Log in

Relevant bibliographies by topics / Metalloproteasi

Contents

Journal articles
Dissertations / Theses
Books
Book chapters
Conference papers
Reports

Academic literature on the topic 'Metalloproteasi'

Author: Grafiati

Published: 9 March 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Metalloproteasi.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Metalloproteasi"

1

Harte, James V., Samantha L. Wakerlin, Andrew J. Lindsay, Justin V. McCarthy, and Caroline Coleman-Vaughan. "Metalloprotease-Dependent S2′-Activation Promotes Cell–Cell Fusion and Syncytiation of SARS-CoV-2." Viruses 14, no. 10 (September 21, 2022): 2094. http://dx.doi.org/10.3390/v14102094.

Full text

Abstract:

SARS-CoV-2 cell–cell fusion and syncytiation is an emerging pathomechanism in COVID-19, but the precise factors contributing to the process remain ill-defined. In this study, we show that metalloproteases promote SARS-CoV-2 spike protein-induced syncytiation in the absence of established serine proteases using in vitro cell–cell fusion assays. We also show that metalloproteases promote S2′-activation of the SARS-CoV-2 spike protein, and that metalloprotease inhibition significantly reduces the syncytiation of SARS-CoV-2 variants of concern. In the presence of serine proteases, however, metalloprotease inhibition does not reduce spike protein-induced syncytiation and a combination of metalloprotease and serine protease inhibition is necessitated. Moreover, we show that the spike protein induces metalloprotease-dependent ectodomain shedding of the ACE2 receptor and that ACE2 shedding contributes to spike protein-induced syncytiation. These observations suggest a benefit to the incorporation of pharmacological inhibitors of metalloproteases into treatment strategies for patients with COVID-19.

APA, Harvard, Vancouver, ISO, and other styles

2

Slapak, Etienne J., JanWillem Duitman, Cansu Tekin, Maarten F. Bijlsma, and C. Arnold Spek. "Matrix Metalloproteases in Pancreatic Ductal Adenocarcinoma: Key Drivers of Disease Progression?" Biology 9, no. 4 (April 18, 2020): 80. http://dx.doi.org/10.3390/biology9040080.

Full text

Abstract:

Pancreatic cancer is a dismal disorder that is histologically characterized by a dense fibrotic stroma around the tumor cells. As the extracellular matrix comprises the bulk of the stroma, matrix degrading proteases may play an important role in pancreatic cancer. It has been suggested that matrix metalloproteases are key drivers of both tumor growth and metastasis during pancreatic cancer progression. Based upon this notion, changes in matrix metalloprotease expression levels are often considered surrogate markers for pancreatic cancer progression and/or treatment response. Indeed, reduced matrix metalloprotease levels upon treatment (either pharmacological or due to genetic ablation) are considered as proof of the anti-tumorigenic potential of the mediator under study. In the current review, we aim to establish whether matrix metalloproteases indeed drive pancreatic cancer progression and whether decreased matrix metalloprotease levels in experimental settings are therefore indicative of treatment response. After a systematic review of the studies focusing on matrix metalloproteases in pancreatic cancer, we conclude that the available literature is not as convincing as expected and that, although individual matrix metalloproteases may contribute to pancreatic cancer growth and metastasis, this does not support the generalized notion that matrix metalloproteases drive pancreatic ductal adenocarcinoma progression.

APA, Harvard, Vancouver, ISO, and other styles

3

Beek, J., H. Nauwynck, D. Maes, and A. Van Soom. "Inhibitors of zinc-dependent metalloproteases hinder sperm passage through the cumulus oophorus during porcine fertilization in vitro." REPRODUCTION 144, no. 6 (December 2012): 687–97. http://dx.doi.org/10.1530/rep-12-0311.

Full text

Abstract:

In this study, we report for the first time on a possible contribution of metalloproteases in sperm passage through the cumulus matrix in pigs. The presence of 20 μM 1,10-phenanthroline (1,10-PHEN), inhibitor of zinc-dependent metalloproteases, strongly inhibited the degree of sperm penetration in cumulus-intact (CI), but not in cumulus-free (CF), porcine oocytes during IVF. The inhibitory effect of 1,10-PHEN was due to the chelation of metal ions as a non-chelating analog (1,7-PHEN) did not affect IVF rates. Furthermore, incubation with 1,10-PHEN did not affect sperm binding to the zona pellucida nor sperm motility, membrane integrity, or acrosomal status. These findings led to the assumption that 1,10-PHEN interacts with a sperm- or cumulus-derived metalloprotease. Metalloproteases are key players in physiological processes involving degradation or remodeling of extracellular matrix. In vivo, their proteolytic activity is regulated by tissue inhibitors of metalloproteases (TIMP1–TIMP4). We tested the effect of TIMP3 on fertilization parameters after porcine IVF. Similar to 1,10-PHEN, TIMP3 inhibited total fertilization rate of CI but not CF oocytes and did not influence sperm quality parameters. Although the inhibitory effect was stronger in CI oocytes, TIMP3 also reduced the degree of sperm penetration in CF oocytes, suggesting the involvement of a metalloprotease in a subsequent step during fertilization. In conclusion, our results indicate the involvement of TIMP3-sensitive, zinc-dependent metalloprotease activity in sperm passage through the cumulus oophorus in pigs. The results should provide the basis for further biochemical research toward the localization and identification of the metalloprotease involved.

