 12 proteins in respect to the exponential phase and for 18 proteins in respect to the stationary phase. Transcriptional changes of the lag-phase proteins in L. lactis were studied by oligonucleotide microarrays. Good correlation between protein and gene expression studies was demonstrated for several differentially expressed proteins, including nucleotide biosynthetic enzymes, adenylosuccinate synthase (PurA), IMP dehydrogenase (GuaB), and aspartate carbamoyl transferase (PyrB); heat-shock protein DnaK; serine hydroxymethyl transferase (GlyA); carbon catabolite control protein (CcpA); elongation factor G (FusA); and cell division protein (FtsZ).
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Coenye, Tom, Elke Vanlaere, Enevold Falsen, and Peter Vandamme. "Stenotrophomonas africana Drancourt et al. 1997 is a later synonym of Stenotrophomonas maltophilia (Hugh 1981) Palleroni and Bradbury 1993." International Journal of Systematic and Evolutionary Microbiology 54, no. 4 (July 1, 2004): 1235–37. http://dx.doi.org/10.1099/ijs.0.63093-0.
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Type and reference strains of Stenotrophomonas maltophilia and Stenotrophomonas africana were compared with each other and with the type strains of other Stenotrophomonas species, using SDS-PAGE of whole-cell proteins, DNA–DNA hybridization and extensive biochemical characterization. S. maltophilia LMG 958T and S. africana LMG 22072T had very similar whole-cell-protein patterns and were also biochemically very similar. A DNA–DNA binding level of 70 % between both type strains confirmed that S. africana and S. maltophilia represent the same taxon. It is concluded that S. africana is a later synonym of S. maltophilia.
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El-Behaedi, Salma, Rebekah Landsman, Michael Rudloff, Emily Kolyvas, Rakan Albalawy, Xianyu Zhang, Tapan Bera, Keith Collins, Serguei Kozlov, and Christine Alewine. "Protein Synthesis Inhibition Activity of Mesothelin Targeting Immunotoxin LMB-100 Decreases Concentrations of Oncogenic Signaling Molecules and Secreted Growth Factors." Toxins 10, no. 11 (October 31, 2018): 447. http://dx.doi.org/10.3390/toxins10110447.
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LMB-100 is a mesothelin-targeted recombinant immunotoxin (iTox) that carries a modified Pseuodomonas exotoxin A (PE) payload. PE kills cells by inhibiting synthesis of new proteins. We found that treatment of pancreatic cancer cells with LMB-100 for 24–48 h did not change total protein level despite inducing protein synthesis inhibition (PSI). Further, increased levels of ubiquitinated proteins were detected, indicating that cells may have limited ability to compensate for PSI by reducing protein degradation. Together, these data suggest that PE depletes concentrations of a minority of cellular proteins. We used reverse phase protein array and Luminex assay to characterize this subset. LMB-100 decreased the abundance of 24 of 32 cancer-related proteins (including Bcl-x, Her2, Her3 and MUC16) without compensatory increases in other analytes. Further, cancer cells failed to maintain extracellular concentrations of cancer cell secreted growth factors (CCSGFs), including Vascular Endothelial Growth Factor (VEGF) following treatment with cytostatic LMB-100 doses both in culture and in mouse tumors. Decreased VEGF concentration did not change tumor vasculature density, however, LMB-100 caused tissue-specific changes in concentrations of secreted factors made by non-cancer cells. In summary, our data indicate that PSI caused by cytostatic LMB-100 doses preferentially depletes short-lived proteins such as oncogenic signaling molecules and CCSGFs.
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Kuniyoshi, Hisato, Kotaro Baba, Ryu Ueda, Shunzo Kondo, Wakae Awano, Naoto Juni, and Daisuke Yamamoto. "lingerer, a Drosophila Gene Involved in Initiation and Termination of Copulation, Encodes a Set of Novel Cytoplasmic Proteins." Genetics 162, no. 4 (December 1, 2002): 1775–89. http://dx.doi.org/10.1093/genetics/162.4.1775.
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Abstract In an effort to uncover genetic components underlying the courtship behavior of Drosophila melanogaster, we have characterized a novel gene, lingerer (lig), mutations of which result in abnormal copulation. Males carrying a hypomorphic mutation in lig fail to withdraw their genitalia upon termination of copulation, but display no overt abnormalities in their genitalia. A severe reduction in the dosage of the lig gene causes repeated attempted copulations but no successful copulations. Complete loss of lig function results in lethality during early pupal stages. lig is localized to polytene segment 44A on the second chromosome and encodes three alternatively spliced transcripts that generate two types of 150-kD proteins, Lig-A and Lig-B, differing only at the C terminus. Lig proteins show no similarity to known proteins. However, a set of homologous proteins in mammals suggest that Drosophila Lig belongs to a family of proteins that share five highly conserved domains. Lig is a cytoplasmic protein expressed in the central nervous system (CNS), imaginal discs, and gonads. Lig-A expression is selectively reduced in lig mutants and the ubiquitous supply of this protein at the beginning of metamorphosis restores the copulatory defects of the lig mutant. We propose that lig may act in the nervous system to mediate the control of copulatory organs during courtship.
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Nilsen, Trine, Ingolf F. Nes, and Helge Holo. "Enterolysin A, a Cell Wall-Degrading Bacteriocin from Enterococcus faecalis LMG 2333." Applied and Environmental Microbiology 69, no. 5 (May 2003): 2975–84. http://dx.doi.org/10.1128/aem.69.5.2975-2984.2003.
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ABSTRACT A novel antimicrobial protein, designated enterolysin A, was purified from an Enterococcus faecalis LMG 2333 culture. Enterolysin A inhibits growth of selected enterococci, pediococci, lactococci, and lactobacilli. Antimicrobial activity was initially detected only on solid media, but by growing the bacteria in a fermentor under optimized production conditions (MRS broth with 4% [wt/vol] glucose, pH 6.5, and a temperature between 25 and 35°C), the bacteriocin activity was increased to 5,120 bacteriocin units ml−1. Enterolysin A production was regulated by pH, and activity was first detected in the transition between the logarithmic and stationary growth phases. Killing of sensitive bacteria by enterolysin A showed a dose-response behavior, and the bacteriocin has a bacteriolytic mode of action. Enterolysin A was purified, and the primary structure was determined by combined amino acid and DNA sequencing. This bacteriocin is translated as a 343-amino-acid preprotein with an sec-dependent signal peptide of 27 amino acids, which is followed by a sequence corresponding to the N-terminal part of the purified protein. Mature enterolysin A consists of 316 amino acids and has a calculated molecular weight of 34,501, and the theoretical pI is 9.24. The N terminus of enterolysin A is homologous to the catalytic domains of different cell wall-degrading proteins with modular structures. These include lysostaphin, ALE-1, zoocin A, and LytM, which are all endopeptidases belonging to the M37 protease family. The N-terminal part of enterolysin A is linked by a threonine-proline-rich region to a putative C-terminal recognition domain, which shows significant sequence identity to two bacteriophage lysins.
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Bagon, Bernadette B., Ju Kyoung Oh, Valerie Diane V. Valeriano, Edward Alain B. Pajarillo, and Dae-Kyung Kang. "Exploring the Bile Stress Response of Lactobacillus mucosae LM1 through Exoproteome Analysis." Molecules 26, no. 18 (September 20, 2021): 5695. http://dx.doi.org/10.3390/molecules26185695.
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Lactobacillus sp. have long been studied for their great potential in probiotic applications. Recently, proteomics analysis has become a useful tool for studies on potential lactobacilli probiotics. Specifically, proteomics has helped determine and describe the physiological changes that lactic acid bacteria undergo in specific conditions, especially in the host gut. In particular, the extracellular proteome, or exoproteome, of lactobacilli contains proteins specific to host– or environment–microbe interactions. Using gel-free, label-free ultra-high performance liquid chromatography tandem mass spectrometry, we explored the exoproteome of the probiotic candidate Lactobacillus mucosae LM1 subjected to bile treatment, to determine the proteins it may use against bile stress in the gut. Bile stress increased the size of the LM1 exoproteome, secreting ribosomal proteins (50S ribosomal protein L27 and L16) and metabolic proteins (lactate dehydrogenase, phosphoglycerate kinase, glyceraldehyde-3-phosphate dehydrogenase and pyruvate dehydrogenases, among others) that might have moonlighting functions in the LM1 bile stress response. Interestingly, membrane-associated proteins (transporters, peptidase, ligase and cell division protein ftsH) were among the key proteins whose secretion were induced by the LM1 bile stress response. These specific proteins from LM1 exoproteome will be useful in observing the proposed bile response mechanisms via in vitro experiments. Our data also reveal the possible beneficial effects of LM1 to the host gut.
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Faye, Therese, Dag Anders Brede, Thor Langsrud, Ingolf F. Nes, and Helge Holo. "An Antimicrobial Peptide Is Produced by Extracellular Processing of a Protein from Propionibacterium jensenii." Journal of Bacteriology 184, no. 13 (July 1, 2002): 3649–56. http://dx.doi.org/10.1128/jb.184.13.3649-3656.2002.
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ABSTRACT A protease-activated antimicrobial peptide (PAMP) and its inactive precursor were purified from the culture supernatant of Propionibacterium jensenii LMG 3032 and characterized at the molecular level. PAMP is a 64-amino-acid cationic peptide of 6,383 Da with physicochemical features similar to those of bacteriocins from gram-positive bacteria. This peptide displayed bactericidal activity against several propionibacteria and lactobacilli. DNA sequencing indicated that the PAMP-encoding gene (pamA) is translated as a proprotein of 198 amino acids with an N-terminal signal peptide of 27 amino acids and that PAMP constitutes the C-terminal part of this precursor. The amino acid sequence of pro-PAMP showed no similarity to those of other known proteins. By using activity tests and mass spectrometry, we showed that PAMP was formed upon protease treatment of the precursor protein. The propionibacteria produced the PAMP precursor constitutively during growth up to a level of ∼4 mg/liter, but the producing bacteria were unable to activate the precursor. The requirement for an external protease represents a novel strategy for generating antimicrobial peptides.
