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Journal articles on the topic 'Syndecan interaction'

Author: Grafiati

Published: 25 May 2024

Last updated: 31 July 2025

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1

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 (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

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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 (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

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3

Baston-Buest, Dunja Maria, Olga Altergot-Ahmad, Sarah Jean Pour, et al. "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

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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 (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

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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 (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 propos

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Støle, Thea Parsberg, Marianne Lunde, Katja Gehmlich, Geir Christensen, William E. Louch, and Cathrine Rein Carlson. "Exploring Syndecan-4 and MLP and Their Interaction in Primary Cardiomyocytes and H9c2 Cells." Cells 13, no. 11 (2024): 947. http://dx.doi.org/10.3390/cells13110947.

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The transmembrane proteoglycan syndecan-4 is known to be involved in the hypertrophic response to pressure overload. Although multiple downstream signaling pathways have been found to be involved in this response in a syndecan-4-dependent manner, there are likely more signaling components involved. As part of a larger syndecan-4 interactome screening, we have previously identified MLP as a binding partner to the cytoplasmic tail of syndecan-4. Interestingly, many human MLP mutations have been found in patients with hypertrophic (HCM) and dilated cardiomyopathy (DCM). To gain deeper insight int

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7

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 (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,

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8

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 (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 s

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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 (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 synde

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10

Carulli, Sonia, Konrad Beck, Guila Dayan, Sophie Boulesteix, Hugues Lortat-Jacob та 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, № 15 (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 biochemica

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11

Munesue, Seiichi, Yasuo Yoshitomi, Yuri Kusano, 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 (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

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Couchman, John R., Susan Vogt, Ssang-Taek Lim, et al. "Regulation of Inositol Phospholipid Binding and Signaling through Syndecan-4." Journal of Biological Chemistry 277, no. 51 (2002): 49296–303. http://dx.doi.org/10.1074/jbc.m209679200.

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Syndecan-4 is a transmembrane heparan sulfate proteoglycan that can regulate cell-matrix interactions and is enriched in focal adhesions. Its cytoplasmic domain contains a central region unlike that of any other vertebrate or invertebrate syndecan core protein with a cationic motif that binds inositol phospholipids. In turn, lipid binding stabilizes the syndecan in oligomeric form, with subsequent binding and activation of protein kinase C. The specificity of phospholipid binding and its potential regulation are investigated here. Highest affinity of the syndecan-4 cytoplasmic domain was seen

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13

KEUM, Eunyoung, Yeonhee KIM, Jungyean KIM, et al. "Syndecan-4 regulates localization, activity and stability of protein kinase C-alpha." Biochemical Journal 378, no. 3 (2004): 1007–14. http://dx.doi.org/10.1042/bj20031734.

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During cell–matrix adhesion, syndecan-4 transmembrane heparan sulphate proteoglycan plays a critical role in the formation of focal adhesions and stress fibres. We have shown previously that the syndecan-4 cytoplasmic domain directly binds to and activates PKC-α (protein kinase C-α) in vitro [Oh, Woods and Couchman (1997) J. Biol. Chem. 272, 8133–8136]. However, whether syndecan-4 has the same activity in vivo needs to be addressed. Using mammalian two-hybrid assays, we showed that syndecan-4 interacted with PKC-α in vivo and that this interaction was mediated through syndecan-4 cytoplasmic do

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BASS, Mark D., and Martin J. HUMPHRIES. "Cytoplasmic interactions of syndecan-4 orchestrate adhesion receptor and growth factor receptor signalling." Biochemical Journal 368, no. 1 (2002): 1–15. http://dx.doi.org/10.1042/bj20021228.