APA, Harvard, Vancouver, ISO, and other styles

4

Ramos, O. H. P., and H. S. Selistre-de-Araujo. "Identification of metalloprotease gene families in sugarcane." Genetics and Molecular Biology 24, no. 1-4 (December 2001): 285–90. http://dx.doi.org/10.1590/s1415-47572001000100037.

Full text

Abstract:

Metalloproteases play a key role in many physiological processes in mammals such as cell migration, tissue remodeling and processing of growth factors. They have also been identified as important factors in the patho-physiology of a number of human diseases, including cancer and hypertension. Many bacterial pathogens rely on proteases in order to infect the host. Several classes of metalloproteases have been described in humans, bacteria, snake venoms and insects. However, the presence and characterization of plant metalloproteases have rarely been described in the literature. In our research, we searched the sugarcane expressed sequence tag (SUCEST) DNA library in order to identify, by homology with sequences deposited in other databases, metalloprotease gene families expressed under different conditions. Protein sequences from Arabidopsis thaliana and Glycine max were used to search the SUCEST data bank. Conserved regions corresponding to different metalloprotease domains and sequence motifs were identified in the reads to characterize each group of enzymes. At least four classes of sugarcane metalloproteases have been identified, i.e. matrix metalloproteases, zincins, inverzincins, and ATP-dependent metalloproteases. Each enzyme class was analyzed for its expression in different conditions and tissues.

APA, Harvard, Vancouver, ISO, and other styles

5

Corbett, C. R., M. N. Burtnick, C. Kooi, D. E. Woods, and P. A. Sokol. "An extracellular zinc metalloprotease gene of Burkholderia cepacia." Microbiology 149, no. 8 (August 1, 2003): 2263–71. http://dx.doi.org/10.1099/mic.0.26243-0.

Full text

Abstract:

Burkholderia cepacia produces at least one extracellular zinc metalloprotease that may be involved in virulence. A B. cepacia zinc metalloprotease gene was cloned using a Burkholderia pseudomallei zinc metalloprotease gene as a probe. The predicted amino acid sequences of these B. cepacia and a B. pseudomallei extracellular zinc metalloproteases indicate that they are similar to the thermolysin-like family of metalloproteases (M4 family of metalloendopeptidases) and they are likely to be secreted via the general secretory pathway. zmpA isogenic mutants were constructed in B. cepacia genomovar III strains Pc715j and K56-2 by insertional inactivation of the zmpA genes. The zmpA mutants produced less protease than the parent strains. The B. cepacia strain K56-2 zmpA mutant was significantly less virulent than its parent strain in a chronic respiratory infection model; however, there was no difference between the virulence of B. cepacia strain Pc715j and a Pc715j zmpA mutant. The results indicate that this extracellular zinc metalloprotease may play a greater role in virulence in some strains of B. cepacia.

APA, Harvard, Vancouver, ISO, and other styles

6

Goblirsch, Brandon R., Buenafe T. Arachea, Daniel J. Councell, and Michael C. Wiener. "Phosphoramidon inhibits the integral membrane protein zinc metalloprotease ZMPSTE24." Acta Crystallographica Section D Structural Biology 74, no. 8 (July 24, 2018): 739–47. http://dx.doi.org/10.1107/s2059798318003431.

Full text

Abstract:

The integral membrane protein zinc metalloprotease ZMPSTE24 possesses a completely novel structure, comprising seven long kinked transmembrane helices that encircle a voluminous 14 000 Å3cavity within the membrane. Functionally conserved soluble zinc metalloprotease residues are contained within this cavity. As part of an effort to understand the structural and functional relationships between ZMPSTE24 and soluble zinc metalloproteases, the inhibition of ZMPSTE24 by phosphoramidon [N-(α-rhamnopyranosyl-oxyhydroxyphosphinyl)-Leu-Trp], a transition-state analog and competitive inhibitor of multiple soluble zinc metalloproteases, especially gluzincins, has been characterized functionally and structurally. The functional results, the determination of preliminary IC50values by the use of an intramolecular quenched-fluorescence fluorogenic peptide assay, indicate that phosphoramidon inhibits ZMPSTE24 in a manner consistent with competitive inhibition. The structural results, a 3.85 Å resolution X-ray crystal structure of a ZMPSTE24–phosphoramidon complex, indicate that the overall binding mode observed between phosphoramidon and soluble gluzincins is conserved. Based on the structural data, a significantly lower potency than that observed for soluble gluzincins such as thermolysin and neprilysin is predicted. These results strongly suggest a close relationship between soluble gluzincins and the integral membrane protein zinc metalloprotease ZMPSTE24.

APA, Harvard, Vancouver, ISO, and other styles

7

DE MAERE, V., I. VERCAUTEREN, P. GELDHOF, K. GEVAERT, J. VERCRUYSSE, and E. CLAEREBOUT. "Molecular analysis of astacin-like metalloproteases ofOstertagia ostertagi." Parasitology 130, no. 1 (December 13, 2004): 89–98. http://dx.doi.org/10.1017/s0031182004006274.