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Popielarska-Konieczna, Marzena, Katarzyna Sala, Mohib Abdullah, Monika Tuleja, and Ewa Kurczyńska. "Extracellular matrix and wall composition are diverse in the organogenic and non-organogenic calli of Actinidia arguta." Plant Cell Reports 39, no. 6 (March 30, 2020): 779–98. http://dx.doi.org/10.1007/s00299-020-02530-2.
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Abstract Key message Differences in the composition and the structural organisation of the extracellular matrix correlate with the morphogenic competence of the callus tissue that originated from the isolated endosperm of kiwifruit. Abstract The chemical composition and structural organisation of the extracellular matrix, including the cell wall and the layer on its surface, may correspond with the morphogenic competence of a tissue. In the presented study, this relationship was found in the callus tissue that had been differentiated from the isolated endosperm of the kiwiberry, Actinidia arguta. The experimental system was based on callus samples of exactly the same age that had originated from an isolated endosperm but were cultured under controlled conditions promoting either an organogenic or a non-organogenic pathway. The analyses which were performed using bright field, fluorescence and scanning electron microscopy techniques showed significant differences between the two types of calli. The organogenic tissue was compact and the outer walls of the peripheral cells were covered with granular structures. The non-organogenic tissue was composed of loosely attached cells, which were connected via a net-like structure. The extracellular matrices from both the non- and organogenic tissues were abundant in pectic homogalacturonan and extensins (LM19, LM20, JIM11, JIM12 and JIM20 epitopes), but the epitopes that are characteristic for rhamnogalacturonan I (LM5 and LM6), hemicellulose (LM25) and the arabinogalactan protein (LM2) were detected only in the non-organogenic callus. Moreover, we report the epitopes, which presence is characteristic for the Actinidia endosperm (LM21 and LM25, heteromannan and xyloglucan) and for the endosperm-derived cells that undergo dedifferentiation (loss of LM21 and LM25; appearance or increase in the content of LM5, LM6, LM19, JIM11, JIM12, JIM20, JIM8 and JIM16 epitopes).
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Louis, Magali, Jacques R. Poortmans, Marc Francaux, Jacques Berré, Nathalie Boisseau, Eric Brassine, Daniel J. R. Cuthbertson, et al. "No effect of creatine supplementation on human myofibrillar and sarcoplasmic protein synthesis after resistance exercise." American Journal of Physiology-Endocrinology and Metabolism 285, no. 5 (November 2003): E1089—E1094. http://dx.doi.org/10.1152/ajpendo.00195.2003.
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Muscle hypertrophy during resistance training is reportedly increased by creatine supplementation. Having previously failed to find an anabolic effect on muscle protein turnover at rest, either fed or fasted, we have now examined the possibility of a stimulatory effect of creatine in conjunction with acute resistance exercise. Seven healthy men (body mass index, 23 ± 2 kg/m2, 21 ± 1 yr, means ± SE) performed 20 × 10 repetitions of leg extension-flexion at 75% one-repetition maximum in one leg, on two occasions, 4 wk apart, before and after ingesting 21 g/day creatine for 5 days. The subjects ate ∼21 g maltodextrin + 6 g protein/h for 3 h postexercise. We measured incorporation of [1-13C]leucine into quadriceps muscle proteins in the rested and exercised legs. Leg protein breakdown (as dilution of [2H5]phenylalanine) was also assessed in the exercised and rested leg postexercise. Creatine supplementation increased muscle total creatine by ∼21% ( P < 0.01). Exercise increased the synthetic rates of myofibrillar and sarcoplasmic proteins by two- to threefold ( P < 0.05), and leg phenylalanine balance became more positive, but creatine was without any anabolic effect.
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Freedman, Deborah A., and Arnold J. Levine. "Nuclear Export Is Required for Degradation of Endogenous p53 by MDM2 and Human Papillomavirus E6." Molecular and Cellular Biology 18, no. 12 (December 1, 1998): 7288–93. http://dx.doi.org/10.1128/mcb.18.12.7288.
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ABSTRACT The MDM2 oncoprotein targets the p53 tumor suppressor protein for degradation when the two proteins are expressed in cells. The regulation of p53 levels by MDM2 requires the ability of MDM2 to be exported from the nucleus by utilizing its nuclear export signal (NES). The drug leptomycin B (LMB) blocks the formation of nuclear export complexes consisting of CRM1, RanGTP, and NES-containing proteins. It is predicted that LMB should inhibit nuclear-cytoplasmic shuttling by MDM2 and subsequently stabilize p53. This communication demonstrates that LMB treatment of various cell lines led to an increase in the steady-state levels of the p53 protein as a result of an increase in its stability. The stabilized p53 protein localized to the nucleus and was an active transcription factor. These results indicate that the low steady-state levels of p53 in the absence of DNA damage result from p53’s nuclear export for cytoplasmic degradation. LMB also led to p53 stabilization in cell lines that contain human papillomavirus (HPV) DNA and express HPV E6, a protein that targets p53 for degradation. MDM2 is not necessary for E6-dependent degradation of p53, as evidenced by the observation that E6 promoted p53 degradation in cells lacking endogenous MDM2. In addition, LMB reduced E6’s ability to degrade p53 in the absence of MDM2, demonstrating that complete degradation of p53 by E6 requires nuclear export and therefore likely occurs in cytoplasmic proteasomes. These data suggest that the nuclear export of p53 to the cytoplasm for degradation is a general mechanism for regulating p53 levels.
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Koort, Joanna, Tom Coenye, Peter Vandamme, Antti Sukura, and Johanna Björkroth. "Enterococcus hermanniensis sp. nov., from modified-atmosphere-packaged broiler meat and canine tonsils." International Journal of Systematic and Evolutionary Microbiology 54, no. 5 (September 1, 2004): 1823–27. http://dx.doi.org/10.1099/ijs.0.63112-0.
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Isolates 302, 334, 356, 377 and 379, detected in modified-atmosphere-packaged broiler meat, together with strains LMG 12317T and LMG 13617, detected in dog tonsils, were analysed in a polyphasic taxonomy study, including numerical analysis of ribopatterns and whole-cell protein patterns, 16S rRNA gene sequence analysis, DNA–DNA hybridization and determination of some phenotypic properties. The results indicated that these isolates represent a novel species in the genus Enterococcus. The isolates showed classical phenotypic reactions for the genus Enterococcus with the exception of not possessing the Lancefield group D antigen. Isolates 334, LMG 12317T and LMG 13617 showed the highest 16S rRNA gene sequence similarity (98·3–99·0 %) to the Enterococcus pallens type strain. In the distance matrix tree based on 16S rRNA gene sequences, the three isolates were located in the Enterococcus avium group with E. pallens as their closest phylogenetic neighbour. Numerical analyses of whole-cell protein patterns and HindIII/EcoRI ribotypes placed all seven isolates together in a single cluster separated from the E. avium group reference strains. The DNA–DNA hybridization level between strains 334 and LMG 12317T was 93·5 %, confirming that they represent the same species. Low hybridization levels (12–30 %) were, by contrast, obtained with the E. pallens and Enterococcus raffinosus type strains. The name Enterococcus hermanniensis sp. nov. is proposed, with strain LMG 12317T (=CCUG 48100T) as the type strain.
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Naser, Sabri M., Marc Vancanneyt, Evelyne De Graef, Luc A. Devriese, Cindy Snauwaert, Karen Lefebvre, Bart Hoste, et al. "Enterococcus canintestini sp. nov., from faecal samples of healthy dogs." International Journal of Systematic and Evolutionary Microbiology 55, no. 5 (September 1, 2005): 2177–82. http://dx.doi.org/10.1099/ijs.0.63752-0.
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The taxonomic position of strain LMG 13590T, originally isolated from dog faeces and classified as Enterococcus dispar in the BCCM/LMG Bacteria Catalogue, was reinvestigated. This strain and 12 recent isolates from faecal samples of healthy dogs occupied a clearly separate position when investigated with multilocus sequence analysis (MLSA) of the genes encoding the alpha subunit of ATP synthase (atpA), RNA polymerase alpha subunit (rpoA) and phenylalanyl-tRNA synthase alpha subunit (pheS). The 16S rRNA gene sequence of one representative strain showed highest similarities of 98–99 % with E. dispar LMG 13521T, Enterococcus canis LMG 12316T and Enterococcus asini LMG 18727T. A further polyphasic taxonomic study based on whole-cell protein fingerprinting, DNA–DNA hybridization and biochemical features demonstrated that the 13 enterococcal dog faecal strains represent a single, novel Enterococcus species for which the name Enterococcus canintestini sp. nov. is proposed. The type strain is LMG 13590T (=CCM 7285T).
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Ogborn, Daniel I., Bryon R. McKay, Justin D. Crane, Gianni Parise, and Mark A. Tarnopolsky. "The unfolded protein response is triggered following a single, unaccustomed resistance-exercise bout." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 307, no. 6 (September 15, 2014): R664—R669. http://dx.doi.org/10.1152/ajpregu.00511.2013.
