Academic literature on the topic 'Pyrin Domain-Containing 3 Protein'
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Journal articles on the topic "Pyrin Domain-Containing 3 Protein"
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Dr., Pruthvi S. Suthar. "NLRP3 Inflammasome and it's Inhibitors in Chronic Inflammatory Diseases." Science world a Monthly e magazine 5, no. 2 (2025): 6345–47. https://doi.org/10.5281/zenodo.14956404.
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Inflammasomes are a group of cytosolic protein complexes that are formed to mediate host immune responses to microbial infection and cellular damage. There are five members of pattern-recognition receptors (PRRs) that have been confirmed to form inflammasomes: NLRP1, NLRP3, and NLRC4, Absent-In-Melanoma 2 (AIM2) and Pyrin. NLRP3 (Nucleotide-binding domain, Leucine-Rich–containing family, Pyrin domain–containing-3) combines sensing, regulation and effector functions to regulate inflammation in health and disease (Moossavi et al., 2018).
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Perri, Anna. "The NLRP3-Inflammasome in Health and Disease." International Journal of Molecular Sciences 23, no. 21 (2022): 13103. http://dx.doi.org/10.3390/ijms232113103.
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The nucleotide-binding domain (NOD)-, leucine-rich repeat (LRR)-, and pyrin domain (PYD)-containing protein 3, NLRP3, is a multiprotein complex belonging to the innate immune system that can be activated by pathogens or danger-associated molecular patterns [...]
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Machtens, Dominik Alexander, Ian Philipp Bresch, Jan Eberhage, Thomas Frank Reubold, and Susanne Eschenburg. "The Inflammasome Activity of NLRP3 Is Independent of NEK7 in HEK293 Cells Co-Expressing ASC." International Journal of Molecular Sciences 23, no. 18 (2022): 10269. http://dx.doi.org/10.3390/ijms231810269.
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The cytosolic immune receptor NLRP3 (nucleotide-binding domain, leucine-rich repeat (LRR), and pyrin domain (PYD)-containing protein 3) oligomerizes into the core of a supramolecular complex termed inflammasome in response to microbes and danger signals. It is thought that NLRP3 has to bind NEK7 (NIMA (never in mitosis gene a)-related kinase 7) to form a functional inflammasome core that induces the polymerization of the adaptor protein ASC (Apoptosis-associated speck-like protein containing a CARD (caspase recruitment domain)), which is a hallmark for NLRP3 activity. We reconstituted the NLRP3 inflammasome activity in modified HEK293 (human embryonic kidney 293) cells and showed that the ASC speck polymerization is independent of NEK7 in the context of this cell system. Probing the interfaces observed in the different, existing structural models of NLRP3 oligomers, we present evidence that the NEK7-independent, constitutively active NLRP3 inflammasome core in HEK293 cells may resemble a stacked-torus-like hexamer seen for NLRP3 lacking its PYD (pyrin domain).
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Wilhelm, Imola, Ádám Nyúl-Tóth, Mihály Kozma, Attila E. Farkas, and István A. Krizbai. "Role of pattern recognition receptors of the neurovascular unit in inflamm-aging." American Journal of Physiology-Heart and Circulatory Physiology 313, no. 5 (2017): H1000—H1012. http://dx.doi.org/10.1152/ajpheart.00106.2017.
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Aging is associated with chronic inflammation partly mediated by increased levels of damage-associated molecular patterns, which activate pattern recognition receptors (PRRs) of the innate immune system. Furthermore, many aging-related disorders are associated with inflammation. PRRs, such as Toll-like receptors (TLRs) and nucleotide-binding oligomerization domain-like receptors (NLRs), are expressed not only in cells of the innate immune system but also in other cells, including cells of the neurovascular unit and cerebral vasculature forming the blood-brain barrier. In this review, we summarize our present knowledge about the relationship between activation of PRRs expressed by cells of the neurovascular unit-blood-brain barrier, chronic inflammation, and aging-related pathologies of the brain. The most important damage-associated molecular pattern-sensing PRRs in the brain are TLR2, TLR4, and NLR family pyrin domain-containing protein-1 and pyrin domain-containing protein-3, which are activated during physiological and pathological aging in microglia, neurons, astrocytes, and possibly endothelial cells and pericytes.
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Hu, Jian, Yun Zhu, Jian-Zhong Zhang, Rong-Guang Zhang, and Hou-Min Li. "A Novel Mutation in the Pyrin Domain of the NOD-like Receptor Family Pyrin Domain Containing Protein 3 in Muckle-Wells Syndrome." Chinese Medical Journal 130, no. 5 (2017): 586–93. http://dx.doi.org/10.4103/0366-6999.200537.
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Moghaddas, Fiona, Rafael Llamas, Dominic De Nardo, et al. "A novel Pyrin-Associated Autoinflammation with Neutrophilic Dermatosis mutation further defines 14-3-3 binding of pyrin and distinction to Familial Mediterranean Fever." Annals of the Rheumatic Diseases 76, no. 12 (2017): 2085–94. http://dx.doi.org/10.1136/annrheumdis-2017-211473.
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ObjectivePyrin-Associated Autoinflammation with Neutrophilic Dermatosis (PAAND) is a recently described monogenic autoinflammatory disease. The causal p.S242R MEFV mutation disrupts a binding motif of the regulatory 14-3-3 proteins within pyrin. Here, we investigate a family with clinical features consistent with PAAND in whom the novel p.E244K MEFV mutation, located in the +2 site of the 14-3-3 binding motif in pyrin, has been found.MethodsMultiplex cytokine analyses were performed on p.E244K patient and control serum. Peripheral blood mononuclear cells were stimulated ex vivo with lipopolysaccharide (LPS). In vitro, inflammasome complex formation was evaluated by flow cytometry of Apoptosis-associated Speck-like protein containing a Caspase recruitment domain (ASC) specks. Interleukin-1β (IL-1β) and IL-18 production was quantified by ELISA. The ability of the p.E244K pyrin mutation to interact with 14-3-3 was assessed by immunoprecipitation.ResultsPAAND p.E244K patient serum displayed a different cytokine profile compared with patients with Familial Mediterranean Fever (FMF). In overexpression models, p.E244K pyrin was associated with decreased 14-3-3 binding and increased ASC speck formation. THP-1 monocytes expressing PAAND pyrin mutations demonstrated spontaneous caspase-1-dependent IL-1β and IL-18 secretion, as well as cell death, which were significantly greater than those of wild-type and the FMF-associated mutation p.M694V.ConclusionIn PAAND, disruption of the +2 position of a 14-3-3 binding motif in pyrin results in its constitutive activation, with spontaneous production of IL-1β and IL-18, associated with inflammatory cell death. The altered serum cytokine profile may explain the different clinical features exhibited by PAAND patients compared with those with FMF.