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Syndecan-4 is a ubiquitous transmembrane proteoglycan that localizes to the focal adhesions of adherent cells and binds to a range of extracellular ligands, including growth factors and extracellular-matrix proteins. Engagement of syndecan-4 is essential for adhesion formation in cells adhering via certain integrins, and for cell proliferation and migration in response to growth factors. The cytoplasmic domain of syndecan-4 interacts with a number of signalling and structural proteins, and both extracellular and cytoplasmic domains are necessary for regulated activation of associated transmemb

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Wang, Haiyao, Haining Jin, DeannaLee M. Beauvais та Alan C. Rapraeger. "Cytoplasmic Domain Interactions of Syndecan-1 and Syndecan-4 with α6β4 Integrin Mediate Human Epidermal Growth Factor Receptor (HER1 and HER2)-dependent Motility and Survival". Journal of Biological Chemistry 289, № 44 (2014): 30318–32. http://dx.doi.org/10.1074/jbc.m114.586438.

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Epithelial cells are highly dependent during wound healing and tumorigenesis on the α6β4 integrin and its association with receptor tyrosine kinases. Previous work showed that phosphorylation of the β4 subunit upon matrix engagement depends on the matrix receptor syndecan (Sdc)-1 engaging the cytoplasmic domain of the β4 integrin and coupling of the integrin to human epidermal growth factor receptor-2 (HER2). In this study, HER2-dependent migration activated by matrix engagement is compared with migration stimulated by EGF. We find that whereas HER2-dependent migration depends on Sdc1, EGF-dep

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Derksen, Patrick W. B., Robert M. J. Keehnen, Ludo M. Evers, Marinus H. J. van Oers, Marcel Spaargaren, and Steven T. Pals. "Cell surface proteoglycan syndecan-1 mediates hepatocyte growth factor binding and promotes Met signaling in multiple myeloma." Blood 99, no. 4 (2002): 1405–10. http://dx.doi.org/10.1182/blood.v99.4.1405.

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Heparan sulfate proteoglycans (HSPGs) play a crucial role in growth regulation by assembling signaling complexes and presenting growth factors to their cognate receptors. Within the immune system, expression of the HSPG syndecan-1 (CD138) is characteristic of terminally differentiated B cells, ie, plasma cells, and their malignant counterpart, multiple myeloma (MM). This study explored the hypothesis that syndecan-1 might promote growth factor signaling and tumor growth in MM. For this purpose, the interaction was studied between syndecan-1 and hepatocyte growth factor (HGF), a putative paracr

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Baciu, P. C., S. Saoncella, S. H. Lee, F. Denhez, D. Leuthardt, and P. F. Goetinck. "Syndesmos, a protein that interacts with the cytoplasmic domain of syndecan-4, mediates cell spreading and actin cytoskeletal organization." Journal of Cell Science 113, no. 2 (2000): 315–24. http://dx.doi.org/10.1242/jcs.113.2.315.

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Syndecan-4 is a cell surface heparan sulfate proteoglycan which, in cooperation with integrins, transduces signals for the assembly of focal adhesions and actin stress fibers in cells plated on fibronectin. The regulation of these cellular events is proposed to occur, in part, through the interaction of the cytoplasmic domains of these transmembrane receptors with intracellular proteins. To identify potential intracellular proteins that interact with the cytoplasmic domain of syndecan-4, we carried out a yeast two-hybrid screen in which the cytoplasmic domain of syndecan-4 was used as bait. As

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Volta, Manuela, Stefano Calza, Anne M. Roberts, and Roland G. Roberts. "Characterisation of the interaction between syndecan-2, neurofibromin and CASK: Dependence of interaction on syndecan dimerization." Biochemical and Biophysical Research Communications 391, no. 2 (2010): 1216–21. http://dx.doi.org/10.1016/j.bbrc.2009.12.043.

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Choi, Youngsil, Seungin Kim, Junghyun Lee та ін. "The oligomeric status of syndecan-4 regulates syndecan-4 interaction with α-actinin". European Journal of Cell Biology 87, № 10 (2008): 807–15. http://dx.doi.org/10.1016/j.ejcb.2008.04.005.

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20

Cohen, Alexandra R., Daniel F. Wood, Shirin M. Marfatia, Zenta Walther, Athar H. Chishti, and James Melvin Anderson. "Human CASK/LIN-2 Binds Syndecan-2 and Protein 4.1 and Localizes to the Basolateral Membrane of Epithelial Cells." Journal of Cell Biology 142, no. 1 (1998): 129–38. http://dx.doi.org/10.1083/jcb.142.1.129.

