Academic literature on the topic 'Syndecan interaction'
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Journal articles on the topic "Syndecan interaction"
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Hudák, Anett, Annamária Letoha, László Szilák, and Tamás Letoha. "Contribution of Syndecans to the Cellular Entry of SARS-CoV-2." International Journal of Molecular Sciences 22, no. 10 (May 19, 2021): 5336. http://dx.doi.org/10.3390/ijms22105336.
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The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a novel emerging pathogen causing an unprecedented pandemic in 21st century medicine. Due to the significant health and economic burden of the current SARS-CoV-2 outbreak, there is a huge unmet medical need for novel interventions effectively blocking SARS-CoV-2 infection. Unknown details of SARS-CoV-2 cellular biology hamper the development of potent and highly specific SARS-CoV-2 therapeutics. Angiotensin-converting enzyme-2 (ACE2) has been reported to be the primary receptor for SARS-CoV-2 cellular entry. However, emerging scientific evidence suggests the involvement of additional membrane proteins, such as heparan sulfate proteoglycans, in SARS-CoV-2 internalization. Here, we report that syndecans, the evolutionarily conserved family of transmembrane proteoglycans, facilitate the cellular entry of SARS-CoV-2. Among syndecans, the lung abundant syndecan-4 was the most efficient in mediating SARS-CoV-2 uptake. The S1 subunit of the SARS-CoV-2 spike protein plays a dominant role in the virus’s interactions with syndecans. Besides the polyanionic heparan sulfate chains, other parts of the syndecan ectodomain, such as the cell-binding domain, also contribute to the interaction with SARS-CoV-2. During virus internalization, syndecans colocalize with ACE2, suggesting a jointly shared internalization pathway. Both ACE2 and syndecan inhibitors exhibited significant efficacy in reducing the cellular entry of SARS-CoV-2, thus supporting the complex nature of internalization. Data obtained on syndecan specific in vitro assays present syndecans as novel cellular targets of SARS-CoV-2 and offer molecularly precise yet simple strategies to overcome the complex nature of SARS-CoV-2 infection.
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Hudák, Anett, Katalin Jósvay, Ildikó Domonkos, Annamária Letoha, László Szilák, and Tamás Letoha. "The Interplay of Apoes with Syndecans in Influencing Key Cellular Events of Amyloid Pathology." International Journal of Molecular Sciences 22, no. 13 (June 30, 2021): 7070. http://dx.doi.org/10.3390/ijms22137070.
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Apolipoprotein E (ApoE) isoforms exert intricate effects on cellular physiology beyond lipid transport and metabolism. ApoEs influence the onset of Alzheimer’s disease (AD) in an isoform-dependent manner: ApoE4 increases AD risk, while ApoE2 decreases it. Previously we demonstrated that syndecans, a transmembrane proteoglycan family with increased expression in AD, trigger the aggregation and modulate the cellular uptake of amyloid beta (Aβ). Utilizing our previously established syndecan-overexpressing cellular assays, we now explore how the interplay of ApoEs with syndecans contributes to key events, namely uptake and aggregation, in Aβ pathology. The interaction of ApoEs with syndecans indicates isoform-specific characteristics arising beyond the frequently studied ApoE–heparan sulfate interactions. Syndecans, and among them the neuronal syndecan-3, increased the cellular uptake of ApoEs, especially ApoE2 and ApoE3, while ApoEs exerted opposing effects on syndecan-3-mediated Aβ uptake and aggregation. ApoE2 increased the cellular internalization of monomeric Aβ, hence preventing its extracellular aggregation, while ApoE4 decreased it, thus helping the buildup of extracellular plaques. The contrary effects of ApoE2 and ApoE4 remained once Aβ aggregated: while ApoE2 reduced the uptake of Aβ aggregates, ApoE4 facilitated it. Fibrillation studies also revealed ApoE4′s tendency to form fibrillar aggregates. Our results uncover yet unknown details of ApoE cellular biology and deepen our molecular understanding of the ApoE-dependent mechanism of Aβ pathology.