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Shen, Guowei, Shichang Yan, Siyuan Shen, et al. "Curculigoside Inhibits the Progression of Osteoarthritis via Regulating Nucleotide-Binding Oligomerization Domain-Like Receptor Containing Pyrin Domain 3." Journal of Biomedical Nanotechnology 19, no. 9 (2023): 1594–602. http://dx.doi.org/10.1166/jbn.2023.3695.
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This study aimed to explore the potential effects of curculigoside on NLRP3 expression and catabolic genes in osteoarthritis (OA) development. OA mouse models were generated by destabilizing the medial meniscus (DMM) and treated with curculigoside. Curculigoside treatment resulted in dose-dependent reductions in OARSI scores, with the 20 μg dose restoring scores to normal levels. Curculigoside increased mRNA and protein levels of iNOS and MMP9 induced by DMM surgery in a dose-dependent manner. Moreover, curculigoside downregulated the expression of NLRP3, NF-κB, and PKR at both mRNA and protein levels. Additionally, curculigoside reversed the effects of IL-1β on MMP-9, iNOS, and Col2A mRNA and protein levels in a dose-dependent manner, similar to the NLRP3 inhibitor MCC950. In vivo and in vitro results supported curculigoside’s potential to aid cartilage restoration in OA patients by blocking the NLRP3 pathway. These findings suggest curculigoside as a potential therapeutic option for OA, offering hope for improved public health outcomes related to this degenerative joint condition.
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Magupalli, Venkat Giri, Roberto Negro, Yuzi Tian, et al. "HDAC6 mediates an aggresome-like mechanism for NLRP3 and pyrin inflammasome activation." Science 369, no. 6510 (2020): eaas8995. http://dx.doi.org/10.1126/science.aas8995.
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Inflammasomes are supramolecular complexes that play key roles in immune surveillance. This is accomplished by the activation of inflammatory caspases, which leads to the proteolytic maturation of interleukin 1β (IL-1β) and pyroptosis. Here, we show that nucleotide-binding domain, leucine-rich repeat, and pyrin domain–containing protein 3 (NLRP3)- and pyrin-mediated inflammasome assembly, caspase activation, and IL-1β conversion occur at the microtubule-organizing center (MTOC). Furthermore, the dynein adapter histone deacetylase 6 (HDAC6) is indispensable for the microtubule transport and assembly of these inflammasomes both in vitro and in mice. Because HDAC6 can transport ubiquitinated pathological aggregates to the MTOC for aggresome formation and autophagosomal degradation, its role in NLRP3 and pyrin inflammasome activation also provides an inherent mechanism for the down-regulation of these inflammasomes by autophagy. This work suggests an unexpected parallel between the formation of physiological and pathological aggregates.
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Zhang, Chen, Mingjing Lu, CunNeng Li та ін. "Mechanism of inhibition of TLR4/NFκB/NLRP3 inflammatory pathway against AD based on the network pharmacology of Erjing Pills". Medicine 103, № 34 (2024): e39392. http://dx.doi.org/10.1097/md.0000000000039392.
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Alzheimer disease is an irreversible neurodegenerative disease, and its pathogenesis involves various mechanisms such as neuroinflammation and β-amyloid deposition. Erjing Pills can inhibit neuroinflammation by inhibiting toll-like receptor 4/nuclear factor kappa-B/nucleotide-binding domain leucine-rich repeat and pyrin domain-containing protein 3; however, qualitative analysis of the material basis is lacking. Therefore, it is necessary to analyze and explore the material basis of network pharmacology research. This study employed a multifaceted approach, including drug-like screening, molecular docking, and bioinformatic analysis. Preliminary screening identified 59 drug ingredients in Erjing Pills that met the Absorption, Distribution, Metabolism, Excretion and Toxicity screening criteria. Among these, 7 ingredients, including diosgenin, exhibited superior binding properties compared with the positive drugs in molecular docking. Gene ontology annotation and pathway analysis revealed their involvement in crucial biological processes, such as hormone response, insulin resistance, and steroid hormone biosynthesis signaling pathways, which are known for their anti-inflammatory and cognitive enhancement effects. A meta-analysis of relevant literature corroborated the anti-inflammatory activities of diosgenin and 5 other ingredients. These 5 ingredients, with diosgenin as a prominent candidate, exert anti-inflammatory effects by targeting key components of the toll-like receptor 4/nuclear factor kappa-B/nucleotide-binding domain leucine-rich repeat and pyrin domain-containing protein 3 inflammatory pathway, thereby presenting potential efficacy in the treatment of Alzheimer disease.
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Ren, Honglei, Ying Kong, Zhijia Liu, et al. "Selective NLRP3 (Pyrin Domain–Containing Protein 3) Inflammasome Inhibitor Reduces Brain Injury After Intracerebral Hemorrhage." Stroke 49, no. 1 (2018): 184–92. http://dx.doi.org/10.1161/strokeaha.117.018904.
Full textDissertations / Theses on the topic "Pyrin Domain-Containing 3 Protein"
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Burgess, Joshua T. "The role of SAM and SH3 domain-containing protein 1 (SASH1) in DNA damage repair and tumourigenesis." Thesis, Queensland University of Technology, 2016. https://eprints.qut.edu.au/98661/1/Joshua_Burgess_Thesis.pdf.