Full text

Abstract:

In this study, we describe the molecular analysis of zinc-metalloproteases from the abomasal nematodeOstertagia ostertagiwhich were exclusively recognized by local antibodies of immune cattle. Full-length or partial coding sequences of 4 different zinc-metalloprotease cDNAs ofOstertagia(met-1, -2, -3 and -4) were amplified using gene-specific primers using the 3′- and 5′-Rapid Amplification of cDNA Ends (RACE) technique. Sequence analysis identified the cDNAs as encoding zinc-metalloproteases, which showed between 62% and 70% homology to a metalloprotease 1 precursor ofAncylostoma caninum. The full-length cDNA ofmet-1consists of an open reading frame (ORF) of 586 amino acids which contains 5 potentialN-glycosylation sites and a predicted zinc-binding domain (HEBXHXBGFXHEXXRXDRD). The complete coding sequence ofmet-3contains an ORF of 508 aa and the same conserved zinc-binding domain. These domains are signature sequences of the astacin family of the superfamily of metzincin metalloproteases. The presence of a threonine amino acid after the third histidine in MET-1 and MET-3, however, may place them in a new family or subfamily. Real-time PCR analysis of L3, exsheathed L3, L4and adult cDNA identified transcription of the 4 metalloproteases in different life-stages. The protein MET-1 was expressed in insect cells using the baculovirus expression system but the immunization of calves with this molecule did not lead to protection against challenge infection.

APA, Harvard, Vancouver, ISO, and other styles

8

Wladyka, Benedykt, Michal Bista, Artur J. Sabat, Emilia Bonar, Sabina Grzeszczuk, Waleria Hryniewicz, and Adam Dubin. "A novel member of the thermolysin family, cloning and biochemical characterization of metalloprotease from Staphylococcus pseudintermedius." Acta Biochimica Polonica 55, no. 3 (September 4, 2008): 525–36. http://dx.doi.org/10.18388/abp.2008_3059.

Full text

Abstract:

Thermolysins constitute a family of secreted bacterial metalloproteases expressed, among others, by several pathogens. Strains of Staphylococcus pseudintermedius isolated from diseased dogs and judged as protease-positive, by skim milk agar plate culture, were investigated for protease content. No proteolytic activity was detected when the bacteria were grown in regular liquid media. Unexpectedly, supplementation of the medium with calcium ions resulted in expression of a metalloprotease and profound changes in the profile of extracellular proteins. On the basis of homology to other staphylococcal metalloproteases, the nucleotide sequence of the gene encoding this protease (Pst) and its flanking regions was determined. The full-length pst codes for a protein with an open reading frame of 505 amino acids. The internal region contains the HEXXH catalytic domain that is conserved in members of the thermolysin family. Regardless of the presence of calcium in the medium, the expression of the protease gene was of the same intensity. This suggests that regulation of the metalloprotease production by calcium ions is at a post-transcriptional level. Isolates of S. pseudintermedius exhibit a proteolytic phenotype due to the metalloprotease expression, however only in presence of calcium ions, which most probably stabilize the structure of the protease.

APA, Harvard, Vancouver, ISO, and other styles

9

Guillemet, Elisabeth, Céline Cadot, Seav-Ly Tran, Marie-Hélène Guinebretière, Didier Lereclus, and Nalini Ramarao. "The InhA Metalloproteases of Bacillus cereus Contribute Concomitantly to Virulence." Journal of Bacteriology 192, no. 1 (October 16, 2009): 286–94. http://dx.doi.org/10.1128/jb.00264-09.

Full text

Abstract:

ABSTRACT The virulence of Bacillus cereus requires that bacteria have the capacity to colonize their host, degrade specific tissues, and circumvent the host immune system. To study this aspect of pathogenesis, we focused on three metalloproteases, InhA1, InhA2, and InhA3, which share more than 66% identity. The expression of these metalloprotease genes was assessed by transcriptional fusions with a lacZ reporter gene. The expression profiles suggest a complementary time course of InhA production. Indeed, the genes are simultaneously expressed but are oppositely controlled during stationary phase. We constructed single and multiple inhA mutants and assessed the bacterial locations of the proteins as well as their individual or additive roles in macrophage escape and toxicity, antibacterial-peptide cleavage, and virulence. InhA1, a major component of the spore exosporium, is the only InhA metalloprotease involved in bacterial escape from macrophages. A mutant lacking inhA1, inhA2, and inhA3 shows a strong decrease in the level of virulence for insects. Taken together, these results show that the InhA metalloproteases of B. cereus are important virulence factors that may allow the bacteria to counteract the host immune system.

APA, Harvard, Vancouver, ISO, and other styles

10

Antúnez, Karina, Daniela Arredondo, Matilde Anido, and Pablo Zunino. "Metalloprotease production by Paenibacillus larvae during the infection of honeybee larvae." Microbiology 157, no. 5 (May 1, 2011): 1474–80. http://dx.doi.org/10.1099/mic.0.044321-0.