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Palomino, Rafael, Hsiau-Wei Lee, and Glenn L. Millhauser. "The agouti-related peptide binds heparan sulfate through segments critical for its orexigenic effects." Journal of Biological Chemistry 292, no. 18 (March 6, 2017): 7651–61. http://dx.doi.org/10.1074/jbc.m116.772822.
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Syndecans potently modulate agouti-related peptide (AgRP) signaling in the central melanocortin system. Through heparan sulfate moieties, syndecans are thought to anchor AgRP near its receptor, enhancing its orexigenic effects. Original work proposed that the N-terminal domain of AgRP facilitates this interaction. However, this is not compatible with evidence that this domain is posttranslationally cleaved. Addressing this long-standing incongruity, we used calorimetry and magnetic resonance to probe interactions of AgRP peptides with glycosaminoglycans, including heparan sulfate. We show that mature, cleaved, C-terminal AgRP, not the N-terminal domain, binds heparan sulfate. NMR shows that the binding site consists of regions distinct from the melanocortin receptor-binding site. Using a library of designed AgRP variants, we find that the strength of the syndecan interaction perfectly tracks orexigenic action. Our data provide compelling evidence that AgRP is a heparan sulfate-binding protein and localizes critical regions in the AgRP structure required for this interaction.
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Baston-Buest, Dunja Maria, Olga Altergot-Ahmad, Sarah Jean Pour, Jan-Steffen Krüssel, Udo Rudolf Markert, Tanja Natascha Fehm, and Alexandra Petra Bielfeld. "Syndecan-1 Acts as an Important Regulator of CXCL1 Expression and Cellular Interaction of Human Endometrial Stromal and Trophoblast Cells." Mediators of Inflammation 2017 (2017): 1–14. http://dx.doi.org/10.1155/2017/8379256.
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Successful implantation of the embryo into the human receptive endometrium is substantial for the establishment of a healthy pregnancy. This study focusses on the role of Syndecan-1 at the embryo-maternal interface, the multitasking coreceptor influencing ligand concentration, release and receptor presentation, and cellular morphology. CXC motif ligand 1, being involved in chemotaxis and angiogenesis during implantation, is of special interest as a ligand of Syndecan-1. Human endometrial stromal cells with and without Syndecan-1 knock-down were decidualized and treated with specific inhibitors to evaluate signaling pathways regulating CXC ligand 1 expression. Western blot analyses of MAPK and Wnt members were performed, followed by analysis of spheroid interactions between human endometrial cells and extravillous trophoblast cells. By mimicking embryo contact using IL-1β, we showed less ERK and c-Jun activation by depletion of Syndecan-1 and less Frizzled 4 production as part of the canonical Wnt pathway. Additionally, more beta-catenin was phosphorylated and therefore degraded after depletion of Syndecan-1. Secretion of CXC motif ligand 1 depends on MEK-1 with respect to Syndecan-1. Regarding the interaction of endometrial and trophoblast cells, the spheroid center-to-center distances were smaller after depletion of Syndecan-1. Therefore, Syndecan-1 seems to affect signaling processes relevant to signaling and intercellular interaction at the trophoblast-decidual interface.
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Vainio, S., M. Jalkanen, and I. Thesleff. "Syndecan and tenascin expression is induced by epithelial-mesenchymal interactions in embryonic tooth mesenchyme." Journal of Cell Biology 108, no. 5 (May 1, 1989): 1945–53. http://dx.doi.org/10.1083/jcb.108.5.1945.