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Endoplasmic reticulum (ER) stress results from an imbalance between the abundance of synthesized proteins and the folding capacity of the ER. In response, the unfolded protein response (UPR) attempts to restore ER function by attenuating protein synthesis and inducing chaperone expression. Resistance exercise (RE) stimulates protein synthesis; however, a postexercise accumulation of unfolded proteins may activate the UPR. Aging may impair protein folding, and the accumulation of oxidized and misfolded proteins may stimulate the UPR at rest in aged muscle. Eighteen younger ( n = 9; 21 ± 3 yr) and older ( n = 9; 70 ± 4 yr) untrained men completed a single, unilateral bout of RE using the knee extensors (four sets of 10 repetitions at 75% of one repetition maximum on the leg press and leg extension) to determine whether the UPR is increased in resting, aged muscle and whether RE stimulates the UPR. Muscle biopsies were taken from the nonexercised and exercised vastus lateralis at 3, 24, and 48 h postexercise. Age did not affect any of the proteins and transcripts related to the UPR. Glucose-regulated protein 78 (GRP78) and protein kinase R-like ER protein kinase (PERK) proteins were increased at 48 h postexercise, whereas inositol-requiring enzyme 1 alpha (IRE1α) was elevated at 24 h and 48 h. Despite elevated protein, GRP78 and PERK mRNA was unchanged; however, IRE1α mRNA was increased at 24 h postexercise. Activating transcription factor 6 (ATF6) mRNA increased at 24 h and 48 h, whereas ATF4, CCAAT/enhancer-binding protein homologous protein (CHOP), and growth arrest and DNA damage protein 34 mRNA were unchanged. These data suggest that RE activates specific pathways of the UPR (ATF6/IRE1α), whereas PERK/eukaryotic initiation factor 2 alpha/CHOP does not. In conclusion, acute RE results in UPR activation, irrespective of age.
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Debruyne, Lies, Tina Broman, Sven Bergström, Björn Olsen, Stephen L. W. On, and Peter Vandamme. "Campylobacter volucris sp. nov., isolated from black-headed gulls (Larus ridibundus)." International Journal of Systematic and Evolutionary Microbiology 60, no. 8 (August 1, 2010): 1870–75. http://dx.doi.org/10.1099/ijs.0.013748-0.
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During a study of the prevalence of Campylobacter jejuni in black-headed gulls (Larus ridibundus) in Sweden, three isolates, strains LMG 24379, LMG 24380T and LMG 24381, were initially identified as Campylobacter lari. Further characterization by both AFLP and whole-cell protein SDS-PAGE analyses revealed that they formed a distinct group in the genus Campylobacter. This unique position was confirmed by phenotypic characterization, 16S rRNA and hsp60 gene sequence analysis and DNA–DNA hybridizations. The combined data confirm that these isolates represent a novel species within the genus Campylobacter, for which the name Campylobacter volucris sp. nov. is proposed. The type strain is LMG 24380T (=CCUG 57498T).
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Vesali, Rokhsareh F., Norbert Cibicek, Towe Jakobsson, Maria Klaude, Jan Wernerman, and Olav Rooyackers. "Protein metabolism in leg muscle following an endotoxin injection in healthy volunteers." Clinical Science 118, no. 6 (December 14, 2009): 421–27. http://dx.doi.org/10.1042/cs20090332.
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The human endotoxin model has been used to study the early phase of sepsis. The aim of the present study was to assess leg muscle protein kinetics after an endotoxin challenge given to healthy human volunteers. Six healthy male subjects were studied in the post-absorptive state before and during 4 h following an intravenous endotoxin bolus (4 ng/kg of body weight). Primed continuous infusion of [2H5]phenylalanine and [2H3]3-methylhistidine in combination with sampling from the radial artery, femoral vein and muscle tissue were used to assess leg muscle protein kinetics. Both two- and three-compartment models were used to calculate protein kinetics. In addition 26S proteasome activity and protein ubiquitination were assessed. An increase in the net release of phenylalanine from the leg following the endotoxin challenge was observed; however, this phenylalanine originates from the free intracellular pool and not from protein. Net protein balance was unchanged, whereas both protein synthesis and breakdown were decreased. Degradation rates of contractile proteins were not affected by endotoxin, as indicated by an unchanged rate of appearance of 3-methylhistidine from leg muscle. In addition, proteasome activity and protein ubiquitination were unaffected by endotoxaemia. In conclusion, intravenous endotoxin administration to healthy volunteers resulted in an increased release of free phenylalanine from skeletal muscle, whereas protein balance was unaffected. Both protein synthesis and breakdown were decreased to a similar extent.
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Silva, Kleber Resende, Vinícius Coelho Kuster, Ana Flávia de Melo Silva, and Denis Coelho de Oliveira. "Remodelling of cell wall composition during leaf development in Lavoisiera mucorifera (Melastomataceae)." Australian Journal of Botany 67, no. 2 (2019): 140. http://dx.doi.org/10.1071/bt18123.
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How does the deposition of cell wall components structure cell shape and function during leaf ontogenesis? Although this issue has been the subject of several studies, a wide variety of standards have been reported and many knowledge gaps remain. In this study we evaluated cell wall composition in leaf tissues of Lavoisiera mucorifera Mart. & Schrank ex DC. (Melastomataceae) regarding cellulose, pectin (homogalacturonans (HGs) and rhamnogalacturonans I (RGI)) and arabinogalactan protein (AGP) distribution during ontogenesis. Leaf primordium, as well as young and mature leaves, were submitted to histochemical analysis using calcofluor white and ruthenium red, and immunocytochemical analysis using primary monoclonal antibodies (JIM5, JIM7, LM2, LM5 and LM6). Results showed that the distribution of cell wall components depends on tissue and leaf developmental stage. At the beginning of cell differentiation in the leaf primordium, two main patterns of cellulose microfibril orientation occur: perpendicular and random. This initial microfibril arrangement determines final cell shape and leaf tissue functionality in mature leaves. During leaf development, especially in epidermal and collenchyma cells, the association of HGs with low methyl-esterified groups and cellulose guarantees mechanical support. As a result, cell wall properties, such as rigidity and porosity, may also be acquired by changes in cell wall composition and are associated with morphogenetic patterns in L. mucorifera.
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Moulin, Pauline, Kévin Patron, Camille Cano, Mohamed Amine Zorgani, Emilie Camiade, Elise Borezée-Durant, Agnès Rosenau, Laurent Mereghetti, and Aurélia Hiron. "The Adc/Lmb System Mediates Zinc Acquisition in Streptococcus agalactiae and Contributes to Bacterial Growth and Survival." Journal of Bacteriology 198, no. 24 (September 26, 2016): 3265–77. http://dx.doi.org/10.1128/jb.00614-16.
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ABSTRACT The Lmb protein of Streptococcus agalactiae is described as an adhesin that binds laminin, a component of the human extracellular matrix. In this study, we revealed a new role for this protein in zinc uptake. We also identified two Lmb homologs, AdcA and AdcAII, redundant binding proteins that combine with the AdcCB translocon to form a zinc-ABC transporter. Expression of this transporter is controlled by the zinc concentration in the medium through the zinc-dependent regulator AdcR. Triple deletion of lmb , adcA , and adcAII , or that of the adcCB genes, impaired growth and cell separation in a zinc-restricted environment. Moreover, we found that this Adc zinc-ABC transporter promotes S. agalactiae growth and survival in some human biological fluids, suggesting that it contributes to the infection process. These results indicated that zinc has biologically vital functions in S. agalactiae and that, under the conditions tested, the Adc/Lmb transporter constitutes the main zinc acquisition system of the bacterium. IMPORTANCE A zinc transporter, composed of three redundant binding proteins (Lmb, AdcA, and AdcAII), was characterized in Streptococcus agalactiae . This system was shown to be essential for bacterial growth and morphology in zinc-restricted environments, including human biological fluids.
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Sinha, Krishna Murari, Jane C. Hines, and Dan S. Ray. "Cell Cycle-Dependent Localization and Properties of a Second Mitochondrial DNA Ligase in Crithidia fasciculata." Eukaryotic Cell 5, no. 1 (January 2006): 54–61. http://dx.doi.org/10.1128/ec.5.1.54-61.2006.
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ABSTRACT The mitochondrial DNA in kinetoplastid protozoa is contained in a single highly condensed structure consisting of thousands of minicircles and approximately 25 maxicircles. The disk-shaped structure is termed kinetoplast DNA (kDNA) and is located in the mitochondrial matrix near the basal body. We have previously identified a mitochondrial DNA ligase (LIG kβ) in the trypanosomatid Crithidia fasciculata that localizes to antipodal sites flanking the kDNA disk where several other replication proteins are localized. We describe here a second mitochondrial DNA ligase (LIG kα). LIG kα localizes to the kinetoplast primarily in cells that have completed mitosis and contain either a dividing kinetoplast or two newly divided kinetoplasts. Essentially all dividing or newly divided kinetoplasts show localization of LIG kα. The ligase is present on both faces of the kDNA disk and at a high level in the kinetoflagellar zone of the mitochondrial matrix. Cells containing a single nucleus show localization of the LIG kα to the kDNA but at a much lower frequency. The mRNA level of LIG kα varies during the cell cycle out of phase with that of LIG kβ. LIG kα transcript levels are maximal during the phase when cells contain two nuclei, whereas LIG kβ transcript levels are maximal during S phase. The LIG kα protein decays with a half-life of 100 min in the absence of protein synthesis. The periodic expression of the LIG kα transcript and the instability of the LIG kα protein suggest a possible role of the ligase in regulating minicircle replication.
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Baixeras, E., B. Huard, C. Miossec, S. Jitsukawa, M. Martin, T. Hercend, C. Auffray, F. Triebel, and D. Piatier-Tonneau. "Characterization of the lymphocyte activation gene 3-encoded protein. A new ligand for human leukocyte antigen class II antigens." Journal of Experimental Medicine 176, no. 2 (August 1, 1992): 327–37. http://dx.doi.org/10.1084/jem.176.2.327.