Full text

Abstract:

American foulbrood is a bacterial disease of worldwide distribution that affects larvae of the honeybee Apis mellifera. The causative agent is the Gram-positive, spore-forming bacterium Paenibacillus larvae. Several authors have proposed that P. larvae secretes metalloproteases that are involved in the larval degradation that occurs after infection. The aim of the present work was to evaluate the production of a metalloprotease by P. larvae during larval infection. First, the complete gene encoding a metalloprotease was identified in the P. larvae genome and its distribution was evaluated by PCR in a collection of P. larvae isolates from different geographical regions. Then, the complete gene was amplified, cloned and overexpressed, and the recombinant metalloprotease was purified and used to generate anti-metalloprotease antibodies. Metalloprotease production was evaluated by immunofluorescence and fluorescence in situ hybridization. The gene encoding a P. larvae metalloprotease was widely distributed in isolates from different geographical origins in Uruguay and Argentina. Metalloprotease was detected inside P. larvae vegetative cells, on the surface of P. larvae spores and secreted to the external growth medium. Its production was also confirmed in vivo, during the infection of honeybee larvae. This protein was able to hydrolyse milk proteins as described for P. larvae, suggesting that could be involved in larval degradation. This work contributes to the knowledge of the pathogenicity mechanisms of a bacterium of great economic significance and is one step in the characterization of potential P. larvae virulence factors.

APA, Harvard, Vancouver, ISO, and other styles

More sources

Dissertations / Theses on the topic "Metalloproteasi"

1

Mazzoni, Annalisa <1979&gt. "Ruolo delle metalloproteasi nei processi degenerativi dei tessuti duri del cavo orale." Doctoral thesis, Alma Mater Studiorum - Università di Bologna, 2009. http://amsdottorato.unibo.it/2165/1/mazzoni_annalisa_tesi.pdf.pdf.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Mazzoni, Annalisa <1979&gt. "Ruolo delle metalloproteasi nei processi degenerativi dei tessuti duri del cavo orale." Doctoral thesis, Alma Mater Studiorum - Università di Bologna, 2009. http://amsdottorato.unibo.it/2165/.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Orpianesi, E. "STUDIO DELLE CITOCHINE E DELLE METALLOPROTEASI NELLA LINFANGIOLEIOMIOMATOSI E NELLA SCLEROSI TUBEROSA." Doctoral thesis, Università degli Studi di Milano, 2014. http://hdl.handle.net/2434/230542.

Full text

Abstract:

Tuberous sclerosis complex (TSC), an autosomal dominant disease, is characterized by the formation of hamartomas in various organs such as brain, kidney, skin, retina and heart, and is caused by mutations in TSC1 e TSC2 tumor suppressor genes, encoding hamartin and tuberin, respectively. Lymphangioleiomyomatosis (LAM) is a rare lung disease characterized by cystic lung destruction leading to progressive respiratory failure and formation of abdominal tumors. LAM can be sporadic or associated to TSC and LAM lung alterations resulting from proliferation of neoplastic cells bearing mutations in either TSC1 or TSC2 genes. A metastatic process has been proposed in dissemination of LAM and TSC cells to explain the identical TSC2 mutations and loss of heterozigosity (LOH) patterns in LAM cells of lung nodules, angiomyolipomas and lymph nodes of the same sporadic LAM patients, that is consistent with metastatic spread among organs. The aim of this project is to study the role of cytokines and matrix metalloproteinases in LAM and TSC. LAM/TSC cells, isolated from chylous of a patient affected by LAM associated to TSC, bear a TSC2 germline mutation and do not express tuberin for an epigenetic silencing of the TSC2 second allele that confirms our previously published evidence that an epigenetic alterations of TSC2 can cause the loss of tuberin in TSC cells. Treatment of LAM/TSC cells with 5-azacytidine that inhibits CpG DNA methylation led to the expression of tuberin as consequence of the chromatin remodeling. Proliferation of LAM/TSC cells is epidermal growth factor (EGF)-dependent and blockade of EGF receptor causes cell death, as we previously showed in cells lacking tuberin, while rapamycin, an mTOR inhibitor, significantly reduced proliferation. LAM/TSC cells have the ability to grow independently from adhesion and survive in adherent and nonadherent condition. For these features these cells are a good model to study the mechanisms of motility in LAM and TSC and the relation to tuberin expression. We studied the effect of anti-EGFR Ab and rapamycin on motility, cytokines and MMPs (Matrix metalloproteinases) expression. LAM/TSC cells spontaneously detach and undergo spontaneous cycles of adhesion and nonadhesion conditions likely for the inactivation of the focal adhesion kinase (FAK)/Akt/mTOR pathway. In LAM/TSC cells FAK inhibition caused the reduction of AKT phosphorylation which was followed by inhibition of mTOR phosphorylation and mTOR autophosphorylation and, consequently, by a strong reduction of S6 phosphorilation as it occurs in nonadherent cells. Anti-EGFR antibody and rapamycin reduced the viability of adherent and nonadherent cells while 5-azacytidine slightly increased the percentage of detaching cells. Nonadherent LAM/TSC cells underwent an extremely low proliferation rate consistent with tumour stem cell characteristics. One of the step driving EMT is the repression of E-cadherin, resulting in the loss of cell-cell adhesion. LAM/TSC cells did not express E-cadherin, but they express vimentin, marker of mesenchymal cells. EMT process controls the migration of cancer cells from primary tumors depending on an inflammatory microenvironment. LAM/TSC cells secreted high amount of IL-6, IL-8 and IL-1α, cytokines crucial for a variety of cancer cells. The levels of IL-6, IL-8 and IL-1α were not affected by rapamycin or anti-EGFR antibody but were regulated by tuberin expression since their levels were reduced by 5-azacytidine incubation. MMPs degrade and modify the extracellular matrix (ECM), facilitating detachment of cells from the tissue. Levels of MMP-2 and MMP-9 in urine are predictive of disease status in a variety of cancers and also in LAM. MMP-2 and MMP-9 levels are high in urine of LAM patients and MMP-2 is substantially up-regulated in their lung tissue. Matrilisin (MMP-7) contributes to tumor progression, invasion and is overexpressed in several types of invasive cancers. In adherent status LAM/TSC cells expressed higher levels of MMP-2 mRna and lower of MMP-7 than in nonadherent condition. Consistent with ECM degration and invasive features respectively,. MMP-2 and MMP-7 mRna expression appeared to be related to tuberin since they were significantly reduced by 5-azacytidine incubation. Anti-EGFR Ab and rapamycin significantly decreased MMP-2 mRna expression while their effect was the opposite on MMP-7. Extracellular matrix metalloproteinase inducer (EMMPRIN), is thought to affect tumor progression through its ability to stimulate MMPs expression. EMMPRIN expression, quantified by cytometric analysis, was reduced by 5-azacytidine and was much higher in LAM/TSC cells than in MCF7, breast cancer cells. Anti-EGFR antibody and rapamycin did not change EMMPRIN levels. For the mesenchymal feature of LAM/TSC cells and their ability to survive in adherent and nonadherent conditions, we evaluated LAM/TSC motility in wound healing assay providing an indication of cell migration rate. LAM/TSC cells closed wounds in about 11h, much faster than tumoral cells such as MCF7. Cell motility of LAM/TSC cells is related to tuberin expression since 5-azacytidine treatment, and the consequent induced-tuberin expression, increased the time of wound closure to 19h. However, 5-azacytidine treatment did not have any effect on MMP-2 and MMP-7 mRna expression in wound healing assay. Rapamycin and anti-EGFR Ab decreased the migration rate of LAM/TSC cells leading to the closure of wound in about 25h and causing an induced an increase of MMP-2 and MMP-7 levels. However during wound closure (50%) MMP-2 secretion was increased by anti-EGFR and rapamycin treatments and normalized at complete wound closure. In conclusion, LAM/TSC cells express invasive and migratory features which appear to be related to tuberin expression . Phosphorylation of FAK and MMP-2 expression was reduced in nonadherent LAM/TSC cells compared to adherent cells suggesting that FAK signaling was required for the activation of MMP-2 expression. MMP-2 and MMP-7 are related to the adherent and nonadherent conditions and are involved in the metastatic process proposed in dissemination of LAM cells. LAM/TSC cells have the ability to migrate and their motility is related to tuberin expression and reduced by anti-EGFR antibody and rapamycin. Rapamycin and anti-EGFR Ab control MMP-2 and MMP-7 expression and secretion during cell migration. These data suggest a specific role for MMP-2 and MMP-7 in LAM/TSC cell motility and thereby in the pathogenesis of LAM and TSC indicating their involvement in the metastatic process proposed in dissemination of LAM cells. The understanding of LAM/TSC cell features in motility is important for the assessment of cell invasiveness in LAM and TSC and provide highlights to sustain MMPs pathways as potential target for LAM. TSC and TSC related disorders.

APA, Harvard, Vancouver, ISO, and other styles

4

Testoni, Blasco di Sciacca Alessandra Lucia Maria. "Metalloproteasi 9, TIMP-1 e Osteopontina quali possibili biomarcatori del carcinoma dell endometrio." Doctoral thesis, Università di Catania, 2012. http://hdl.handle.net/10761/1217.

Full text

Abstract:

Lo scopo del nostro lavoro è stato quello di valutare l esistenza di una diversa espressione tissutale e periferica di metalloproteasi MMP9, TIMP1 (la sua proteina inibitoria) e Osteopontina, quali possibili biomarcatori di progressione tumorale, in donne con patologie benigne dell endometrio, con carcinoma dello stesso, e di un gruppo di donne come controllo. Abbiamo reclutato per il nostro studio 31 pazienti che si erano sottoposte ad un esame isteroscopico o per sanguinamenti anomali, o per un ispessimento endometriale evidenziato durante un ecografia ginecologica. Lo stesso giorno in cui alle pazienti veniva eseguita l isteroscopia della cavità uterina, sono stati prelevati circa 10 ml di sangue venoso periferico, suddivisi in due provette: 2-3 ml per la raccolta del siero e 6-7 ml per la raccolta del plasma, con aggiunta di Na++ eparina. Le provette sono state quindi inviate, entro 30 minuti, per la loro centrifugazione ed i campioni di plasma e siero aliquotati, sono stati conservati a -80°C, fino al momento del saggio. Successivamente sono stati eseguiti i dosaggi in ELISA su siero o plasma delle tre proteine da noi considerate, con Kits disponibili commercialmente secondo la metodica indicata dal produttore (R e D System). In corso di isteroscopia, sono state praticate delle biopsie della cavità uterina o dei polipi endometriali. Un piccolo frammento tissutale veniva raccolto in Rna Later, e conservato ad una temperatura di -80°C fino alle indagini di biologia molecolare (estrazione dell RNA ed Immunoistochimica - Elisa); il restante materiale è stato inviato per effettuare l esame istologico. In accordo ai dati della letteratura, i valori medi sierici dei tre parametri da noi considerati, nonchè quelli ricavati dalle biopsie della cavità uterina di donne con carcinoma, sono significativamente più elevati rispetto a quelli di donne con patologie benigne dell endometrio ed ancora di più rispetto ai controlli. La MMP-9 e il suo inibitore TIMP-1, hanno mostrato lo stesso andamento di OPN anche se i valori di TIMP-1 circolante, in accordo con i dati riferiti in letteratura hanno mostrato una maggiore correlazione rispetto alla MMP-9.