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Morphogenesis of embryonic organs is regulated by epithelial-mesenchymal interactions associating with changes in the extracellular matrix (ECM). The response of the cells to the changes in the ECM must involve integral cell surface molecules that recognize their matrix ligand and initiate transmission of signal intracellularly. We have studied the expression of the cell surface proteoglycan, syndecan, which is a matrix receptor for epithelial cells (Saunders, S., M. Jalkanen, S. O'Farrell, and M. Bernfield. J. Cell Biol. In press.), and the matrix glycoprotein, tenascin, which has been proposed to be involved in epithelial-mesenchymal interactions (Chiquet-Ehrismann, R., E. J. Mackie, C. A. Pearson, and T. Sakakura. 1986. Cell. 47:131-139) in experimental tissue recombinations of dental epithelium and mesenchyme. Our earlier studies have shown that in mouse embryos both syndecan and tenascin are intensely expressed in the condensing dental mesenchyme surrounding the epithelial bud (Thesleff, I., M. Jalkanen, S. Vainio, and M. Bernfield. 1988. Dev. Biol. 129:565-572; Thesleff, I., E. Mackie, S. Vainio, and R. Chiquet-Ehrismann. 1987. Development. 101:289-296). Analysis of rat-mouse tissue recombinants by a monoclonal antibody against the murine syndecan showed that the presumptive dental epithelium induces the expression of syndecan in the underlying mesenchyme. The expression of tenascin was induced in the dental mesenchyme in the same area as syndecan. The syndecan and tenascin positive areas increased with time of epithelial-mesenchymal contact. Other ECM molecules, laminin, type III collagen, and fibronectin, did not show a staining pattern similar to that of syndecan and tenascin. Oral epithelium from older embryos had lost its ability to induce syndecan expression but the presumptive dental epithelium induced syndecan expression even in oral mesenchyme of older embryos. Our results indicate that the expression of syndecan and tenascin in the tooth mesenchyme is regulated by epithelial-mesenchymal interactions. Because of their early appearance, syndecan and tenascin may be used to study the molecular regulation of this interaction. The similar distribution patterns of syndecan and tenascin in vivo and in vitro and their early appearance as a result of epithelial-mesenchymal interaction suggest that these molecules may be involved in the condensation and differentiation of dental mesenchymal cells.
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Miettinen, H. M., and M. Jalkanen. "The cytoplasmic domain of syndecan-1 is not required for association with Triton X-100-insoluble material." Journal of Cell Science 107, no. 6 (June 1, 1994): 1571–81. http://dx.doi.org/10.1242/jcs.107.6.1571.
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Cell surface heparan sulfate proteoglycans such as syndecan-1 bind various extracellular matrix proteins and have been suggested to interact with the cytoskeleton. Such interactions are thought to be important for stabilizing cell morphology. Syndecan-1 resists extraction with Triton X-100. This insolubility was reported not to be affected by removal of the glycosaminoglycan chains, suggesting that the insolubility is not due to binding to the extracellular matrix, but rather to an association with the actin cytoskeleton (Rapraeger, A., Jalkanen, M. and Bernfield, M. (1986) J. Cell Biol. 103, 2683–2696). To examine further the interaction of syndecan-1 with the Triton X-100-insoluble residue, we expressed wild-type mouse syndecan-1 and a cytoplasmic deletion mutant (tail-less) in Chinese hamster ovary cells. We observed that both the wild-type and the tail-less syndecan-1 were partly insoluble in Triton X-100. The insolubility was not affected by increasing temperature (37 degrees C or 50 degrees C) or by cytochalasin D. Removal of the glycosaminoglycan chains from the ectodomain, however, resulted in complete Triton X-100 solubility, unlike previous reports. Syndecan-1 could also be released into the Triton X-100-soluble fraction by addition of heparin or heparan sulfate to the extraction medium. We conclude that the cytoplasmic domain of syndecan-1 is not responsible for Triton X-100 insolubility. Instead, our results indicate that Triton X-100 insolubility is caused by an interaction of syndecan-1 molecules with other cellular and/or extracellular molecules mediated by the heparan sulfate chains.
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Ethell, Iryna M., Kazuki Hagihara, Yoshiaki Miura, Fumitoshi Irie, and Yu Yamaguchi. "Synbindin, a Novel Syndecan-2–Binding Protein in Neuronal Dendritic Spines." Journal of Cell Biology 151, no. 1 (October 2, 2000): 53–68. http://dx.doi.org/10.1083/jcb.151.1.53.