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In Caenorhabditis elegans, mutations in the lin-2 gene inactivate the LET-23 receptor tyrosine kinase/Ras/MAP kinase pathway required for vulval cell differentiation. One function of LIN-2 is to localize LET-23 to the basal membrane domain of vulval precursor cells. LIN-2 belongs to the membrane-associated guanylate kinase family of proteins. We have cloned and characterized the human homolog of LIN-2, termed hCASK, and Northern and Western blot analyses reveal that it is ubiquitously expressed. Indirect immunofluorescence localizes CASK to distinct lateral and/or basal plasma membrane domains

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Miftode, Radu-Stefan, Ionela-Lăcrămioara Şerban, Amalia-Stefana Timpau, et al. "Syndecan-1: A Review on Its Role in Heart Failure and Chronic Liver Disease Patients’ Assessment." Cardiology Research and Practice 2019 (November 11, 2019): 1–7. http://dx.doi.org/10.1155/2019/4750580.

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The close connection and interaction between the cardiac and the liver functions are well-known, as cirrhotic cardiomyopathy is an important clinical entity which best describes the mutual pathogenical influence between these two organs. Due to the fact that cardiac dysfunction in patients with chronic hepatic disorders is oligosymptomatic or even asymptomatic, an early diagnosis represents a challenge for every physician. Syndecan-1—a transmembrane proteoglycan that exerts its functions mainly via its heparane sulfate chains—is a very promising biomarker, correlated not only with the degree o

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Kon, Shigeyuki, Masahiro Ikesue, Chiemi Kimura, et al. "Syndecan-4 protects against osteopontin-mediated acute hepatic injury by masking functional domains of osteopontin." Journal of Experimental Medicine 205, no. 1 (2007): 25–33. http://dx.doi.org/10.1084/jem.20071324.

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Osteopontin (OPN) is a T helper type 1 immunoregulatory cytokine that plays a critical role in various inflammatory disorders. OPN exerts proinflammatory reactions through interaction with integrin receptors. OPN function can be modulated by protease digestion. However, the molecular mechanisms that regulate OPN function in vivo have not been elucidated. There are two putative heparin-binding domains (HBDs) within the OPN molecule, which may bind both heparin and heparin-like glycosaminoglycans such as syndecan. We show that expression of OPN and syndecan-4 is significantly up-regulated after

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HALDEN, Yvonne, Angelika REK, Werner ATZENHOFER, Laszlo SZILAK, Astrid WABNIG, and Andreas J. KUNGL. "Interleukin-8 binds to syndecan-2 on human endothelial cells." Biochemical Journal 377, no. 2 (2004): 533–38. http://dx.doi.org/10.1042/bj20030729.

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Application of reverse transcription–PCR to total RNA prepared from TNF-α (tumour necrosis factor-α)-stimulated HUVECs (human umbilical vein endothelial cells) revealed that the syndecan-2 mRNA was up-regulated by this inflammatory stimulus. By immunoprecipitation using an anti-syndecan-2 antibody on TNF-α-stimulated HUVEC lysates, inflammation-induced interleukin-8 was found to be an interaction partner of this HS (heparan sulphate) proteoglycan, but not of any other syndecan on these cells. The glycosylated [Syn2ect(+HS)] and non-glycosylated [Syn2ect(−HS)] forms of Syn2ect (the syndecan-2 e

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Imai, Shinji, Marko Kaksonen, Erkki Raulo, et al. "Osteoblast Recruitment and Bone Formation Enhanced by Cell Matrix–associated Heparin-binding Growth-associated Molecule (HB-GAM)." Journal of Cell Biology 143, no. 4 (1998): 1113–28. http://dx.doi.org/10.1083/jcb.143.4.1113.