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The lymphocyte activation gene 3 (LAG-3), expressed in human activated T and natural killer (NK) cells, is closely related to CD4 at the gene and protein levels. We report here the initial characterization of the LAG-3-encoded protein. We have generated two monoclonal antibodies after immunization of mice with a 30-amino acid peptide that corresponds to an exposed extra loop region present in the LAG-3 immunoglobulin-like first domain. The reactivity of these reagents is directed against LAG-3 since they recognize both membrane-expressed and soluble recombinant LAG-3 molecules produced in a baculovirus expression system. The two antibodies are likely to react with the same or closely related epitope (termed LAG-3.1) exposed on the LAG-3 first domain extra loop, as assessed in competition experiments on LAG-3-expressing activated lymphocytes. Cellular distribution analysis indicated that the LAG-3.1 epitope is expressed on activated T (both CD4+ and CD8+ subsets) and NK cells, and not on activated B cells or monocytes. In immunoprecipitation experiments performed on activated T and NK cell lysates, a 70-kD protein was detected after SDS-PAGE analysis. 45-kD protein species were also immunoprecipitated. Both the 70- and 45-kD proteins were shown to be N-glycosylated. In Western blot analysis, only the former molecule was recognized by the anti-LAG-3 antibodies, demonstrating that it is LAG-3 encoded. These anti-LAG-3 antibodies were used to investigate whether the LAG-3 protein interacts with the CD4 ligands. By using a high-level expression cellular system based on COS-7 cell transfection with recombinant CDM8 vectors and a quantitative cellular adhesion assay, we demonstrate that rosette formation between LAG-3-transfected COS-7 cells and human leukocyte antigen (HLA) class II-bearing B lymphocytes is specifically dependent on LAG-3/HLA class II interaction. In contrast to CD4, LAG-3 does not bind the human immunodeficiency virus gp120. This initial characterization will guide further studies on the functions of this molecule, which may play an important role in immune responses mediated by T and NK lymphocytes.
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Švec, Pavel, Marc Vancanneyt, Luc A. Devriese, Sabri M. Naser, Cindy Snauwaert, Karen Lefebvre, Bart Hoste, and Jean Swings. "Enterococcus aquimarinus sp. nov., isolated from sea water." International Journal of Systematic and Evolutionary Microbiology 55, no. 5 (September 1, 2005): 2183–87. http://dx.doi.org/10.1099/ijs.0.63722-0.
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Two enterococcal strains LMG 16607T and LMG 16612 originating from sea water were analysed in a polyphasic taxonomic study. Both strains, assigned as Enterococcus sp. in the BCCM/LMG culture collection, possessed analogous protein profiles, but these were different from all other enterococcal species. 16S rRNA gene sequence analysis of one strain showed the highest similarity, 96·9–96·1 %, with its closest phylogenetic neighbours Enterococcus saccharolyticus, Enterococcus sulfureus, Enterococcus saccharominimus and Enterococcus italicus. Further genomic analysis by (GTG)5-PCR fingerprinting and sequence analysis of the housekeeping gene phenylalanyl-tRNA synthase (pheS) and distinct biochemical features confirmed that the two strains represent a novel enterococcal species for which the name Enterococcus aquimarinus sp. nov. is proposed. The type strain is LMG 16607T (=CCM 7283T).
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Townsend, Jeremy, Jaclyn Morimune, Megan Jones, Laurel Littlefield, Stephen Heffington, Trisha Van Dusseldorp, Yuri Feito, and Gerald Mangine. "The Effects of a Protease Enzyme Blend on Post-Resistance Exercise Intramuscular Anabolic Signaling." Current Developments in Nutrition 4, Supplement_2 (May 29, 2020): 1767. http://dx.doi.org/10.1093/cdn/nzaa066_022.
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Abstract Objectives Protease supplementation has been reported to decrease inflammation and indices of muscle damage while increasing functional recovery following strenuous resistance exercise compared to a placebo. While various mechanisms have been proposed, the effects of protease supplementation on the resistance exercise induced anabolic signaling response has not been reported in the literature. To examine the effects of a protease enzyme blend added to whey protein on post-resistance exercise intramuscular anabolic signaling. Methods Ten resistance-trained males (24.4 ± 4.1yrs, 1.79 ± 0.86 m, 92.6 ± 10.4 kg) were enrolled in this double-blind, cross-over, placebo controlled study and engaged in three separate bouts of resistance exercise. Each participant completed 4 sets of leg presses and leg extensions for 8–10 repetitions at 75% of their 1-repetition maximum with 90 seconds of rest between each set. Immediately following the resistance exercise protocol, participants consumed either 250 mg of a protease enzyme blend + 26 g of whey protein (PW), 26 g whey alone (W), or non-caloric control (CON) in a counterbalanced fashion. Skeletal muscle microbiopsies were obtained from the vastus lateralis pre-exercise (PRE), 1-hour (1H), and 3-hours (3H) post-exercise. Multiplex signaling assay kits were used to quantify the phosphorylation status of proteins specific to the mTOR (AKT, mTOR, p70S6K) and MAPK (ERK1/2, JNK, p38) signaling pathways using the MAGPIX® (Luminex, Austin, TX, USA). A 2-way repeated measures analysis of variance (ANOVA) was used to identify differences between treatments over time. Results A main effect for time (p < 0.05) revealed phosphorylation of AKT was decreased at 1H (p < 0.001), mTOR was increased at 1H (P = 0.025) and 3H (P = 0.009) post-exercise, while p70S6K remained unchanged (P > 0.05) from PRE. A main effect for time (p < 0.05) was found with increased phosphorylation at 1H for JNK (P = 0.001), and decreased phosphorylation at 3H for ERK 1/2 (P = 0.022) with respect to baseline. Additionally, there were no differences in any mTOR nor MAPK signaling proteins observed between treatments. Conclusions These data suggest that acute protease supplementation may not alter mTOR or MAPK signaling in skeletal muscle following acute resistance exercise. Funding Sources Deerland Enzymes, Kennesaw, GA.
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Turner, MD, ME Rennison, SE Handel, CJ Wilde, and RD Burgoyne. "Proteins are secreted by both constitutive and regulated secretory pathways in lactating mouse mammary epithelial cells." Journal of Cell Biology 117, no. 2 (April 15, 1992): 269–78. http://dx.doi.org/10.1083/jcb.117.2.269.
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Lactating mammary epithelial cells secrete high levels of caseins and other milk proteins. The extent to which protein secretion from these cells occurs in a regulated fashion was examined in experiments on secretory acini isolated from the mammary glands of lactating mice at 10 d postpartum. Protein synthesis and secretion were assayed by following the incorporation or release, respectively, of [35S]methionine-labeled TCA-precipitable protein. The isolated cells incorporated [35S]methionine into protein linearly for at least 5 h with no discernible lag period. In contrast, protein secretion was only detectable after a lag of approximately 1 h, consistent with exocytotic secretion of proteins immediately after passage through the secretory pathway and package into secretory vesicles. The extent of protein secretion was unaffected by the phorbol ester PMA, 8-bromo-cAMP, or 8-bromo-cGMP but was doubled by the Ca2+ ionophore ionomycin. In a pulse-label protocol in which proteins were prelabeled for 1 h before a chase period, constitutive secretion was unaffected by depletion of cytosolic Ca2+ but ionomycin was found to give a twofold stimulation of the secretion of presynthesized protein in a Ca(2+)-dependent manner. Ionomycin was still able to stimulate protein secretion after constitutive secretion had terminated. These results suggest that lactating mammary cells possess both a Ca(2+)-independent constitutive pathway and a Ca(2+)-activated regulatory pathway for protein secretion. The same proteins were secreted by both pathways. No ultrastructural evidence for apocrine secretion was seen in response to ionomycin and so it appears that regulated casein release involves exocytosis. Ionomycin was unlikely to be acting by disassembling the cortical actin network since cytochalasin D did not mimic its effects on secretion. The regulated pathway may be controlled by Ca2+ acting at a late step such as exocytotic membrane fusion.
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Blakemore, Stephen J., Peter K. Rickhuss, Peter W. Watt, Michael J. Rennie, and Harinder S. Hundal. "Effects of Limb Immobilization on Cytochrome C Oxidase Activity and GLUT4 and GLUT5 Protein Expression in Human Skeletal Muscle." Clinical Science 91, no. 5 (November 1, 1996): 591–99. http://dx.doi.org/10.1042/cs0910591.
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1. We investigated the effects of limb immobilization (for 1 or 6 weeks) in a long leg cast after a closed tibial fracture (n = 11). Biopsies of vastus lateralis were taken on admission and after either 1 week (n = 5) or 6 weeks (n = 6) and analysed for muscle fibre type characteristics, cytochrome c oxidase activity and the abundance of GLUT4 and GLUT5 hexose transporters. 2. After 1 week of immobilization there was a significant decrease (8%) in the cross-sectional area of type I, but not type II, muscle fibres and in the protein—DNA ratio (16%) compared with the initial biopsy. Six weeks of immobilization led to further muscle atrophy compared with the initial biopsy and a further reduction in the cross-sectional area of both type I and II fibres (29% and 36% decrease respectively) and in the protein—DNA ratio (25%). No changes were observed in the free leg after 1 week. However, at the end of the 6 week study period, the cross-sectional area of both type I and II fibres of the free leg were increased (7% and 5%) and there was significant increase in the protein—DNA ratio (14%), indicating a net increase in muscle protein content. 3. Assay for cytochrome c oxidase activity showed significant reduction after 1 (30%) or 6 weeks (36%) of immobilization, reflecting a reduced capacity for oxidative metabolism. No significant changes in activity were observed in muscle from the free leg after 1 or 6 weeks of study. 4. The concentrations of GLUT4 and GLUT5 protein were determined by Western blot analysis. Limb immobilization induced a marked (50%) reduction in muscle GLUT4 protein concentration after 1 week that persisted for 6 weeks. A transient but significant increase (approximately twofold) in GLUT4 concentration was detected in muscle from the free leg after 1 week, but this returned to preimmobilization values at 6 weeks. Unlike GLUT4, no significant changes in the abundance of the GLUT5 protein were detected in either the immobilized or free leg at the end of the 1 or 6 week periods. 5. The present findings indicate that disuse rapidly induces a selective loss of activity and abundance of some non-myofibrillar proteins in humans. The decrease in GLUT4 protein abundance and cytochrome c oxidase activity during muscle disuse is consistent with a decreased capacity for glucose uptake and with a lower oxidative potential of inactive muscle. The lack of any major changes in GLUT5 protein abundance during limb immobilization indicates that the expression of some non-myofibrillar proteins is differentially regulated in response to muscle disuse.