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Dendritic spines are small protrusions on the surface of dendrites that receive the vast majority of excitatory synapses. We previously showed that the cell-surface heparan sulfate proteoglycan syndecan-2 induces spine formation upon transfection into hippocampal neurons. This effect requires the COOH-terminal EFYA sequence of syndecan-2, suggesting that cytoplasmic molecules interacting with this sequence play a critical role in spine morphogenesis. Here, we report a novel protein that binds to the EFYA motif of syndecan-2. This protein, named synbindin, is expressed by neurons in a pattern similar to that of syndecan-2, and colocalizes with syndecan-2 in the spines of cultured hippocampal neurons. In transfected hippocampal neurons, synbindin undergoes syndecan-2–dependent clustering. Synbindin is structurally related to yeast proteins known to be involved in vesicle transport. Immunoelectron microscopy localized synbindin on postsynaptic membranes and intracellular vesicles within dendrites, suggesting a role in postsynaptic membrane trafficking. Synbindin coimmunoprecipitates with syndecan-2 from synaptic membrane fractions. Our results show that synbindin is a physiological syndecan-2 ligand on dendritic spines. We suggest that syndecan-2 induces spine formation by recruiting intracellular vesicles toward postsynaptic sites through the interaction with synbindin.
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Sanderson, R. D., T. B. Sneed, L. A. Young, G. L. Sullivan, and A. D. Lander. "Adhesion of B lymphoid (MPC-11) cells to type I collagen is mediated by integral membrane proteoglycan, syndecan." Journal of Immunology 148, no. 12 (June 15, 1992): 3902–11. http://dx.doi.org/10.4049/jimmunol.148.12.3902.
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Abstract Differentiating B lymphocytes undergo changes in cell-cell and cell-matrix adhesion that control their movement through a series of distinct microenvironments. The integral membrane proteoglycan, syndecan, is a candidate for mediating B lymphocyte-matrix interactions because it is expressed on B lymphocytes only at times when they associate with matrix, and because syndecan is known to behave as a matrix receptor on simple epithelia. However, syndecan from B lymphocytes is significantly smaller in molecular mass than syndecan from simple epithelia (85 vs 160 kDa) suggesting that syndecan may have distinct functions on these two cell types. Our study was undertaken to determine if syndecan mediates adhesion of B lineage cells to extracellular matrix. The murine myeloma cell line MPC-11 was used because syndecan is the only major heparan sulfate proteoglycan detected on these cells and because they express a form of syndecan almost identical to that found on normal B lymphocytes. Cell binding assays demonstrate that syndecan binds MPC-11 cells to type I collagen. Binding is inhibited by heparin, by pretreatment of cells with heparitinase or by growth of cells before the assay in chlorate, an inhibitor of sulfation. Solid phase assays show that syndecan purified from MPC-11 cells binds to type I collagen but not type IV collagen, laminin, or fibronectin. The interaction of MPC-11-derived syndecan with type I collagen is of relatively high affinity (Kd app = 143 nM) as measured by affinity coelectrophoresis. However, the 160-kDa form of syndecan isolated from epithelial cells has a greater than fourfold higher affinity for type I collagen (Kd app = 31 nM) than does the MPC-11 syndecan, suggesting that different molecular forms of syndecan have distinct ligand binding properties. These results demonstrate that syndecan can mediate B lymphocyte interactions with matrix and suggest that changes in syndecan expression during B cell differentiation are a mechanism for controlling B cell localization within specific microenvironments.
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Carulli, Sonia, Konrad Beck, Guila Dayan, Sophie Boulesteix, Hugues Lortat-Jacob, and Patricia Rousselle. "Cell Surface Proteoglycans Syndecan-1 and -4 Bind Overlapping but Distinct Sites in Laminin α3 LG45 Protein Domain." Journal of Biological Chemistry 287, no. 15 (February 20, 2012): 12204–16. http://dx.doi.org/10.1074/jbc.m111.300061.