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SASH1 (SAM and SH3 domain-containing protein 1) is a putative tumour suppressor functioning in the control of apoptosis and cellular proliferation. In summary this project has further characterised the role of SASH1 in genome maintenance, including DNA repair and apoptosis, which has implications on its links with tumourigenesis. In addition we have also identified that targeting SASH1 may be a novel cancer treatment target and shown that Chloropyramine may act as an effective anti-cancer agent through a SASH1-dependent pathway.
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Yoshinaga, Masanori. "Regnase-1 Maintains Iron Homeostasis via the Degradation of Transferrin Receptor 1 and Prolyl-Hydroxylase-Domain-Containing Protein 3 mRNAs." Kyoto University, 2020. http://hdl.handle.net/2433/253191.
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Goulet, Isabelle. "New Roles for Arginine Methylation in RNA Metabolism and Cancer." Thèse, Université d'Ottawa / University of Ottawa, 2011. http://hdl.handle.net/10393/20293.
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Because it can expand the range of a protein’s interactions or modulate its activity, post-translational methylation of arginine residues in proteins must be duly coordinated and ‘decoded’ to ensure appropriate cellular interpretation of this biological cue. This can be achieved through modulation of the enzymatic activity/specificity of the protein arginine methyltransferases (PRMTs) and proper recognition of the methylation ‘mark’ by a subset of proteins containing ‘methyl-sensing’ protein modules known as ‘Tudor’ domains. In order to gain a better understanding of these regulatory mechanisms, we undertook a detailed biochemical characterization of the predominant member of the PRMT family, PRMT1, and of the novel Tudor domain-containing protein 3 (TDRD3). First, we found that PRMT1 function can be modulated by 1) the expression of up to seven PRMT1 isoforms (v1-7), each with a unique N-terminal region that confers distinct substrate specificity, and by 2) differential subcellular localization, as revealed by the presence of a nuclear export sequence unique to PRMT1v2. Second, our findings suggest that TDRD3 is recruited to cytoplasmic stress granules (SGs) in response to environmental stress potentially by engaging in methyl-dependent protein-protein interactions with proteins involved in the control of gene expression. We also found that arginine methylation may serve as a general regulator of overall SG dynamics. Finally, we uncovered that alteration of PRMT1, TDRD3, and global arginine methylation levels in breast cancer cells may be closely associated with disease progression and poor prognosis. Therefore, further studies into the pathophysiological consequences ensuing from misregulation of arginine methylation will likely lead to the development of novel strategies for the prevention and treatment of breast cancer.
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Liu, Xiao [Verfasser], and Alexander [Akademischer Betreuer] Weber. "Human NACHT, LRR, and PYD domain-containing protein 3 (NLRP3) inflammasome activity is regulated by and potentially targetable through Bruton tyrosine kinase / Xiao Liu ; Betreuer: Alexander Weber." Tübingen : Universitätsbibliothek Tübingen, 2018. http://d-nb.info/119911538X/34.
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Rapone, Roberta. "Essential cytoplasmic role(s) of the histone lysine methyltransferase Setdb1 in post-transcriptional regulation of gene expression." Thesis, Université de Paris (2019-....), 2019. https://theses.md.univ-paris-diderot.fr/RAPONE_Roberta_va.pdf.
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Setdb1 est une «histone» lysine méthyltransférase (KMT) appartenant à la famille SUV39, l’une des principales machineries épigénétiques de répression des gènes. Setdb1 établit notamment la mono-, la di- et la tri- méthylation sur la lysine 9 de l'histone H3 (H3K9).Setdb1 est essentiel pour la survie, la pluripotence et l'auto-renouvellement des cellules souches embryonnaires de souris (mESCs); son knock-out est mortel au stade de la péri-implantation à 3,5 dpc chez la souris. Setdb1 est également nécessaire pour la différenciation de nombreux types de cellules progénitrices : spermatogenèse, neurogenèse, différenciation des chondrocytes et différenciation des muscles squelettiques. De plus, Setdb1 a été associé à plusieurs maladies: il est amplifié dans le mélanome et le cancer du poumon et il est dérégulé dans les cancers du foie, de la prostate, colorectal et du sein, dans la maladie de Huntington et la schizophrénie. Remarquablement, au-delà des histones, Setdb1 méthyle nombreux substrats non-histones, y compris UBF, p53, Akt, Tat et Ing2.Bien que Setdb1 ait toujours été associé à son rôle nucléaire, il s'avère que Setdb1 est la seule KMT de la famille SUV39 à avoir également une localisation cytoplasmique, dans plusieurs types de cellules, y compris les mESCs, les fibroblastes embryonnaires de souris (MEFs) et les cellules HeLa. Cependant, la fonction de Setdb1 dans le cytoplasme reste totalement inconnue. Pour étudier le rôle cytoplasmique de Setdb1, nous avons utilisé des cellules souches embryonnaires de souris (mESCs), dans lesquelles Setdb1 est essentiel. Nos résultats montrent que Setdb1 cytoplasmique est crucial pour la survie des mESCs: en effet, le nombre de cellules apoptotiques augmente après la perte de Setdb1 cytoplasmique. Nous avons constaté que le Setdb1 cytoplasmique affecte la synthèse de protéines dans les mESCs. Nous montrons en outre que le Setdb1 cytoplasmique interagit avec la protéine Trim71 spécifique de mESC (également appelée Lin41) et avec le facteur