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Svanberg, E., A. C. Moller-Loswick, D. E. Matthews, U. Korner, M. Andersson, and K. Lundholm. "Effects of amino acids on synthesis and degradation of skeletal muscle proteins in humans." American Journal of Physiology-Endocrinology and Metabolism 271, no. 4 (October 1, 1996): E718—E724. http://dx.doi.org/10.1152/ajpendo.1996.271.4.e718.
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Synthesis and degradation of globular and myofibrillar proteins across arm and leg muscles were examined during stepwise increased intravenous infusion of amino acids (0.1, 0.2, 0.4, and 0.8 g N.kg-1.day-1) to healthy volunteers. Protein dynamics were measured by a primed constant infusion of L-[ring-2H5]phenylalanine and the release of 3-methylhistidine from skeletal muscles. Arterial concentrations and flux of glucose, lactate, and free fatty acids were unchanged despite increasing concentrations of plasma amino acids from 2.6 to 5.7 mM. Plasma insulin, insulin-like growth factor I (IGF-I), and plasma concentrations of IGF-I-binding proteins-1 and -3 remained at fasting levels throughout the investigation. Amino acid infusion caused a significant uptake of the majority of amino acids across arm and leg tissues, except tyrosine, tryptophan, and cysteine, probably due to low concentrations of these amino acids in the formulation. The balance of globular proteins improved significantly (P < 0.01) due to stimulation of synthesis and attenuation of degradation across arm and leg tissues, despite insignificant uptake of tyrosine, tryptophan, and cysteine. Degradation of myofibrillar proteins was uninfluenced by provision of amino acids. The results demonstrate that neither insulin nor circulating IGF-I explained improved protein balance in skeletal muscles after elevation of plasma amino acids. Rather, some amino acids in themselves trigger cellular reactions that initiate peptide formation. Limited availability of some extracellular amino acids was overcome by increased reutilization of the intracellular amino acid.
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De Bruyne, Katrien, Ulrich Schillinger, Lily Caroline, Benjamin Boehringer, Ilse Cleenwerck, Marc Vancanneyt, Luc De Vuyst, Charles M. A. P. Franz, and Peter Vandamme. "Leuconostoc holzapfelii sp. nov., isolated from Ethiopian coffee fermentation and assessment of sequence analysis of housekeeping genes for delineation of Leuconostoc species." International Journal of Systematic and Evolutionary Microbiology 57, no. 12 (December 1, 2007): 2952–59. http://dx.doi.org/10.1099/ijs.0.65292-0.
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A Gram-positive, ovoid lactic acid bacterium, strain LMG 23990T, was isolated from Ethiopian coffee fermentation. 16S rRNA gene sequence analysis indicated that the novel strain belongs to the genus Leuconostoc, with Leuconostoc citreum and Leuconostoc lactis as the closest neighbours (99.6 and 99.0 % 16S rRNA gene sequence similarity, respectively). Genotypic fingerprinting by fluorescent amplified fragment length polymorphism, whole-cell protein electrophoresis, DNA–DNA hybridizations, comparative sequence analysis of pheS, rpoA, atpA, and physiological and biochemical tests allowed us to differentiate strain LMG 23990T from all established Leuconostoc species. Strain LMG 23990T (=CCUG 54536T) therefore represents a novel species, for which the name Leuconostoc holzapfelii sp. nov. is proposed.
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Staub, Henrique Luiz, Gary Lewis Norman, Tiffany Crowther, Viviane Roseli da Cunha, Aline Polanczyk, Jussara Maria Bohn, Jefferson Gomes Fernandes, Wiliam Habib Chahade, and Carlos Alberto von Mühlen. "Antibodies to the atherosclerotic plaque components beta2-glycoprotein I and heat-shock proteins as risk factors for acute cerebral ischemia." Arquivos de Neuro-Psiquiatria 61, no. 3B (September 2003): 757–63. http://dx.doi.org/10.1590/s0004-282x2003000500010.
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One third of cases of cerebral ischemia have no clear etiology. A humoral response to the atherosclerotic plaques components beta2-glycoprotein l (beta2-gpl) and heat-shock proteins (Hsp) might be involved in the pathogenesis of stroke. This case-control study includes a complete profile of anti-beta2-gpl antibodies and testing of IgG antibodies to the 60/65 kilodaltons (kDa) Hsp in stroke patients. Ninety-three patients with acute ischemic stroke and 93 controls were evaluated for age, sex, race, hypertension, smoking, previous cardiopathy, diabetes mellitus, hypercholesterolemia and previous history of cerebral ischemia. lgG/lgM/lgA anticardiolipin (aCL) and anti-beta2-gpl antibodies, as well as lgG antibodies to human 60 kDa Hsp and to Mycobacterium bovis 65 kDa Hsp, were detected by immunoassay. Adjusted odds ratios (OR) were calculated by logistic regression. The adjusted OR for IgA anti-beta2-gpl antibodies was 4.6 (90%Cl 1.5 to 14.3; p = 0.025). The non-adjusted OR for IgG antibodies to Hsp 60 was 26.1. The adjusted OR for IgG antibodies to Hsp 65 was 3.2 (90%Cl 1.2 to 8.3; p = 0.044). The adjusted OR for lgG to any Hsp (60 or 65) was 4.8 (90%Cl 1.9 to 12.1; p = 0.006). This study demonstrates that elevated IgA anti-beta2-gpl and lgG anti-Hsp 60/65 antibodies are associated with increased risk of ischemic stroke. The association occurred independently of other risk factors. This humoral response might link autoimmunity, thrombophilia and atherosclerosis in stroke patients.
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Silver, G., and J. D. Etlinger. "Regulation of myofibrillar accumulation in chick muscle cultures: evidence for the involvement of calcium and lysosomes in non-uniform turnover of contractile proteins." Journal of Cell Biology 101, no. 6 (December 1, 1985): 2383–91. http://dx.doi.org/10.1083/jcb.101.6.2383.
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The effect of calcium on myofibrillar turnover in primary chick leg skeletal muscle cultures was examined. Addition of the calcium ionophore A23187 at subcontraction threshold levels (0.38 microM) increased significantly rates of efflux of preloaded 45Ca+2 but had no effect on total protein accumulation. However, A23187 as well as ionomycin caused decreased accumulation of the myofibrillar proteins, myosin heavy chain (MHC), myosin light chain 1f (LC1f), 2f (LC2f), alpha-actin (Ac), and tropomyosin (TM). A23187 increased the degradation rate of LC1f, LC2f, and TM after 24 h. In contrast, the calcium ionophore caused decreased degradation of Ac and troponin-C and had no effect on the degradation of MHC, troponin-T, troponin-I, or alpha, beta-desmin (Dm). In addition, A23187 did not alter degradation of total myotube protein. The ionophore had little or no effect on the synthesis of total myotube proteins, but caused a marked decrease in the synthesis of MHC, LC1f, LC2f, Ac, TM, and Dm after 48 h. The mechanisms involved in calcium-stimulated degradation of the myofibrillar proteins were also investigated. Increased proteolysis appeared to involve a lysosomal pathway, since the effect of the Ca++ ionophore could be blocked by the protease inhibitor leupeptin and the lysosomotropic agents methylamine and chloroquine. The effects of A23187 occur in the presence of serum, a condition in which no lysosomal component of overall protein degradation is detected. The differential effect of A23187 on the degradative rates of the myofibrillar proteins suggests a dynamic structure for the contractile apparatus.
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Zapf, Thomas, Christian Zafiu, Christoph Zaba, Cherng-Wen Darren Tan, Walter Hunziker, and Eva-Kathrin Sinner. "Nanoscopic leg irons: harvesting of polymer-stabilized membrane proteins with antibody-functionalized silica nanoparticles." Biomaterials Science 3, no. 9 (2015): 1279–83. http://dx.doi.org/10.1039/c5bm00133a.
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Naser, Sabri M., Marc Vancanneyt, Cindy Snauwaert, Gino Vrancken, Bart Hoste, Luc De Vuyst, and Jean Swings. "Reclassification of Lactobacillus amylophilus LMG 11400 and NRRL B-4435 as Lactobacillus amylotrophicus sp. nov." International Journal of Systematic and Evolutionary Microbiology 56, no. 11 (November 1, 2006): 2523–27. http://dx.doi.org/10.1099/ijs.0.64463-0.
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The taxonomic position of six Lactobacillus amylophilus strains isolated from swine waste-corn fermentations was reinvestigated. All strains were included in a multilocus sequence analysis (MLSA) study for species identification of Lactobacillus using the genes encoding the phenylalanyl-tRNA synthase alpha subunit (pheS) and RNA polymerase alpha subunit (rpoA). Partial pheS and rpoA gene sequences showed that strains LMG 11400 and NRRL B-4435 represent a separate lineage that is distantly related to the type strain of L. amylophilus, LMG 6900T, and to three other strains of the species. The MLSA data showed that the two strains LMG 11400 and NRRL B-4435 constituted a distinct cluster, sharing 100 % pheS and rpoA gene sequence similarity. The other reference strains clustered together with the type strain of L. amylophilus, LMG 6900T, and were clearly differentiated from strains LMG 11400 and NRRL B-4435 (80 and 89 % pheS and rpoA gene sequence similarity, respectively). The 16S rRNA gene sequences of the latter two strains are 100 % identical, with the nearest phylogenetic neighbour L. amylophilus LMG 6900T showing only 97.2 % 16S rRNA gene sequence similarity. Further polyphasic taxonomic study based on whole-cell protein fingerprinting, DNA–DNA hybridization and biochemical features demonstrated that the two strains represent a single, novel Lactobacillus species, for which the name Lactobacillus amylotrophicus sp. nov. is proposed. The type strain is LMG 11400T (=NRRL B-4436T=DSM 20534T).