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Keratinocyte migration during epidermal repair depends on interactions between cellular heparan sulfate proteoglycan receptors, syndecan-1 and -4, and the C-terminal globular domains (LG45) of the extracellular matrix protein laminin 332. This study investigates the molecular basis of the binding specificity of the syndecan-1 and -4 receptors expressed by human keratinocytes. We used site-directed mutagenesis to alter a recombinant LG45 protein by substituting the most critical basic residues with glutamine. All proteins were expressed in mammalian cells, purified, and characterized biochemically. We used in vitro binding assays, including surface plasmon resonance, to examine interactions between mutated LG45 and heparan sulfates, syndecan-1 and -4. We identify a major heparin binding domain on the outer edge of a β-strand of LG45 surrounded by a track of converging low affinity residues. This domain harbors distinctive syndecan-1 and -4 binding-specific sequences. This is the first study to demonstrate a binding specificity of two proteoglycans produced by a single cell type. In addition, we found that although syndecan-1 interacts exclusively through its glycosaminoglycan chains, syndecan-4 binding relies on both its core protein and its heparan sulfate chains. These results suggest that LG45 may trigger different signals toward keratinocytes depending on its interaction with syndecan-1 or -4.
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Munesue, Seiichi, Yasuo Yoshitomi, Yuri Kusano, Yoshie Koyama, Akiko Nishiyama, Hayao Nakanishi, Kaoru Miyazaki, et al. "A Novel Function of Syndecan-2, Suppression of Matrix Metalloproteinase-2 Activation, Which Causes Suppression of Metastasis." Journal of Biological Chemistry 282, no. 38 (July 10, 2007): 28164–74. http://dx.doi.org/10.1074/jbc.m609812200.
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The syndecans comprise a family of cell surface heparan sulfate proteoglycans exhibiting complex biological functions involving the interaction of heparan sulfate side chains with a variety of soluble and insoluble heparin-binding extracellular ligands. Here we demonstrate an inverse correlation between the expression level of syndecan-2 and the metastatic potential of three clones derived from Lewis lung carcinoma 3LL. This correlation was proved to be a causal relationship, because transfection of syndecan-2 into the higher metastatic clone resulted in the suppression of both spontaneous and experimental metastases to the lung. Although the expression levels of matrix metalloproteinase-2 (MMP-2) and its cell surface activators, such as membrane-type 1 matrix metalloproteinase and tissue inhibitor of metalloproteinase-2, were similar regardless of the metastatic potentials of the clones, elevated activation of MMP-2 was observed in the higher metastatic clone. Removal of heparan sulfate from the cell surface of low metastatic cells by treatment with heparitinase-I promoted MMP-2 activation, and transfection of syndecan-2 into highly metastatic cells suppressed MMP-2 activation. Furthermore, transfection of mutated syndecan-2 lacking glycosaminoglycan attachment sites into highly metastatic cells did not have any suppressive effect on MMP-2 activation, suggesting that this suppression was mediated by the heparan sulfate side chains of syndecan-2. Actually, MMP-2 was found to exhibit a strong binding ability to heparin, the dissociation constant value being 62 nm. These results indicate a novel function of syndecan-2, which acts as a suppressor for MMP-2 activation, causing suppression of metastasis in at least the metastatic system used in the present study.
Dissertations / Theses on the topic "Syndecan interaction"
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Garcia, Manon. "Développement de nouveaux agents anticancéreux inhibiteurs de la syntenin." Electronic Thesis or Diss., Aix-Marseille, 2021. http://theses.univ-amu.fr.lama.univ-amu.fr/210312_GARCIA_59el396udxeux306vl471dzd_TH.pdf.