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Bone has an enormous capacity for growth, regeneration, and remodeling. This capacity is largely due to induction of osteoblasts that are recruited to the site of bone formation. The recruitment of osteoblasts has not been fully elucidated, though the immediate environment of the cells is likely to play a role via cell– matrix interactions. We show here that heparin-binding growth-associated molecule (HB-GAM), an extracellular matrix–associated protein that enhances migratory responses in neurons, is prominently expressed in the cell matrices that act as target substrates for bone formation. I

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Bischof, Daniela, Sherine F. Elsawa, George Mantchev, et al. "Selective activation of TACI by syndecan-2." Blood 107, no. 8 (2006): 3235–42. http://dx.doi.org/10.1182/blood-2005-01-0256.

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Abstract B-lymphocyte homeostasis and function are regulated by complementary actions of the TNFR family members TACI, BCMA, and BAFF-R, which are expressed by mature B cells. How these receptors are differentially activated is not entirely understood, because the primary ligand BAFF binds to all three. We searched for alternative ligands for TACI using recombinant TACI-Fc fusion protein as a probe and identified syndecan-2 as a new binding partner. TACI binding appears to require heparan sulfate posttranslational modifications of syndecan-2, because free heparin or pretreatment with heparitin

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Slimani, Hocine, Nathalie Charnaux, Elisabeth Mbemba, et al. "Interaction of RANTES with syndecan-1 and syndecan-4 expressed by human primary macrophages." Biochimica et Biophysica Acta (BBA) - Biomembranes 1617, no. 1-2 (2003): 80–88. http://dx.doi.org/10.1016/j.bbamem.2003.09.006.

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Bespalov, Maxim M., Yulia A. Sidorova, Sarka Tumova, et al. "Heparan sulfate proteoglycan syndecan-3 is a novel receptor for GDNF, neurturin, and artemin." Journal of Cell Biology 192, no. 1 (2011): 153–69. http://dx.doi.org/10.1083/jcb.201009136.

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Glial cell line–derived neurotrophic factor (GDNF) family ligands (GFLs) are potent survival factors for dopaminergic neurons and motoneurons with therapeutic potential for Parkinson’s disease. Soluble GFLs bind to a ligand-specific glycosylphosphatidylinositol-anchored coreceptor (GDNF family receptor α) and signal through the receptor tyrosine kinase RET. In this paper, we show that all immobilized matrix-bound GFLs, except persephin, use a fundamentally different receptor. They interact with syndecan-3, a transmembrane heparan sulfate (HS) proteoglycan, by binding to its HS chains with high

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Elhassan, AKB, AM Suleiman, NIA El Dawi, and Sofia B. Mohamed. "Detection of Micro-invasion in Sudanese Oral Verrucous Carcinoma Samples Using Syndecan-1 Stain." Biomarkers in Cancer 11 (January 2019): 1179299X1986195. http://dx.doi.org/10.1177/1179299x19861957.

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Aim: Verrucous carcinoma (VC) is a low-grade rare variant of squamous cell carcinoma (SCC). Syndecan-1 (CD138) is a heparan sulfate proteoglycan which participates in cell-to-cell adhesion and cell-matrix interaction. Being misled by the apparent non-aggressive nature of VC, some clinicians and pathologists believe that this tumor is not an aggressive tumor, not realizing the fact that some of these lesions may contain nests or foci of well-differentiated SCC. This study aimed to assess syndecan-1 expression of VC and detection of micro-invasion in VC using syndecan-1 immunohistochemical (IHC)

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Fages, C., M. Kaksonen, T. Kinnunen, E. L. Punnonen, and H. Rauvala. "Regulation of mRNA localization by transmembrane signalling: local interaction of HB-GAM (heparin-binding growth-associated molecule) with the cell surface localizes beta-actin mRNA." Journal of Cell Science 111, no. 20 (1998): 3073–80. http://dx.doi.org/10.1242/jcs.111.20.3073.