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Wübbeler, Jan Hendrik, Tina Lütke-Eversloh, Stefanie Van Trappen, Peter Vandamme, and Alexander Steinbüchel. "Tetrathiobacter mimigardefordensis sp. nov., isolated from compost, a betaproteobacterium capable of utilizing the organic disulfide 3,3′-dithiodipropionic acid." International Journal of Systematic and Evolutionary Microbiology 56, no. 6 (June 1, 2006): 1305–10. http://dx.doi.org/10.1099/ijs.0.64126-0.
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In this study, a novel betaproteobacterium, strain DPN7T, was isolated under mesophilic conditions from compost because of its capacity to utilize the organic disulfide 3,3′-dithiodipropionic acid. Analysis of the 16S rRNA gene sequence of strain DPN7T revealed 98.5 % similarity to that of Tetrathiobacter kashmirensis LMG 22695T. Values for sequence similarity to members of the genera Alcaligenes, Castellaniella and Taylorella, the nearest neighbours of the genus Tetrathiobacter, were about 95 % or less. The DNA G+C content of strain DPN7T was 55.1 mol%. The level of DNA–DNA hybridization between strain DPN7T and T. kashmirensis LMG 22695T was 41 %, whereas it was much lower between strain DPN7T and Alcaligenes faecalis LMG 1229T (7 %) or Castellaniella defragrans LMG 18538T (5 %). This genotypic divergence was supported by differences in biochemical and chemotaxonomic characteristics. For this reason, and because of the differences in the protein and fatty acid profiles, strain DPN7T should be classified within a novel species of Tetrathiobacter, for which the name Tetrathiobacter mimigardefordensis sp. nov. is proposed. The type strain is strain DPN7T (=DSM 17166T=LMG 22922T).
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Yamamoto, Kosuke, and Yutaka Tamaru. "A Noncellulosomal Mannanase26E Contains a CBM59 inClostridium cellulovorans." BioMed Research International 2014 (2014): 1–7. http://dx.doi.org/10.1155/2014/438787.
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A multicomponent enzyme-complex prevents efficient degradation of the plant cell wall for biorefinery. In this study, the method of identifying glycoside hydrolases (GHs) to degrade hemicelluloses was demonstrated. The competence ofC. cellulovorans, which changes to be suitable for degradation of each carbon source, was used for the method.C. cellulovoranswas cultivated into locust bean gum (LBG) that is composed of galactomannan. The proteins produced byC. cellulovoranswere separated into either fractions binding to crystalline cellulose or not. Proteins obtained from each fraction were further separated by SDS-PAGE and were stained with Coomassie Brilliant Blue and were detected for mannanase activity. The proteins having the enzymatic activity for LBG were cut out and were identified by mass spectrometry. As a result, four protein bands were classified into glycosyl hydrolase family 26 (GH26) mannanases. One of the identified mannanases, Man26E, contains a carbohydrate-binding module (CBM) family 59, which binds to xylan, mannan, and Avicel. Although mannose and galactose are the same as a hexose, the expression patterns of the proteins fromC. cellulovoranswere quite different. More interestingly, zymogram for mannanase activity showed that Man26E was detected in only LBG medium.
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Caballero, L., L. M. Martín, and J. B. Alvarez. "Relationships between the HMW- and LMW-glutenin subunits and SDS-sedimentation volume in Spanish hulled wheat lines." Czech Journal of Genetics and Plant Breeding 44, No. 3 (November 4, 2008): 114–17. http://dx.doi.org/10.17221/8/2008-cjgpb.
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Emmer and spelt are two hulled wheats that were widely grown in Spain until the latter 1960s. Twenty-nine emmer and twenty-six spelt lines obtained from Spanish accessions of these hulled wheats were analysed for quality traits and endosperm storage protein composition. The results showed a wide range of variability in these traits. Likewise, a certain association between some alleles of these proteins and the SDS-sedimentation volume has been detected.
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Spellerberg, Barbara, Eva Rozdzinski, Simone Martin, Josephine Weber-Heynemann, Norbert Schnitzler, Rudolf Lütticken, and Andreas Podbielski. "Lmb, a Protein with Similarities to the LraI Adhesin Family, Mediates Attachment of Streptococcus agalactiae to Human Laminin." Infection and Immunity 67, no. 2 (February 1, 1999): 871–78. http://dx.doi.org/10.1128/iai.67.2.871-878.1999.
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ABSTRACT Streptococcus agalactiae is a leading cause of neonatal sepsis and meningitis. Adherence to extracellular matrix proteins is considered an important factor in the pathogenesis of infection, but the genetic determinants of this process remain largely unknown. We identified and sequenced a gene which codes for a putative lipoprotein that exhibits significant homology to the streptococcal LraI protein family. Mutants of this locus were demonstrated to have substantially reduced adherence to immobilized human laminin. The nucleotide sequence of the gene was subsequently designated lmb (laminin binding) and shown to be present in all of the common serotypes of S. agalactiae. To determine the role of Lmb in the adhesion of S. agalactiaewild-type strains to laminin, a recombinant Lmb protein harboring six consecutive histidine residues at the C terminus was cloned, expressed, and purified from Escherichia coli. Preincubation of immobilized laminin with recombinant Lmb significantly reduced adherence of the wild-type strain O90R to laminin. These results indicate that Lmb mediates the attachment of S. agalactiae to human laminin, which may be essential for the bacterial colonization of damaged epithelium and translocation of bacteria into the bloodstream.
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Tipton, Kevin D., Tabatha A. Elliott, Melanie G. Cree, Asle A. Aarsland, Arthur P. Sanford, and Robert R. Wolfe. "Stimulation of net muscle protein synthesis by whey protein ingestion before and after exercise." American Journal of Physiology-Endocrinology and Metabolism 292, no. 1 (January 2007): E71—E76. http://dx.doi.org/10.1152/ajpendo.00166.2006.
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Timing of nutrient ingestion has been demonstrated to influence the anabolic response of muscle following exercise. Previously, we demonstrated that net amino acid uptake was greater when free essential amino acids plus carbohydrates were ingested before resistance exercise rather than following exercise. However, it is unclear if ingestion of whole proteins before exercise would stimulate a superior response compared with following exercise. This study was designed to examine the response of muscle protein balance to ingestion of whey proteins both before and following resistance exercise. Healthy volunteers were randomly assigned to one of two groups. A solution of whey proteins was consumed either immediately before exercise (PRE; n = 8) or immediately following exercise (POST; n = 9). Each subject performed 10 sets of 8 repetitions of leg extension exercise. Phenylalanine concentrations were measured in femoral arteriovenous samples to determine balance across the leg. Arterial amino acid concentrations were elevated by ∼50%, and net amino acid balance switched from negative to positive following ingestion of proteins at either time. Amino acid uptake was not significantly different between PRE and POST when calculated from the beginning of exercise (67 ± 22 and 27 ± 10 for PRE and POST, respectively) or from the ingestion of each drink (60 ± 17 and 63 ± 15 for PRE and POST, respectively). Thus the response of net muscle protein balance to timing of intact protein ingestion does not respond as does that of the combination of free amino acids and carbohydrate.
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Švec, Pavel, Marc Vancanneyt, Ivo Sedláček, Sabri M. Naser, Cindy Snauwaert, Karen Lefebvre, Bart Hoste, and Jean Swings. "Enterococcus silesiacus sp. nov. and Enterococcus termitis sp. nov." International Journal of Systematic and Evolutionary Microbiology 56, no. 3 (March 1, 2006): 577–81. http://dx.doi.org/10.1099/ijs.0.63937-0.
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Three enterococci constituted two aberrant branches after numerical analysis of (GTG)5-PCR fingerprints: analogous patterns were found for two water isolates, strains W213 and W442T, and a separate position was found for an isolate from the gut of a termite, strain LMG 8895T. 16S rRNA gene sequence analysis classified all three strains in the Enterococcus faecalis species group. Further sequencing analysis of the housekeeping gene pheS (encoding the phenylalanyl-tRNA synthase α-subunit) and whole-cell-protein analysis confirmed a distinct position for the two water isolates and the termite strain, respectively. DNA–DNA hybridization experiments and distinct phenotypic features between the strains studied and representatives of the E. faecalis species group confirmed novel species status, respectively, for the two water isolates, strains W213 and W442T, and for strain LMG 8895T. The names Enterococcus silesiacus sp. nov. and Enterococcus termitis sp. nov. are proposed for the novel taxa, with W442T (=CCM 7319T=LMG 23085T) and LMG 8895T (=CCM 7300T) as the respective type strains.
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Brown, Alistair S., David F. Ackerley, and Mark J. Calcott. "High-Throughput Screening for Inhibitors of the SARS-CoV-2 Protease Using a FRET-Biosensor." Molecules 25, no. 20 (October 13, 2020): 4666. http://dx.doi.org/10.3390/molecules25204666.
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The global SARS-CoV-2 pandemic started late 2019 and currently continues unabated. The lag-time for developing vaccines means it is of paramount importance to be able to quickly develop and repurpose therapeutic drugs. Protein-based biosensors allow screening to be performed using routine molecular laboratory equipment without a need for expensive chemical reagents. Here we present a biosensor for the 3-chymotrypsin-like cysteine protease from SARS-CoV-2, comprising a FRET-capable pair of fluorescent proteins held in proximity by a protease cleavable linker. We demonstrate the utility of this biosensor for inhibitor discovery by screening 1280 compounds from the Library of Pharmaceutically Active Compounds collection. The screening identified 65 inhibitors, with the 20 most active exhibiting sub-micromolar inhibition of 3CLpro in follow-up EC50 assays. The top hits included several compounds not previously identified as 3CLpro inhibitors, in particular five members of a family of aporphine alkaloids that offer promise as new antiviral drug leads.