de traduction d'initiation eIF3c dans les mESC. Enfin, nous avons démontré que Setdb1 et Trim71 co-régulent ensemble la stabilité et la traduction des mARNs. Nos données actuelles mettent au jour la fonction cytoplasmique essentielle d'une lysine méthyltransférase appelée Setdb1, au début considérée comme étant spécifique uniquement des histones et apportent de nouvelles informations sur la régulation post-transcriptionnelle de l'expression génique médiée par un régulateur épigénétique fondamental<br>Setdb1 is a “histone” lysine methyltransferase (KMT) belonging to the SUV39 family that methylates lysine 9 of histone H3 (H3K9), one of the major epigenetic machineries mainly involved in gene repression. Notably, Setdb1 establishes mono-, di- and tri-methylation of H3K9. Setdb1, or Eset in mice, is essential for the survival, the pluripotency and the self-renewal of mouse embryonic stem cells (mESCs); Eset knockout is lethal at the peri-implantation stage at 3.5 dpc in mice. Setdb1 is also required for the differentiation of many progenitor cell types: spermatogenesis, neurogenesis, chondrocyte differentiation and skeletal muscle differentiation. Moreover, Setdb1 has been associated with several diseases: it is amplified in melanoma and lung cancer and it is dysregulated in liver, prostate, colorectal and breast cancers, Huntington disease and schizophrenia.Remarkably, beyond histones, Setdb1 methylates many non-histone substrates, such as UBF, p53, AKT, Tat and ING2 proteins. Although Setdb1 has been always associated with its nuclear role, it turns out that Setdb1 is the only H3K9 KMT to have also a cytoplasmic localization, in several cell types, including mESCs, mouse embryonic fibroblasts (MEFs) and HeLa cells. However, the function of Setdb1 in the cytoplasm remains totally unknown. To investigate Setdb1 cytoplasmic role, we have used mouse embryonic stem cells (mESCs), in which Setdb1 is essential. Our results show that cytoplasmic Setdb1 is crucial for the survival of mESCs: indeed, the number of apoptotic cells increases after the loss of cytoplasmic Setdb1. We found that cytoplasmic Setdb1 affects newly protein synthesis in mESCs. We further show that cytoplasmic Setdb1 interacts with mESCs-specific protein Trim71 (also called Lin41) and with the initiation translation factor eIF3c in mESCs. Finally, we reported that Setdb1 and Trim71 together co-regulate mRNA stability and translation. Our current data unravel the essential cytoplasmic function of Setdb1, for long time considered exclusively an “histone” lysine methyltransferase, and provide new insights into the post-transcriptional regulation of gene expression mediated by a fundamental epigenetic regulator
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Li, Zengqiu. "Characterization of the Acyl-CoA binding domain containing 3 protein." Thesis, 2006. http://hdl.handle.net/10125/20721.
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Wieczerzak, Krzysztof. "Analysis of coiled coil domain containing 33 protein (CCDC33) and determination of infertility causes in mutant mouse line with the deletion of six germ cell-specific genes." Doctoral thesis, 2012. http://hdl.handle.net/11858/00-1735-0000-000E-0131-3.
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Zusammenfassung
Da die meisten Fälle männlicher Unfruchtbarkeit immer noch idiopatisch bleiben, könnte eine Untersuchung der Mechanismen, in denen Gene der Spermatogenese-Kontrolle involviert sind, helfen, die Gründe besser zu verstehen. Diese Arbeit besteht aus zwei Teilen die zwei verschiedene Aspekte humaner Fertilitätsforschung betreffen. Das erste Projekt betrifft die Analyse des coiled coil domain containing 33 (CCDC33) Proteins und seiner Rolle als peroxisomal testis specific 1 (PXT1) Interaktionspartner. Im zweite Projekt haben wir die Ursache männlicher Unfruchtbarkeit in Mäusen mit multiplen knockouts bestimmt und den Phänotyp anlaysiert. Folgende Gene wurden ausgeknocked: Tnp2, Hist1h1t, Theg, Acr, Creb3l4 and Tex22.
Im ersten Teil dieser Arbeit wurden Domänen, die bei der CCDC33 und PXT1-Interaktion beteilgt sind, identifiziert. Die Interaktion dieser beiden Proteine wurde duch Kaczmarek identifiziert (Kaczmarek, 2009). Wir zeigten, dass nicht die coiled coil Domänen für die Interaktion mit PXT1 verantwortlich sind, sondern eine Aminosäuresequenz welche der Sequenz in Leucin-reichen Domänen ähnlich ist. Durch induzierte Mutagenese in der PXT1-Sequenz haben wir Aminosäuresequenzen identifiziert, die für die Interaktion von PXT1 und CCDC33 bedeutend sind. PXT1 ist ein erstes peroxisomales Protein das eine funktionale BH3-ähnliche Domäne enthält, die dafür bekannt ist Apoptose zu induzieren. Aufgrund von Experimenten mit Co-transfizieretn HeLa Zellen konnten wir eine Co-Lokalisation von CCDC33 und PXT1 im Zytoplasma nachweisen. Zudem zeigten Zellen mit Co-Lokalisation beider Proteine eine Reduktion der Apoptoserate im Vergleich zu Zellen die nur mit dem PXT1-Konstrukt transfiziert waren. Dieser Befund könnte suggerieren, dass die physikalische Bindung beider Proteine die PXT1-induzierte Apoptose verhindert. Durch Western Blot und immunhistochemische Experimente konnten wir zeigen, dass das CCDC33 Protein in den Hoden während der Spermatogenese ab dem Spermatocyten- Stadium lokalisiert ist. Sowohl die Interaktion von CCDC33 und PXT1 als auch das Expressionsmuster beider Gene implizieren, dass Ccdc33 in der Kontrolle der Spermatogenese involiert sein könnte. Wir postulieren, dass CCDC33 ein neues peroxisomales Protein sein könnte, welches Apoptose während der Spermatogenes reguliert. Jedoch sind weitere Untersuchungen, u.a. die Analyse von CCDC33 knockout Maus-Modellen, nötig, um feststellen zu können ob Ccdc33 für die männliche Fertilität essentiell ist.