APA, Harvard, Vancouver, ISO, and other styles

5

LEONE, LUCIA. "Ruolo del complesso distrofina-distroglicano e delle metalloproteasi nella plasticità neuronale e sinaptica del ganglio cervicale superiore di roditori." Doctoral thesis, La Sapienza, 2005. http://hdl.handle.net/11573/916857.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Paren, Helen. "Inhibitors of metalloproteases." Thesis, University of Oxford, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.260150.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

Schneider, Richard. "Zielgerichtete Evolution Matrix-Metalloprotease-aktivierbarer Retroviren." [S.l.] : [s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=972141375.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Xiang, Yaozu. "Characterisation of the ADAMTS13 metalloprotease domain." Thesis, Imperial College London, 2012. http://hdl.handle.net/10044/1/9835.

Full text

Abstract:

Von Willebrand Factor (VWF) is a large multi-domain plasma glycoprotein that is critical for normal platelet tethering during haemostasis. ADAMTS13 is a plasma metalloprotease that regulates VWF multimeric size/function by cleaving the Tyr1605-Met1606 bond in the VWF A2 domain. Deficiency of ADAMTS13 causes microvascular thrombosis. The only reported cleavage of VWF by ADAMTS13 is that of the Tyr1605-Met1606 bond. How this high substrate specificity is conferred remains unclear. To date, all the interactions between these molecules that have been described involve VWF residues C-terminal to the scissile bond and the non-catalytic domains of ADAMTS13. I hypothesised that VWF also contains an interaction site for ADAMTS13 N-terminal of the cleavage site to aid both in positioning of the scissile bond in the active site and substrate specificity. Previous studies have suggested that the VWF sequence between Asp1596 and Val1604, N-terminal to the cleavage site, is essential for cleavage by ADAMTS13. My aim was to identify the residues in this region that are important determinants for ADAMTS13 proteolysis. A panel of mutations were introduced into the substrate VWF 115 (VWF residues 1554- 1668). The mutants were expressed purified and their proteolysis by ADAMTS13 analysed. It was found that the proteolysis of VWF 115 variants (L1603A, L1603S, L1603N or L1603K) were all substantially impaired (up to >400 fold reduction). The importance of VWF Leu1603 was confirmed using a synthetic peptide 1596DREQAPNLVY1605, which competitively inhibited proteolysis of VWF 115 by ADAMTS13. A mutant peptide containing the L1603A mutation, 1596DREQAPNAVY1605, had minimal effect. When the VWF L1603A substitution was introduced into the full-length recombinant VWF, proteolysis by ADAMTS13 was again substantially reduced. These findings implied the presence of a subsite (S3) in the ADAMTS13 metalloprotease (MP) domain that interacts with VWF Leu1603. Using molecular modelling, the distance between VWF Leu1603 and the scissile bond was estimated as ~10Å. Structural homology modelling of the MP domain, mutagenesis of 11 candidate residues and functional characterisation of these variants identified two clusters, Leu198/Leu232/Leu274 and Val195/Leu151, as possible subsites interacting with VWF. It is suggested that VWF Leu1603 interacts with Leu198/Leu232/Leu274, while Val195/Leu151 may interact with VWF Tyr1605. I propose a mechanism for VWF cleavage involving remote C-terminal domain interactions that assist initial orientation of the VWF scissile bond within the active site of ADAMTS13, but in which N-terminal hydrophobic interactions between VWF Leu1603 and the S3 subsite in the MP domain of ADAMTS13 are critical for the positioning required for cleavage of the Tyr1605-Met1606 scissile bond.

APA, Harvard, Vancouver, ISO, and other styles

9

Solomon, Emilia A. "Regulation and proteolytic activity of ADAM12 metalloprotease." Diss., Manhattan, Kan. : Kansas State University, 2009. http://hdl.handle.net/2097/2197.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Denkin, Steven Michael. "Regulations of empA metalloprotease expression in Vibrio anguillarum /." View online ; access limited to URI, 2003. http://0-wwwlib.umi.com.helin.uri.edu/dissertations/dlnow/3115626.