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Happ and Classen. "Arabinogalactan-Proteins from the Liverwort Marchantia polymorpha L., a Member of a Basal Land Plant Lineage, Are Structurally Different to Those of Angiosperms." Plants 8, no. 11 (October 29, 2019): 460. http://dx.doi.org/10.3390/plants8110460.
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The thalloid liverwort Marchantia polymorpha as a member of a basal land plant lineage has to cope with the challenge of terrestrial life. Obviously, the plant cell wall has been strongly involved in the outstanding evolutionary process of water-to-land-transition. AGPs are signaling glycoproteins of the cell wall, which seem to be ubiquitous in seed plants and might play a role in adaption to abiotic and biotic stress situations. Therefore, we investigated the cell wall composition of Marchantia polymorpha with special focus on structural characterization of arabinogalactan-proteins. The Marchantia AGP shows typical features known from seed plant AGPs like precipitation with β-glucosyl-Yariv’s reagent, a protein moiety with hydroxyproline and a carbohydrate part with 1,3,6-linked galactose and terminal arabinose residues. On the other hand, striking differences to AGPs of angiosperms are the occurrence of terminal 3-O-methyl-rhamnose and a highly branched galactan lacking appreciable amounts of 1,6-linked galactose. Binding of different AGP-antibodies (JIM13, KM1, LM2, LM6, LM14, LM26, and MAC207) to Marchantia AGP was investigated and confirmed structural differences between liverwort and angiosperm AGP, possibly due to deviating functions of these signaling molecules in the different taxonomic groups.
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Tang, Jason E., Daniel R. Moore, Gregory W. Kujbida, Mark A. Tarnopolsky, and Stuart M. Phillips. "Ingestion of whey hydrolysate, casein, or soy protein isolate: effects on mixed muscle protein synthesis at rest and following resistance exercise in young men." Journal of Applied Physiology 107, no. 3 (September 2009): 987–92. http://dx.doi.org/10.1152/japplphysiol.00076.2009.
Full textAbstract:
This study was designed to compare the acute response of mixed muscle protein synthesis (MPS) to rapidly (i.e., whey hydrolysate and soy) and slowly (i.e., micellar casein) digested proteins both at rest and after resistance exercise. Three groups of healthy young men ( n = 6 per group) performed a bout of unilateral leg resistance exercise followed by the consumption of a drink containing an equivalent content of essential amino acids (10 g) as either whey hydrolysate, micellar casein, or soy protein isolate. Mixed MPS was determined by a primed constant infusion of l-[ ring-13C6]phenylalanine. Ingestion of whey protein resulted in a larger increase in blood essential amino acid, branched-chain amino acid, and leucine concentrations than either casein or soy (P < 0.05). Mixed MPS at rest (determined in the nonexercised leg) was higher with ingestion of faster proteins (whey = 0.091 ± 0.015, soy = 0.078 ± 0.014, casein = 0.047 ± 0.008%/h); MPS after consumption of whey was ∼93% greater than casein (P < 0.01) and ∼18% greater than soy (P = 0.067). A similar result was observed after exercise (whey > soy > casein); MPS following whey consumption was ∼122% greater than casein (P < 0.01) and 31% greater than soy (P < 0.05). MPS was also greater with soy consumption at rest (64%) and following resistance exercise (69%) compared with casein (both P < 0.01). We conclude that the feeding-induced simulation of MPS in young men is greater after whey hydrolysate or soy protein consumption than casein both at rest and after resistance exercise; moreover, despite both being fast proteins, whey hydrolysate stimulated MPS to a greater degree than soy after resistance exercise. These differences may be related to how quickly the proteins are digested (i.e., fast vs. slow) or possibly to small differences in leucine content of each protein.
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Gebicki, J. M., J. Du, J. Collins, and H. Tweeddale. "Peroxidation of proteins and lipids in suspensions of liposomes, in blood serum, and in mouse myeloma cells." Acta Biochimica Polonica 47, no. 4 (December 31, 2000): 901–11. http://dx.doi.org/10.18388/abp.2000_3945.
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There is growing evidence that proteins are early targets of reactive oxygen species, and that the altered proteins can in turn damage other biomolecules. In this study, we measured the effects of proteins on the oxidation of liposome phospholipid membranes, and the formation of protein hydroperoxides in serum and in cultured cells exposed to radiation-generated hydroxyl free radicals. Lysozyme, which did not affect liposome stability, gave 50% protection when present at 0.3 mg/ml, and virtually completely prevented lipid oxidation at 10 mg/ml. When human blood serum was irradiated, lipids were oxidized only after the destruction of ascorbate. In contrast, peroxidation of proteins proceeded immediately. Protein hydroperoxides were also generated without a lag period in hybrid mouse myeloma cells, while at the same time no lipid peroxides formed. These results are consistent with the theory that, under physiological conditions, lipid membranes are likely to be effectively protected from randomly-generated hydroxyl radicals by proteins, and that protein peroxyl radicals and hydroperoxides may constitute an important hazard to biological systems under oxidative stress.
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Gordon, A. S., L. D. Howell, and V. Harwood. "Responses of diverse heterotrophic bacteria to elevated copper concentrations." Canadian Journal of Microbiology 40, no. 5 (May 1, 1994): 408–11. http://dx.doi.org/10.1139/m94-067.
Full textAbstract:
The influence of copper on the growth of Escherichia coli, Pseudomonas aeruginosa, Bacillus cereus, Bacillus subtilis, Vibrio parahaemolyticus, Vibrio alginolyticus (three strains), and an unidentified Vibrio sp. was examined in batch cultures. The effects of copper at micromolar concentrations varied from undetectable to complete growth inhibition. Each strain was able to recover from a growth lag observed after copper addition at a characteristic concentration. Copper concentrations that allowed recovery ranged from 25 to 150 μM. Extracellular proteins in the medium of cultures that had recovered from copper stress were compared with those from control cultures. Protein profiles were analyzed for the presence of proteins similar to extracellular copper-binding proteins (CuBP) previously reported in V. alginolyticus. CuBP-like proteins were found in each Vibrio sp. examined. A protein of similar molecular mass was also detected in copper-stressed cultures of P. aeruginosa and not in control cultures. Escherichia coli and Bacillus spp. did not produce CuBP-like proteins. The data show that CuBP-like proteins are not produced by all bacteria in response to copper stress and indicate that such proteins are common in marine Vibrio spp.Key words: copper toxicity, heterotrophic bacteria, extracellular protein.
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Franz, Charles M. A. P., Marc Vancanneyt, Katrien Vandemeulebroecke, Marjan De Wachter, Ilse Cleenwerck, Bart Hoste, Ulrich Schillinger, Wilhelm H. Holzapfel, and Jean Swings. "Pediococcus stilesii sp. nov., isolated from maize grains." International Journal of Systematic and Evolutionary Microbiology 56, no. 2 (February 1, 2006): 329–33. http://dx.doi.org/10.1099/ijs.0.63944-0.
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A Gram-positive, coccus-shaped, lactic acid bacterium, strain LMG 23082T, was isolated from steeped maize grains. The organism is homofermentative and produces d- and l-lactic acid from glucose. 16S rRNA gene sequence analysis revealed that the organism belongs to the genus Pediococcus, with Pediococcus pentosaceus and Pediococcus acidilactici as nearest neighbours. Genotypic fingerprinting, whole-cell protein electrophoresis, DNA–DNA hybridizations and physiological and biochemical tests allowed differentiation of strain LMG 23082T from other established Pediococcus species. A remarkable feature was that, unlike other pediococci, this bacterium was capable of growth at pH 9·0. The strain studied represents a novel species for which the name Pediococcus stilesii sp. nov. is proposed with the type strain LMG 23082T (=BFE 1652T=FAIR-E 180T=CCUG 51290T), the only currently known isolate of the species.
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Hirokawa, N. "270K microtubule-associated protein cross-reacting with anti-MAP2 IgG in the crayfish peripheral nerve axon." Journal of Cell Biology 103, no. 1 (July 1, 1986): 33–39. http://dx.doi.org/10.1083/jcb.103.1.33.
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MAPs (microtubule-associated proteins) were isolated from crayfish walking leg nerves. A major MAP was identified as a high molecular weight protein (270K). This protein co-migrated with mammalian MAP2, stimulated the polymerization of rat brain tubulin into microtubules, and was heat resistant. Rotary shadowing revealed that the 270K MAP is a long thin flexible structure. It formed cross-bridges of fine strands, linking microtubules with each other in vitro. These strands resemble the cross-bridges between microtubules observed in the crayfish axon permeabilized with saponin and quick-frozen, deep-etched. Antibodies against mammalian MAP2 cross-reacted with this crayfish MAP and stained the axoplasm of the walking leg nerves. Thus MAPs, especially the 270K MAP, appear to be a major component of the cross-linking strands between microtubules observed in the crayfish axon.
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Marnef, Aline, Dominique Weil, and Nancy Standart. "RNA-related nuclear functions of human Pat1b, the P-body mRNA decay factor." Molecular Biology of the Cell 23, no. 1 (January 2012): 213–24. http://dx.doi.org/10.1091/mbc.e11-05-0415.