Im zweiten Teil dieser Arbeit wird die Analyse von knockout Mäuselinien, in denen 6 keimzellspezifische Gene funktionsunfähig gemacht wurden, beschrieben. In ca. 20% der Mäuse wurde Unfruchtbarkeit festgestellt. In beiden, männlichen fruchtbaren und unfruchtbaren 6xKO Mäusen, ist die Zahl an Spermatozoa mit abnormalen Kopf erhöht und Sperma-Motilität reduziert. Nach Kreuzung von weiblichen wildtyp Mäusen mit männlichen 6xKO Tieren, benötigte das Sperma bemerkenswert längere Zeit um die Oocyte zu befreuchten as im Vergleich zu WT Sperma. Die Unterschiede im Phänotyp der 6xKO Mäuse sind sowohl dem genetischen Hintergrund als auch der Inaktivierung der sechs keimzellspezifischen Gene zuzuschreiben. Um genauer zu untersuchen welche Gene bei der Unfruchhtbarkeit der 6xKO Mäuse involviert sein könnten haben wir ein Transkriptom Assay durchgeführt und die Genexpression in den Hoden von 5xKO Tieren, die fertil waren, mit der in 6xKO Mäusen, die infertil waren, verglichen. Wir haben ein neues Gen, 4933400A11Rik, identifiziert und charakterisiert, welches für die Unfruchtbarkeit männlicher 6xKO Mäuse verantwortlich sein könnte. In WT Mäusen ist 4933400A11Rik in den Keimzellen exprimiert. 4933400A11Rik mRNA wurde ab Tag 16 post partum, wenn primäre Spermatozyten produziert werden, bis zu den ausgewachsenen Spermien detektiert. Es ist jedoch nicht klar, ob die mRNA die in den Spermien entdeckt wurde ein Ergebniss der Expression von 4933400A11Rik sind, oder ob es sich dabei um restliche Moleküle handelt welche während der Spermatogenese nicht abgebaut wurden. 4933400A11RIK weist Sequenzähnlichkeiten zur Aktinfilament capping Proteinfamile auf. Wir zeigten, dass 4933400A11RIK mit F-Aktin capping Protein Untereinheit alpha-1 colokalisiert. Proteine dieser Familie sind bekannt dafür das Wachstum des Zytoskeletts durch Regulation der Aktinfilament-Reorganisation zu kontrollieren. Deregulation der Aktinzytoskelett-Reorganisation in Keimzellen könnte die zugrundeliegende Ursache der männlichen Unfruchtbarkeit in 6x KO Mäusen sein, denn 4933400A11Rik wird in den Hoden fertiler 6xKO Mäuse, aber nicht in den Hoden infertiler 6xKO Mäuse exprimiert. Um die Frage eindeutig zu beantworten, ob das Gen 4933400A11Rik die Fertilität beeinflusst, sollten 4933400A11Rik knockout Mäuse generiert und analysiert werden. Das ´Rescue-Experiment´ könnte ebenso die Involvierung dieses Gens bei männlichen Fertilität bestätigen.
Zusammenfassend präsentiert diese Arbeit interessante Erkenntnisse über die potentielle Funktion von CCDC33 bei der Regulation der Spermatogenese. Außerdem zeigen wir kumulierte Effekte von 6 keimzellspezifischen Genen und einem neuen Gen, 4933400A11Rik, welches für die weitere Forschung männlicher Unfruchtbarkeit interessant sein könnte.
Book chapters on the topic "Pyrin Domain-Containing 3 Protein"
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Salajegheh, Ali. "Sprouty-Related, EVH1 Domain-Containing Protein 1 (SPRED-1)." In Angiogenesis in Health, Disease and Malignancy. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-28140-7_47.
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Jaiswal, Anju, Asha Kumari, and Rashmi Singh. "Role of NLRP3 Inflammasome in Airway Inflammation and Fibrosis." In The NLRP3 Inflammasome: An Attentive Arbiter of Inflammatory Response. BENTHAM SCIENCE PUBLISHERS, 2024. http://dx.doi.org/10.2174/9789815223941124010003.
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The NLRP3 inflammasome is a critical component of the innate immune system that mediates caspase-1 activation and the secretion of proinflammatory cytokines IL-1β/IL-18 in response to microbial infection and cellular damage. Nucleotide-binding oligomerization domain (NOD)-like receptor family pyrin domain 3 (NLRP3), one of the members of the NLR family, consists of NLRP3, the adaptor molecule, apoptosis-associated speck-like protein containing a caspase and recruitment domain (ASC) and an inflammatory caspase-1 that causes excessive inflammasome activation in respiratory diseases like asthma and could exacerbate the progression of asthma by considerably contributing to ECM accumulation and airway remodeling. NLRP3 is closely associated with airway inflammation and asthma exacerbations as endotoxin (lipopolysaccharide, LPS) is one of its activators present in the environment. Asthma is a complex immunological and inflammatory disease characterized by the presence of airway inflammation, airway wall remodeling and bronchial hyperresponsiveness (BHR). Symptomatic attacks of asthma can be caused by a myriad of situations, including allergens, infections, and pollutants, which cause the rapid aggravation of respiratory problems. The presence of LPS in the environment is positively correlated with the incidence of asthma and allergic diseases. In this chapter, we summarize our current understanding of the mechanisms of NLRP3 inflammasome activation by multiple signaling events in asthmatic exacerbations and their regulation.
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"START Domain-Containing Protein." In Encyclopedia of Cancer. Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-46875-3_102175.
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"JmjC Domain-Containing Protein 3." In Encyclopedia of Cancer. Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-46875-3_101264.
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"Jumonji Domain-Containing Protein 3." In Encyclopedia of Cancer. Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-46875-3_101269.
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"EHSH1 (EH Domain/SH3 Domain-Containing Protein)." In Encyclopedia of Cancer. Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-46875-3_100789.
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"Ankyrin Repeat Domain-Containing Protein 3." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_100211.
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"Ras Association Domain-Containing Protein 6." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_103230.
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"CDCP1 (CUB Domain-Containing Protein 1)." In Encyclopedia of Cancer. Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-46875-3_100466.
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"Toll/Interleukin-1 Receptor Domain-Containing Protein." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_103902.
Full textConference papers on the topic "Pyrin Domain-Containing 3 Protein"
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Vos, Samantha, Oyewole Oyekoya, and Olorunseun Ogunwobi. "Visualization of Point Mutations in Fibronectin Type-III Domain-Containing Protein 3 in Prostate Cancer." In ISS '23: Conference on Interactive Surfaces and Spaces. ACM, 2023. http://dx.doi.org/10.1145/3626485.3626531.
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Luborsky, Judith, Seara Edassery, Seby L. Edassery, Animesh Barua та Janice M. Bahr. "Abstract B08: Inflammasome components caspase-1, IL1β, IL18 and NLRP3 (NOD-like receptor family, pyrin domain containing 3) are increased in a spontaneous model (chicken: Gallus gallus) of human ovarian cancer". У Abstracts: Fourth AACR International Conference on Frontiers in Basic Cancer Research; October 23-26, 2015; Philadelphia, PA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.fbcr15-b08.