Full text

APA, Harvard, Vancouver, ISO, and other styles

More sources

Books on the topic "Metalloproteasi"

1

Galea, Charles A., ed. Matrix Metalloproteases. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6863-3.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

M, Hooper N., ed. Zinc metalloproteases in health and disease. London: Taylor & Francis, 1996.

Find full text

APA, Harvard, Vancouver, ISO, and other styles

3

Bambai, Bijan. Purification, cloning, and expression of Cobrin: A C3-cleaving metalloprotease from venom of cobra (Naja naja kaouthia). Hamburg: Ad fontes Verlag, 1998.

Find full text

APA, Harvard, Vancouver, ISO, and other styles

4

Webster, Ellis Lorenzo. Analysis of tissue inhibitor of metalloproteases (TIMP) as the unifying entity in the etiology of abdominal aortic aneurysms. [S.l: s.n.], 1991.

Find full text

APA, Harvard, Vancouver, ISO, and other styles

5

Vincent, Lagente, and Boichot Elisabeth, eds. Matrix metalloproteinases in tissue remodelling and inflammation. Basel: Birkhäuser, 2008.

Find full text

APA, Harvard, Vancouver, ISO, and other styles

6

Astrid, Sigel, and Sigel Helmut, eds. Probing of proteins by metal ions and their low-molecular-weight complexes. New York: Marcel Dekker, 2001.

Find full text

APA, Harvard, Vancouver, ISO, and other styles

7

O, Hill H. A., Sadler P. J, Thomson A. J, and Auld D. S, eds. Metal sites in proteins and models. Berlin: Springer, 1997.

Find full text

APA, Harvard, Vancouver, ISO, and other styles

8

1943-, Greenwald Robert A., Golub Lorne M, and New York Academy of Sciences., eds. Inhibition of matrix metalloproteinases: Therapeutic potential. New York, N.Y: New York Academy of Sciences, 1994.

Find full text

APA, Harvard, Vancouver, ISO, and other styles

9

F, Riordan James, and Vallee Bert L, eds. Metallobiochemistry. San Diego: Academic Press, 1988.

Find full text

APA, Harvard, Vancouver, ISO, and other styles

10

O, Hill H. A., Sadler P. J, and Thompson A. J, eds. Metal sites in proteins and models: Redox centres. Berlin: Springer, 1998.

Find full text

APA, Harvard, Vancouver, ISO, and other styles

More sources

Book chapters on the topic "Metalloproteasi"

1

Gupta, G. S. "Metalloproteases and Metalloprotease Inhibitors." In Proteomics of Spermatogenesis, 655–68. Boston, MA: Springer US, 2005. http://dx.doi.org/10.1007/0-387-27655-6_27.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Ghosh, Arun K., and Sandra Gemma. "Design of Metalloprotease Inhibitors." In Structure-Based Design of Drugs and Other Bioactive Molecules, 143–54. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2015. http://dx.doi.org/10.1002/9783527665211.ch6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Lecomte, Julie, Anne Masset, Dylan R. Edwards, and Agnès Noël. "Tumor Fibroblast-Associated Metalloproteases." In Tumor-Associated Fibroblasts and their Matrix, 175–93. Dordrecht: Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-94-007-0659-0_10.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Auld, David S. "Zinc catalysis in metalloproteases." In Metal Sites in Proteins and Models, 29–50. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/3-540-62874-6_8.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Ugalde, Alejandro P., Gonzalo R. Ordóñez, Pedro M. Quirós, Xose S. Puente, and Carlos López-Otín. "Metalloproteases and the Degradome." In Methods in Molecular Biology, 3–29. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60327-299-5_1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Turner, Anthony J., and Natalia N. Nalivaeva. "Metalloproteases and Proteolytic Processing." In Post-Translational Modifications in Health and Disease, 457–82. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-6382-6_19.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

Spatola, A. F., K. Darlak, S. Pegoraro, K. Nijhawan, M. Anzolin, L. Łankiewicz, and R. D. Gray. "Peptide inhibitors of matrix metalloproteases." In Peptides, 820–21. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1_332.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Montes de Oca Balderas, Pavel. "Metalloproteases in Adaptative Cell Responses." In Proteases in Physiology and Pathology, 121–42. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-2513-6_7.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Singh, Tanya, B. Jayaram, and Olayiwola Adedotun Adekoya. "Computational Approaches to Matrix Metalloprotease Drug Design." In Methods in Molecular Biology, 273–85. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6863-3_15.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Holmbeck, Kenn. "Physiological Functions of Membrane-Type Metalloproteases." In Matrix Proteases in Health and Disease, 57–78. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2012. http://dx.doi.org/10.1002/9783527649327.ch3.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Metalloproteasi"