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Les travaux de thèse présentés décrivent l’identification et l’optimisation d’inhibiteurs sélectifs du complexe protéique syntenin/syndecan, grâce à une stratégie de « Fragment-based drug design » (FBDD), qui pourrait ouvrir la voie vers de nouvelles thérapies anticancéreuses. L'interaction syntenin/syndecan joue un rôle majeur dans le recyclage des endosomes vers la membrane plasmique, ainsi que dans la biogénèse et la libération des exosomes dérivés de cellules tumorales. Par conséquent, nous avons réalisé un programme de FBDD ciblant sélectivement l’interaction syntenin/syndecan. Pour ce faire, deux criblages différents de chimiothèque de fragments, l’un expérimental l’autre virtuel, ont permis d’identifier deux fragments hits qui inhibent spécifiquement l’interaction du complexe syntenin/syndecan. La résolution des structures cristallographiques 3D des complexes de ces deux fragments avec la syntenin a permis leur optimisation par une approche de "Structure-based drug design" reposant sur les informations obtenues sur le site et le mode de liaison des deux fragments. Des études SAR et des étapes d’optimisation par « fragment growing », basées sur des données de docking moléculaire, ont été réalisés. Mon travail a consisté à synthétiser les chimiothèques d’analogues ciblés issus du docking moléculaire et démontrant de fortes interactions avec la syntenin. Parmi tous les analogues synthétisés, nous avons identifiés les inhibiteurs les plus prometteurs qui présentent des IC50 de l’ordre du sub-micromolaire et qui affectent la voie de libération des exosomes dérivés de cellules tumorales, dépendant de l’activité syntenin/syndecanThe thesis describes the identification and optimization of selective inhibitors targeting the syntenin/syndecan complex, using a “Fragment-based drug design” (FBDD) strategy, which could pave the way for new anticancer therapies. The syntenin/syndecan interaction plays a major role in the recycling of endosomes to the plasma membrane, as well as in the biogenesis and release of exosomes derived from tumor cells. Therefore, we performed an FBDD program targeting selectively the syntenin/syndecan interaction. To do this, two different fragment library screenings were performed, one experimental the other virtual, and two fragments hits were identified that specifically inhibit the interaction of the syntenin/syndecan complex. The resolution of 3D crystallographic structures of the complexes between these two fragments and syntenin allowed their optimization by a structure-based drug design approach based on information about their binding site and the mode. SAR studies and fragment growing optimization steps, based on molecular docking studies, were carried out. My work consisted in synthesizing chemical libraries of targeted analogues resulting from molecular docking and demonstrating strong interactions with syntenin. Among all the synthesized analogues, we identified the most promising inhibitors which exhibit sub-micromolar IC50 and which affect the release pathway of exosomes derived from tumor cells, dependent on syntenin/syndecan activity
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Kaksonen, Marko. "Syndecan-3 in neural plasticity : from cell surface interactions to cytoskeletal regulation." Helsinki : University of Helsinki, 2002. http://ethesis.helsinki.fi/julkaisut/mat/bioti/vk/kaksonen/.
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Molteni, Alexandra. "Interactions entre proteoglycannes sulfates et facteur de croissance fibroblastique-2 dans la chondro-osteogenese du condyle mandibulaire et l'osteogenese de la calotte cranienne de rat." Paris 5, 1998. http://www.theses.fr/1998PA05M106.
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Huang, Jin-Wen, and 黃勁文. "The functional role of syndecan-2 in the molecular interaction with RACK1 in cells." Thesis, 2006. http://ndltd.ncl.edu.tw/handle/37579606587413121193.
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碩士國立臺灣大學
動物學研究研究所
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In this study, RACK1 (Receptor for Activated C Kinase 1) was found to be reactive with syndecan-2 in vitro and in vivo. Through affinity column chromatography and immunoprecipitation analysis as well as immunocytochemical colocalization studies, the reaction between RACK1 and syndecan-2 was evidenced in BALB/3T3 cells. Recombinant syndecan-2 and PEP Syn-2-cyto were applied to demonstrate that tyrosine 180 of syndecan-2 is a targeted site for Src tyrosine kinase and the reaction with RACK1 is enhanced after this tyrosine phosphorylation. In parallel, when granulocyte-macrophage colony-stimulating factor (GM-CSF) was applied to activate cellular tyrosine kinase of HeLa cells, a significant positive interaction was revealed between syndecan-2 and RACK1 with time and dose-dependence. HeLa cells were further subject to transfections with wild type and mutant syndecan-2 vectors(Syn-2-Y180F、Syn-2-Y192F、Syn-2-Y180/192F) to show that the reaction of syndecan-2 with RACK1 was suppressed when tyrosine 180 phosphorylation site was absent. To elucidate the physiological significance of this selective reaction between syndecan-2 and RACK1, studies with adhesion, migration, and poliferation were focused. HeLa cells transfected with Syn-2-Y180F mutant vectors exhibited less motile and adhesion ability. Furthermore, the morphology of Syn-2-Y180F transfants became round and refractile. These results imply that tyrosine 180 of syndecan-2 may involve in the cytoskeleton organization, focal contacts formation, and tyrosine kinase regulation through selective reaction with RACK1.