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Chang, Y.-F., Y. Wang, and GL Greene. "Abstract P6-11-14: Src homology 2 domain containing transforming protein 1 and steroid receptor coactivator-3 as novel targets for triple-negative breast cancer." In Abstracts: 2016 San Antonio Breast Cancer Symposium; December 6-10, 2016; San Antonio, Texas. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.sabcs16-p6-11-14.
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O'hara, Patrick J., Frank A. Grant, A. Betty, J. Haldmen, and Mark J. Murray. "Structure of the Human Factor VII Gene." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643786.
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Factor VII is a member of a family of vitamin K-dependent, gamma-carboxylated plasma protein which includes factor IX, factor X, protein C, protein S and prothrombin. Activated factor VII (factor Vila) is a plasma serine protease which participates in a cascade of reactions leading to the coagulation of blood. Two overlapping genomic clones containing sequences encoding human factor VII were isolated and characterized. The complete sequence of the gene was determined and found to span 12.8 kilobases. The mRNA for factor VII as demonstrated by cDNA cloning is polyadenylated at multiple sites but contains only one AAUAAA poly-A signal sequence. The mRNA can undergo alternative splicing forming one transcript containing eight segments as exons and another with an additional exon which encodes a larger pre-pro leader sequence. The portion of the pre-pro leader coded for by the additional exon has no known counterpart in the other vitamin K-dependent proteins. The positions of the introns with respect to the amino acid sequence encoded by the eight essential exons of factor VII are the same as those present in factor IX, factor X, protein C and the first three exons of prothrombin. These exons code for domains generally conserved among members of this gene family, including a pre-pro leader (the essential exon la and alternative exon lb), a gamma-carboxylated domain (exons 2 and 3) a growth factor domain (exons 4 and 5) an activation region (exon 6) and a serine protease (exon 8). The corresponding introns in these genes are dissimilar with respect to size and sequence, with the exception of the third intron in factor VII and protein C. Four introns and a portion of exon 8 in factor VII contain regions made up of tandem repeats of oligonucleotide monomer elements. More than a quarter of the intron sequences and more than a third of the 3' untranslated portion of the mRNA transcript consist of these minisatellite tandem repeats. This type of structure is responsible for polymorphisms due to allelic variation in repeat copy number in other areas of the human genome. Tandem repeats can evolve as a result of random crossover in DNA whose sequence is not maintained by selection. This suggests that much of the sequence information present in the introns and untranslated portion of the message is dispensable.
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Kaufman, Randal J., David G. Bole, and Andrew J. Dorner. "THE INFLUENCE OF N-LINKED GLYCOSYLATION AND BINDING PROTEIN (BiP) ASSOCIATION IN THE SECRETION EFFICIENCY OF COMPLEX GLYCOPROTEINS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644016.
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We have studied the role of Binding Protein (BiP) or glucose regulated protein, GRP 78) in the processing and secretion of factor VIII (fVIII), von Willebrand factor (vWF), and tissue plasminogen activator(tPA) expressed in Chinese hamster ovary cell lines.fVIII is a 300 kDa protein which has a heavily glycosylated internal domain containing 20 clustered potential N-linked glycosylation sites.A significant proportion of the expressed fVIII is bound to BiP in the endoplasmic reticulum (ER) in a stable complex andnever secreted. Deletion of the heavily glycosylatedregion results in a lesser degree of association with BiP and increased secretion. Tunicamycin treatmentof cells producing the deleted form of fVIII resultsin stable association of the unglycosylated fVIII with BiP and inhibition of efficient secretion. vWF contains 17 potential N-linked glycosylation sites which are scattered throughout the molecule. vWF is transiently associated with BiP in the ER, demonstrating that CHO cells are competent to saecrete a complex glycoprotein. tPA, which contains 3 utilized N-linked glycosylation sites, exhibits low level association with BiP and is efficiently secreted. Disruptionof normal N-linked glycosylation of tPA, by site directed mutagenesis of the 3 Asn residues to Gin residues or by tunicamycin treatment of the tPA expressing CHO cells, results in reduced levels of secretion and increased association with BiP. This effect is enhanced by high levels of expression. The findings suggest that occupancy of glycosylation sites may effect protein folding and alter secretion efficiency by influencing the extent and stability of association with BiP.
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Higashiyama, S., I. Ohkubo, H. Ishiguro, and M. Sasaki. "A NEW FUNCTION OF HUMAN KININOGENS: THE AMINO-TERMINAL REGION OF DOMAIN 1 INVOLVES AN EF HAND-LIKE STRACTURE FOR METAL BINDING." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642851.
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Two types of kininogens in mammalian plasma, high molecular weight (HMW) and low molecular weight (LMW) kininogens, are the precursors of kinin. Especially, HMW kininogen circulates in the plasma as a complex with prekallikrein and factor XI, and functions as a cofactor in the initial phase reactions of intrinsic blood coagulation cascade. Recently, it has been found that the kininogens have inhibitory activity toward cysteine proteinases. The heavy chain portion, which is identical for HMW and LMW kininogens, is composed of three domains, domain 1, 2 and 3. Each the domain 2 and 3 has a reactive site as a cysteine proteinase inhibitor. However, physiological function of domain 1 remains still unknown. By using the antibody recognizing the interaction between HMW kininogen and Ca2+ (anti-HMW kininogen-Ca2+ antibody) as a probe, we newly found the Ca2+ binding site in the domain 1.Anti-HMW kininogen-Ca2+ antibody was isolated from anti-HMW kininogen antiserum as an antibody which bound to a HMW kininogen-Sepharose column equilibrated with 40 mM Tris-HCl buffer, pH 7.5, containing 1.0 M NaCl and 1 mM CaCl2, and was eluted with 3 mM EDTA. Resulting from the characterization by ELISA, this antibody specifically recognized the CB-1 region (CNBr-cleavage fragment 1: 1-160 amino acid sequence) of the heavy chain of kininogen molecules in the presence of Ca2+ or Mg2+. Furthermore, circular dichroism (CD) experiments showed that the conformational changes of HMW kininogen and heavy chain were induced by the addition of metal ions such as Ca2+ or Mg2+, and that this change was due to the conformational change of the CB-1 region. The dissociation constant (Kd) for heavy chain measured by Ca2+ titration analysis by CD at 214 nm was found to be 0.33 ± 0.09 mM. The number of Ca2+ binding sites of heavy chain calculated from Hill plot was 1.15 ± 0.04. The EF handlike structure found in the amino-terminal portion of the heavy chain of kininogen molecules strongly supported the above data. This indicates a possibility that kininogens play an important role as a Ca2+ binding protein.