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The evolutionarily conserved Pat1 proteins are P-body components recently shown to play important roles in cytoplasmic gene expression control. Using human cell lines, we demonstrate that human Pat1b is a shuttling protein whose nuclear export is mediated via a consensus NES sequence and Crm1, as evidenced by leptomycin B (LMB) treatment. However, not all P-body components are nucleocytoplasmic proteins; rck/p54, Dcp1a, Edc3, Ge-1, and Xrn1 are insensitive to LMB and remain cytoplasmic in its presence. Nuclear Pat1b localizes to PML–associated foci and SC35-containing splicing speckles in a transcription-dependent manner, whereas in the absence of RNA synthesis, Pat1b redistributes to crescent-shaped nucleolar caps. Furthermore, inhibition of splicing by spliceostatin A leads to the reorganization of SC35 speckles, which is closely mirrored by Pat1b, indicating that it may also be involved in splicing processes. Of interest, Pat1b retention in these three nuclear compartments is mediated via distinct regions of the protein. Examination of the nuclear distribution of 4E-T(ransporter), an additional P-body nucleocytoplasmic protein, revealed that 4E-T colocalizes with Pat1b in PML-associated foci but not in nucleolar caps. Taken together, our findings strongly suggest that Pat1b participates in several RNA-related nuclear processes in addition to its multiple regulatory roles in the cytoplasm.
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Ahmed, MS, M. Kamruzzaman, MM Rana, Z. Akond, and MNH Mollah. "In silico analyses of human collagen protein function prediction." Journal of Bio-Science 24 (July 18, 2018): 55–65. http://dx.doi.org/10.3329/jbs.v24i0.37487.
Full textAbstract:
Collagen is the extracellular matrix protein in the several connective tissues in the human body. It is an important component for mediating cell-cell interactions and pathological conditions in human body. In this study we perform the analysis of physiochemical properties and investigate the functional characteristics of human collagen proteins. Also investigate the functional protein groups by the statistical analysis. The collagen protein family consisting 28 members in human which are involving in the complex structure of protein. The protein function, protein sequence properties, domain composition, phylogenetic and protein-protein interaction (PPI) networks analysis of human collagen alpha-1 protein sequences are implemented by the online bioinformatics tools which are currently available. Based on the PCA analysis amino acid composition, features of collagen protein sequences are divided into two supreme influential functional groups such as collagen 12, 14, 20 formed one group and the rest of others formed another group. The protein-protein interaction network study using STRING showed that top interacting score of functional group proteins 0.952, 0.939 and 0.929. The most common functional domain of collagen proteins are VWC, C4, LamG, VWA, KU, C1Q, TSPN and FN3. Physicochemical, functional and phylogenetic classification can give extensive information of protein’s structure and function. The depiction of alpha-1 chains of collagen protein family in human collagen 12, 14 and 20 as a prospective protein cluster. These three proteins are possess, low glycine and proline, very high aliphatic index and a close evolutionary relation in the human skin.J. bio-sci. 24: 55-65, 2016
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GIESEG, Steven, Sean DUGGAN, and Janusz M. GEBICKI. "Peroxidation of proteins before lipids in U937 cells exposed to peroxyl radicals." Biochemical Journal 350, no. 1 (August 9, 2000): 215–18. http://dx.doi.org/10.1042/bj3500215.
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This study provides the first report of the formation of protein hydroperoxides in cells attacked by reactive oxygen species. U937 cells exposed to peroxyl radicals generated by the thermal decomposition of a water-soluble azo compound gradually accumulated hydroperoxide (-OOH) groups. In an incubation for 22h, 1.2mM peroxyl radicals was generated and each cell acquired 1.5×108 -OOH groups. These groups were located on the cell proteins; no lipid peroxidation was detected. The extent of protein peroxidation was proportional to the rate of generation of the peroxyl radicals. There was no lag period before the onset of peroxidation, indicating that cell antioxidants could not protect the proteins. The half-life of protein hydroperoxides in cell suspensions was approx. 4h at 37°C. Our results suggest that protein hydroperoxides might have a significant role as intermediates in the development of biological damage initiated by reactive oxygen species.
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Sakakibara, Keiichi, Naoya Saito, Takuji Sato, Atsushi Suzuki, Yoko Hasegawa, Jonathan M. Friedman, Donald W. Kufe, Daniel D. VonHoff, Tadahiko Iwami, and Takumi Kawabe. "CBS9106 is a novel reversible oral CRM1 inhibitor with CRM1 degrading activity." Blood 118, no. 14 (October 6, 2011): 3922–31. http://dx.doi.org/10.1182/blood-2011-01-333138.
Full textAbstract:
Abstract CRM1 plays an important role in the nuclear export of cargo proteins bearing nuclear exporting signal sequences. Leptomycin B (LMB), a well-known CRM1 inhibitor, possesses strong antitumor properties. However, its toxicity prevents it from being clinically useful. In this study, we demonstrate that a novel compound, CBS9106, inhibits CRM1-dependent nuclear export, causing arrest of the cell cycle and inducing apoptosis in a time- and dose-dependent manner for a broad spectrum of cancer cells, including multiple myeloma cells. CBS9106 reduces CRM1 protein levels significantly without affecting CRM1 mRNA expression. This effect could be reversed by adding bortezomib or LMB. Moreover, CBS9106-biotin allows capture of CRM1 protein by streptavidin beads in a competitive manner with LMB and vice versa. Mass spectrometric analysis shows that CBS9106 reacts with a synthetic CRM1 peptide that contains Cys528 but not with a Cys528 mutant peptide. Oral administration of CBS9106 significantly suppresses tumor growth and prolongs survival in mice bearing tumor xenograft without a significant loss in body weight. A reduced level of CRM1 protein is also observed in tumor xenografts isolated from mice treated with CBS9106. Taken together, these results indicate that CBS9106 is a novel reversible CRM1 inhibitor and a promising clinical candidate.
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D’Abrosca, Gianluca, Antonella Paladino, Emilio Cuoco, Rosangela Marasco, Severina Pacifico, Simona Piccolella, Valeria Vastano, et al. "Structural Characterization of the Lactobacillus Plantarum FlmC Protein Involved in Biofilm Formation." Molecules 23, no. 9 (September 4, 2018): 2252. http://dx.doi.org/10.3390/molecules23092252.
Full textAbstract:
Lactobacillus plantarum is one of the most predominant species in the human gut microbiota of healthy individuals. We have previously characterized some probiotic features of L. plantarum LM3, as the high resistance to different stress, the binding ability toward some extracellular matrix proteins and plasminogen and the immunomodulatory role of the surface expressed adhesin EnoA1. We have also identified the flmA, flmB and flmC genes, coding for putative proteins named FlmA, FlmB and FlmC, whose null mutations partially impaired biofilm development; the L. plantarum LM3–6 strain, carrying a deletion in flmC, showed a high rate of autolysis, supporting the hypothesis that FlmC might be involved in cell wall integrity. Here, we report the in-silico characterization of ΔTM-FlmC, a portion of the FlmC protein. The protein has been also expressed, purified and characterized by means of CD spectroscopy, ICP-mass and UHPLC-HRMS. The obtained experimental data validated the predicted model unveiling also the presence of a bound lipid molecule and of a Mg(II) ion. Overall, we provide strong evidences that ΔTM-FlmC belongs to the LytR-CpsA-Psr (LCP) family of domains and is involved in cell envelope biogenesis.
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Aspland, S. E., and R. A. White. "Nucleocytoplasmic localisation of extradenticle protein is spatially regulated throughout development in Drosophila." Development 124, no. 3 (February 1, 1997): 741–47. http://dx.doi.org/10.1242/dev.124.3.741.
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The extradenticle protein is a homeodomain transcription factor which has an important role regulating the DNA-binding specificity of homeotic selector proteins. We have made a monoclonal antibody against extradenticle and have studied the expression of the protein in the embryo and in imaginal discs. We find that extradenticle is initially uniformly distributed as expected but strikingly is excluded from nuclei until gastrulation. During the extended germ band stage the protein remains predominantly cytoplasmic and does not accumulate in nuclei until germ band retraction. Nuclear accumulation occurs in a highly spatially regulated pattern. In the imaginal discs the nuclear accumulation of extradenticle is also spatially regulated and, in the wing and leg discs, distal regions exhibit cytoplasmic extradenticle whereas proximally the protein is nuclear. We suggest that this regulation of the sub-cellular localisation of extradenticle is important for the interactions between extradenticle and the homeotic selector proteins and that extradenticle is not simply a ubiquitously available cofactor.
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Tang, Jason E., Joshua J. Manolakos, Greg W. Kujbida, Paul J. Lysecki, Daniel R. Moore, and Stuart M. Phillips. "Minimal whey protein with carbohydrate stimulates muscle protein synthesis following resistance exercise in trained young men." Applied Physiology, Nutrition, and Metabolism 32, no. 6 (December 2007): 1132–38. http://dx.doi.org/10.1139/h07-076.
Full textAbstract:
Whey protein is a supplemental protein source often used by athletes, particularly those aiming to gain muscle mass; however, direct evidence for its efficacy in stimulating muscle protein synthesis (MPS) is lacking. We aimed to determine the impact of consuming whey protein on skeletal muscle protein turnover in the post-exercise period. Eight healthy resistance-trained young men (age = 21 ± 1 .0 years; BMI = 26.8 ± 0.9 kg/m2 (means ± SE)) participated in a double-blind randomized crossover trial in which they performed a unilateral leg resistance exercise workout (EX: 4 sets of knee extensions and 4 sets of leg press; 8–10 repetitions/set; 80% of maximal), such that one leg was not exercised and acted as a rested (RE) comparator. After exercise, subjects consumed either an isoenergetic whey protein plus carbohydrate beverage (WHEY: 10 g protein and 21 g fructose) or a carbohydrate-only beverage (CHO: 21 g fructose and 10 g maltodextran). Subjects received pulse-tracer injections of l-[ring-2H5]phenylalanine and l-[15N]phenylalanine to measure MPS. Exercise stimulated a rise in MPS in the WHEY-EX and CHO-EX legs, which were greater than MPS in the WHEY-RE leg and the CHO-RE leg (all p < 0.05), respectively. The rate of MPS in the WHEY-EX leg was greater than in the CHO-EX leg (p < 0.001). We conclude that a small dose (10 g) of whey protein with carbohydrate (21 g) can stimulate a rise in MPS after resistance exercise in trained young men that would be supportive of a positive net protein balance, which, over time, would lead to hypertrophy.