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McFall, Aidan J. "Molecular interactions of the extracellular protein domain of syndecan-4." 1998. http://catalog.hathitrust.org/api/volumes/oclc/40737394.html.
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Thesis (Ph. D.)--University of Wisconsin--Madison, 1998.Typescript. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 168-185).
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Dews, Ian Charles. "Characterization of transmembrane domain interactions by the syndecan family of integral membrane proteins." Thesis, 2008. http://hdl.handle.net/1911/22270.
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Protein-protein interactions between the transmembrane domains (TMDs) of integral membrane proteins have been increasingly implicated in contributing to biological function. In this thesis, I explore the strength, specificity and sequence dependence of interactions made by the TMDs of the syndecans, a family of four human cell adhesion molecules. Primary sequence alignment of all known syndecan TMDs reveals a completely conserved GxxxG dimerization motif. This motif has been shown to drive dimerization of many biological TMDs, and its strong conservation within the syndecan family would seem to suggest that all syndecans will display a common self-association phenotype. In contrast to this expectation, I show that the syndecan TMDs display a hierarchy of association phenotypes, with the syndecan-1 TMD showing very weak dimerization, the syndecan-3 and -4 TMDs showing strong dimerization, and the syndecan-2 TMD showing very strong dimerization. I further show that oligomerization of the syndecan TMDs depends upon the sequence element GxxxGxxxA, which is also conserved across all known syndecans. Using single and double point mutations, show that residue identities at two positions flanking the GxxxGxxxA motif combine to produce much of the difference in self-association strengths across syndecan paralogs. Residue identities at these intervening positions are different between paralogs but strongly conserved across orthologs, indicating an evolutionary pressure to maintain the hierarchy of association phenotypes. I further show that each syndecan TMD is capable of forming heteromeric complexes with at least two other paralogs and that these interactions are also supported by the GxxxG motif. The strength and stoichiometry of the heteromeric interactions are also paralog specific, meaning that residues in addition to the GxxxG motif are responsible for directing these interactions. These findings show that, although all syndecans possess a GxxxGxxxA sequence element that supports oligomerization, additional residues modulate the strength and stoichiometry of both homo- and heterotypic interactions. The strong conservation of residues that give rise to paralog specific homo- and heterotypic interactions suggests that the complexity of these interactions may play a role in mediating syndecan functions.
Books on the topic "Syndecan interaction"
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Grootjans, Jan Johann. Cytoplasmic interactions of the syndecans. Leuven: Leuven University Press, 2000.
Find full textConference papers on the topic "Syndecan interaction"
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Risquez, Cristobal F., Avignat Patel, Juan C. Osorio, Isis E. Fernandez, Andrew Goodwin, Ying Shi, Xiaomeng Tang, Danielle Morse, Ivan O. Rosas, and Yuanyuan Shi. "Syndecan-2 And CCL2 Interactions Promote Alveolar Macrophage Recruitment During Acute Lung Injury." 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.a3700.
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Shi, Yuanyuan, Isis Fernandez, Guoying Yu, Jiaofei Cao, Zhihua Chen, Zhijian Gao, Gustavo Pacheco-Rodriguez, Stefan W. Ryter, Danielle Morse, and Ivan O. Rosas. "Syndecan-2 Dependent Scavenging Of TGF-²1 Via Caveolin-1 And TGF-²RI Interactions In Human Monocytes." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a3524.
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