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Uzan, G., A. Lajmanovich, M. H. Prandini, Ph Frachet, A. Duperray, and G. Marguerie. "MOLECULAR CLONING OF PLATELET GPIIb FROM HEL CELLS AND HUMAN MEGAKARYOCYTES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643960.
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Platelet GP IIb-IIIa is an heterodimer which functions as a receptor for fibrinogen, fibronectin and Von Willebrand factor and is implicated in platelet adhesive reactions. To study the structure function relationship of this glycoprotein, a recombinant DNA approach was initiated. cDNA expression libraries were constructed in » gtll vector, from erythro-leukemia cells (HEL) and megakaryocytes mRNA. The human megakaryocytes were isolated from patients with chronic myeloid leukemia. The HEL library was initially screened with polyclonal antibodies anti GPIIb IIIa. One clone, λIIbI, containing a 1.65 kbp insert reacted with a panel of different polyclonal antibodies anti GPIIb IIIa and a monoclonal antibody anti GPIIb. To further characterize this clone the synthesis of the fusion protein was induced by IPTG. The bacterial protein was then blotted onto nitro cellulose and incubated with antisera anti GPIIb-IIIa. Antibodies that specifically bound with the fusion protein were eluted and tested on platelet membrane extracts. The selected antibodies produced a positive signal at the GPIIb position similar to the signal produced by the monoclonal antibody anti GPIIb on the same membrane extract. Finally on western blotting, a protein of Mr= 170kD reacted with the monoclonal antibody anti GPIIb. λIIbI insert was used to screen the megakaryocyte library and 3 clones, λIIb2,λIIb3 and λIIb4 were isolated. The size of HEL cells and megakaryocytes GPIIb mRNA was estimated by northern blotting. Only one species of 3.9 kb was identified in both cells. The four different clones accounted for 50% of the coding sequence of this mRNA.Sequencing of these cDNAs indicated that the plasmatic domain of GPIIb contains a cystein rich region. The sequence of these clones will allow the study of the adhesines genetic diversity in different cellular systems.
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Shattil, S. J., J. A. Hoxie, M. Cunningham, C. S. Abrahms, J. O’Brien, and Z. Budzynski. "DETECTION OF ACTIVATED PLATELETS IN WHOLE BLOOD BY FLOW CYTOMETRY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643830.
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Platelets may become activated in a number of clinical disorders and participate in thrombus formation. We have developed a direct test for activated platelets in whole blood that utilizes dual-color flow cytometry and requires no washing steps. Platelets were distinguished from erythrocytes and white blood cells in the flow cytometer by labeling the platelets with biotin-AP1, an antibody specific for membrane glycoprotein lb, and analyzing the cells for phycoerythrin-streptavidin fluorescence. Membrane surface changes resulting from platelet activation were detected with three different FITC-labeled monoclonal antibodies: 1) PAC1, an antibody specific for the fibrinogen receptor on activated platelets; 2) 9F9, which binds to the D-domain of fibrinogen and detects platelet-bound fibrinogen; and 3) S12, which binds to an alpha-granule membrane protein that associates with the platelet surface during secretion. Unstimulated platelets demonstrated no PAC1, 9F9, or S12-specific fluorescence, indicating that they did not bind these antibodies. Upon stimulation with agonists, however, the platelets demonstrated a dose-dependent increase in FITC-fluorescence. The binding of 9F9 to activated platelets required fibrinogen. Low concentrations of ADP and epinephrine, which induce fibrinogen receptors but little secretion, stimulated near-maximal PAC1 or 9F9 binding but little S12 binding. On the other hand, a concentration of phorbol myristate acetate that evokes full platelet aggregation and secretion induced maximal binding of all three antibodies. When blood samples containing activated and non-activated platelets were mixed, as few as 0.8% activated platelets could be detected by this technique. There was a direct correlation between ADP-induced FITC-PAC1 binding and binding determined in a conventional 125I-PAC1 binding assay (r = 0.99; p < 0.001). These studies demonstrate that activated platelets can be reliably detected in whole blood using activation-dependent monoclonal antibodies and flow cytometry. This method may be useful to assess the degree of platelet activation and the efficacy platelet inhibitor therapy in thrombotic disorders.
Reports on the topic "Pyrin Domain-Containing 3 Protein"
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Barg, Rivka, Erich Grotewold, and Yechiam Salts. Regulation of Tomato Fruit Development by Interacting MYB Proteins. United States Department of Agriculture, 2012. http://dx.doi.org/10.32747/2012.7592647.bard.