1

Gurumallesh, Poorani, Baskar Ramakrishnan, and Bhaarathi Dhurai. "Banana peel metalloprotease characterizations." In THE 8TH ANNUAL INTERNATIONAL SEMINAR ON TRENDS IN SCIENCE AND SCIENCE EDUCATION (AISTSSE) 2021. AIP Publishing, 2022. http://dx.doi.org/10.1063/5.0110140.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Holden, T., S. Dehipawala, U. Golebiewska, E. Cheung, G. Tremberger, Jr., E. Williams, P. Schneider, N. Gadura, D. Lieberman, and T. Cheung. "Zn-metalloprotease sequences in extremophiles." In SPIE Optical Engineering + Applications, edited by Richard B. Hoover, Gilbert V. Levin, Alexei Y. Rozanov, and Paul C. W. Davies. SPIE, 2010. http://dx.doi.org/10.1117/12.860091.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Yan, Li, Song Chaojun, Wang Chunyan, Jin Boquan, Jia Wei, and Zhang Duo. "Metalloprotease inhibitors reducing the shedding of human TRAIL." In 2011 International Conference on Human Health and Biomedical Engineering (HHBE). IEEE, 2011. http://dx.doi.org/10.1109/hhbe.2011.6027908.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Nalla, Arun Kumar, Swapna Asuthkar, Venkata Ramesh Dasari, and Jasti S. Rao. "Abstract 434: Radiation-induced matrix metalloprotease-9 promotes mesenchymal transition of Daoy cells and initiates activation of pro-matrix metalloprotease-2." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-434.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Hou, Hsin-Han. "Abstract 542: A disintergrin and metalloprotease (ADAM) 15 promotes non-small cell lung cancer (NSCLC) proliferation through cytosolic domain, not extra-cytosolic metalloprotease activity." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-542.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

"In-Vitro Screening of Clostridium Histolyticum Collagenase and Bacillus Polymyxa Metalloprotease Inhibitory Activities in Ninety-Five Medicinal Plant Extracts." In 4th International Conference on Biological & Health Sciences (CIC-BIOHS’2022). Cihan University, 2022. http://dx.doi.org/10.24086/biohs2022/paper.727.

Full text

Abstract:

Medicinal plants and their different constituents are utilized as therapeutic agents. In present work we report the total phenolics content and screening of ninety five plant extracts for inhibitory activities against Clostridium histolyticum collagenase (ChC) and Bacillus polymyxa metalloprotease (BpM). Total phenolics content from plant methanolic extracts were assessed by using Folin-Ciocalteau assay. Screening of plant extracts for ChC and BpM inhibitory activities was performed by using dot blot assay on X-ray film. G. superba fruit was observed to have the highest phenolics (257.58 ± 0.75 mg GAE /g tissue) content while C. nurvala stem was observed to have the lowest phenolics (0.468 ± 0.003 mg GAE /g tissue) content. Thirty two plants showed ChC inhibitory activities while twenty seven plants showed BpM inhibitory activities. From those plants twenty five plants have common ChC and BpM inhibitory activities. The most of plant Barks were found to have high amount of total phenolics as compared to other plant tissue while the most of plant leaves were found to have low amount of total phenolics. The most of barks were found to exhibit inhibitory activities as compared to other tissue. Only 6 different leaves were found to exhibit inhibitory activity out of 42 different leaves. None of the root extracts exhibited inhibitory activities. In conclusion, the bacterial metalloprotease inhibitory activities of these plant extracts could be explored as significant source for determination of novel drug against human MMPs relevant disorders.

APA, Harvard, Vancouver, ISO, and other styles

7

Churg, A., S. Zhou, O. Preobrazhenska, and JL Wright. "Matrix Metalloprotease Expression in Airways vs Parenchyma of Cigarette Smoke-Exposed Mice." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a1007.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Duitman, Janwillem, Cong Lin, Awen Menou, Keren S. Borensztajn, C. Arnold Spek, and Bruno Crestani. "Detrimental role for matrix metalloprotease-1 in the pathogenesis of pulmonary fibrosis." In ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.pa1034.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Bratcher, Preston, Robert Snelgrove, Nathaniel Weathington, and Amit Gaggar. "Matrix Metalloprotease (MMP)-9 Modulates Surfactant Protein-D (SP-D) Functions In Vitro." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a1382.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Fonseca M de Oliveira, Henrique, LJUBICA TASIC, and Roney Vander dos Santos. "Inhibitory action of hesperetin on a venom metalloprotease from the Bothrops asper snake." In XXV Congresso de Iniciação Cientifica da Unicamp. Campinas - SP, Brazil: Galoa, 2017. http://dx.doi.org/10.19146/pibic-2017-78177.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Reports on the topic "Metalloproteasi"

1

Pytela, Robert. Metalloprotease/Disintegrin Proteins and Mammary Carcinoma Progression. Fort Belvoir, VA: Defense Technical Information Center, October 1998. http://dx.doi.org/10.21236/ada369252.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Yan, Yibing, and Z. Werb. Engineering of Specific Tissue Inhibitors to Block ADAM Type Metalloprotease-Mediated Mammary Neoplasia. Fort Belvoir, VA: Defense Technical Information Center, July 2000. http://dx.doi.org/10.21236/ada390922.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Mobashery, Shahriar. Novel and Selective Inactivators for Matrix Metalloproteases Involved in Breast Cancer Metastasis. Fort Belvoir, VA: Defense Technical Information Center, July 1999. http://dx.doi.org/10.21236/ada374214.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Mobashery, Shahriar. Novel and Selective Inactivators for Matrix Metalloproteases Involved in Breast Cancer Metastasis. Fort Belvoir, VA: Defense Technical Information Center, July 2000. http://dx.doi.org/10.21236/ada392785.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!