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Background to the topic: Early tomato fruit development is executed via extensive cell divisions followed by cell expansion concomitantly with endoreduplication. The signals involved in activating the different modes of growth during fruit development are still inadequately understood. Addressing this developmental process, we identified SlFSM1 as a gene expressed specifically during the cell-division dependent stages of fruit development. SlFSM1 is the founder of a class of small plant specific proteins containing a divergent SANT/MYB domain (Barg et al 2005). Before initiating this project, we found that low ectopic over-expression (OEX) of SlFSM1 leads to a significant decrease in the final size of the cells in mature leaves and fruits, and the outer pericarp is substantially narrower, suggesting a role in determining cell size and shape. We also found the interacting partners of the Arabidopsis homologs of FSM1 (two, belonging to the same family), and cloned their tomato single homolog, which we named SlFSB1 (Fruit SANT/MYB–Binding1). SlFSB1 is a novel plant specific single MYB-like protein, which function was unknown. The present project aimed at elucidating the function and mode of action of these two single MYB proteins in regulating tomato fruit development. The specific objectives were: 1. Functional analysis of SlFSM1 and its interacting protein SlFSB1 in relation to fruit development. 2. Identification of the SlFSM1 and/or SlFSB1 cellular targets. The plan of work included: 1) Detailed phenotypic, histological and cellular analyses of plants ectopically expressing FSM1, and plants either ectopically over-expressing or silenced for FSB1. 2) Extensive SELEX analysis, which did not reveal any specific DNA target of SlFSM1 binding, hence the originally offered ChIP analysis was omitted. 3) Genome-wide transcriptional impact of gain- and loss- of SlFSM1 and SlFSB1 function by Affymetrix microarray analyses. This part is still in progress and therefore results are not reported, 4) Search for additional candidate partners of SlFSB1 revealed SlMYBI to be an alternative partner of FSB1, and 5) Study of the physical basis of the interaction between SlFSM1 and SlFSB1 and between FSB1 and MYBI. Major conclusions, solutions, achievements: We established that FSM1 negatively affects cell expansion, particularly of those cells with the highest potential to expand, such as the ones residing inner to the vascular bundles in the fruit pericarp. On the other hand, FSB1 which is expressed throughout fruit development acts as a positive regulator of cell expansion. It was also established that besides interacting with FSM1, FSB1 interacts also with the transcription factor MYBI, and that the formation of the FSB1-MYBI complex is competed by FSM1, which recognizes in FSB1 the same region as MYBI does. Based on these findings a model was developed explaining the role of this novel network of the three different MYB containing proteins FSM1/FSB1/MYBI in the control of tomato cell expansion, particularly during fruit development. In short, during early stages of fruit development (Phase II), the formation of the FSM1-FSB1 complex serves to restrict the expansion of the cells with the greatest expansion potential, those non-dividing cells residing in the inner mesocarp layers of the pericarp. Alternatively, during growth phase III, after transcription of FSM1 sharply declines, FSB1, possibly through complexing with the transcription factor MYBI serves as a positive regulator of the differential cell expansion which drives fruit enlargement during this phase. Additionally, a novel mechanism was revealed by which competing MYB-MYB interactions could participate in the control of gene expression. Implications, both scientific and agricultural: The demonstrated role of the FSM1/FSB1/MYBI complex in controlling differential cell growth in the developing tomato fruit highlights potential exploitations of these genes for improving fruit quality characteristics. Modulation of expression of these genes or their paralogs in other organs could serve to modify leaf and canopy architecture in various crops.
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Splitter, Gary, and Menachem Banai. Microarray Analysis of Brucella melitensis Pathogenesis. United States Department of Agriculture, 2006. http://dx.doi.org/10.32747/2006.7709884.bard.
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Original Objectives 1. To determine the Brucella genes that lead to chronic macrophage infection. 2. To identify Brucella genes that contribute to infection. 3. To confirm the importance of Brucella genes in macrophages and placental cells by mutational analysis. Background Brucella spp. is a Gram-negative facultative intracellular bacterium that infects ruminants causing abortion or birth of severely debilitated animals. Brucellosis continues in Israel, caused by B. melitensis despite an intensive eradication campaign. Problems with the Rev1 vaccine emphasize the need for a greater understanding of Brucella pathogenesis that could improve vaccine designs. Virulent Brucella has developed a successful strategy for survival in its host and transmission to other hosts. To invade the host, virulent Brucella establishes an intracellular niche within macrophages avoiding macrophage killing, ensuring its long-term survival. Then, to exit the host, Brucella uses placenta where it replicates to high numbers resulting in abortion. Also, Brucella traffics to the mammary gland where it is secreted in milk. Missing from our understanding of brucellosis is the surprisingly lillie basic information detailing the mechanisms that permit bacterial persistence in infected macrophages (chronic infection) and dissemination to other animals from infected placental cells and milk (acute infection). Microarray analysis is a powerful approach to determine global gene expression in bacteria. The close genomic similarities of Brucella species and our recent comparative genomic studies of Brucella species using our B. melitensis microarray, suqqests that the data obtained from studying B. melitensis 16M would enable understanding the pathogenicity of other Brucella organisms, particularly the diverse B. melitensis variants that confound Brucella eradication in Israel. Conclusions Results from our BARD studies have identified previously unknown mechanisms of Brucella melitensis pathogenesis- i.e., response to blue light, quorum sensing, second messenger signaling by cyclic di-GMP, the importance of genomic island 2 for lipopolysaccharide in the outer bacterial membrane, and the role of a TIR domain containing protein that mimics a host intracellular signaling molecule. Each one of these pathogenic mechanisms offers major steps in our understanding of Brucella pathogenesis. Strikingly, our molecular results have correlated well to the pathognomonic profile of the disease. We have shown that infected cattle do not elicit antibodies to the organisms at the onset of infection, in correlation to the stealth pathogenesis shown by a molecular approach. Moreover, our field studies have shown that Brucella exploit this time frame to transmit in nature by synchronizing their life cycle to the gestation cycle of their host succumbing to abortion in the last trimester of pregnancy that spreads massive numbers of organisms in the environment. Knowing the bacterial mechanisms that contribute to the virulence of Brucella in its host has initiated the agricultural opportunities for developing new vaccines and diagnostic assays as well as improving control and eradication campaigns based on herd management and linking diagnosis to the pregnancy status of the animals. Scientific and Agricultural Implications Our BARD funded studies have revealed important Brucella virulence mechanisms of pathogenesis. Our publication in Science has identified a highly novel concept where Brucella utilizes blue light to increase its virulence similar to some plant bacterial pathogens. Further, our studies have revealed bacterial second messengers that regulate virulence, quorum sensing mechanisms permitting bacteria to evaluate their environment, and a genomic island that controls synthesis of its lipopolysaccharide surface. Discussions are ongoing with a vaccine company for application of this genomic island knowledge in a Brucella vaccine by the U.S. lab. Also, our new technology of bioengineering bioluminescent Brucella has resulted in a spin-off application for diagnosis of Brucella infected animals by the Israeli lab by prioritizing bacterial diagnosis over serological diagnosis.