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Localization of mRNAs is currently thought to be partially responsible for molecular sorting to specific compartments within the cell. In mammalian cells the best-studied example is the beta-actin mRNA that is localized to the cell processes, and its localization is necessary in migratory responses of cells. It is reasonable to assume that mRNA localization within cells is coupled to transmembrane signalling due to extracellular factors, but little is known about such putative mechanisms. We show here that HB-GAM, an extracellular matrix-associated factor that enhances migratory responses in c

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Fages, Carole, Marko Kaksonen, Tarja Kinnunen, Eeva-Liisa Punnonen та Heikki Rauvala. "Regulation of mRNA localization by transmembrane signalling: Local interaction of HB-GAM (heparin-binding growth-associated molecule) with the cell surface localizes β-actin mRNA". Journal of Cell Science 111, № 20 (1998): 3073–80. http://dx.doi.org/10.1242/jcs.20.111.3073.

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ABSTRACT Localization of mRNAs is currently thought to be partially responsible for molecular sorting to specific compartments within the cell. In mammalian cells the best-studied example is the β-actin mRNA that is localized to the cell processes, and its localization is necessary in migratory responses of cells. It is reasonable to assume that mRNA localization within cells is coupled to transmembrane signalling due to extracellular factors, but little is known about such putative mechanisms. We show here that HB- GAM, an extracellular matrix-associated factor that enhances migratory respons

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Wang, Haiyao, LuAnn Leavitt, Ravishankar Ramaswamy та Alan C. Rapraeger. "Interaction of Syndecan and α6β4 Integrin Cytoplasmic Domains". Journal of Biological Chemistry 285, № 18 (2010): 13569–79. http://dx.doi.org/10.1074/jbc.m110.102137.

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Verderio, Elisabetta, and Alessandra Scarpellini. "Significance of the Syndecan-4-Transglutaminase-2 Interaction." Scientific World JOURNAL 10 (2010): 1073–77. http://dx.doi.org/10.1100/tsw.2010.102.

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Kim, Minseon, and Yongae Kim. "NMR Structural Study of Syndecan-4 Transmembrane Domain with Cytoplasmic Region." Molecules 28, no. 23 (2023): 7855. http://dx.doi.org/10.3390/molecules28237855.

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Syndecan-4 (SDC4) consists of transmembrane heparan sulfate proteoglycan (HSPG) belonging to the syndecan family. It is present in most cell types of Mammalia. Its structure contains a heparan-sulfate-modified extracellular domain, a single transmembrane domain, and a short C-terminal cytoplasmic domain. Regarding the overall cellular function of SDC4, other cells or ligands can bind to its ecto-domain. In addition, 4,5-bisphosphate phosphatidylinositol (PIP2) or protein kinase Cα can bind to its cyto-domain to activate downstream signaling pathways. To understand the signal transduction mecha

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Couchman, J. R., and A. Woods. "Syndecan-4 and integrins: combinatorial signaling in cell adhesion." Journal of Cell Science 112, no. 20 (1999): 3415–20. http://dx.doi.org/10.1242/jcs.112.20.3415.

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It is now becoming clear that additional transmembrane components can modify integrin-mediated adhesion. Syndecan-4 is a transmembrane heparan sulfate proteoglycan whose external glycosaminoglycan chains can bind extracellular matrix ligands and whose core protein cytoplasmic domain can signal during adhesion. Two papers in this issue of JCS demonstrate, through transfection studies, that syndecan-4 plays roles in the formation of focal adhesions and stress fibers. Overexpression of syndecan-4 increases focal adhesion formation, whereas a partially truncated core protein that lacks the binding

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Whiteford, James R., Xiaojie Xian, Claire Chaussade, Bart Vanhaesebroeck, Sussan Nourshargh, and John R. Couchman. "Syndecan-2 is a novel ligand for the protein tyrosine phosphatase receptor CD148." Molecular Biology of the Cell 22, no. 19 (2011): 3609–24. http://dx.doi.org/10.1091/mbc.e11-02-0099.

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Syndecan-2 is a heparan sulfate proteoglycan that has a cell adhesion regulatory domain contained within its extracellular core protein. Cell adhesion to the syndecan-2 extracellular domain (S2ED) is β1 integrin dependent; however, syndecan-2 is not an integrin ligand. Here the protein tyrosine phosphatase receptor CD148 is shown to be a key intermediary in cell adhesion to S2ED, with downstream β1 integrin–mediated adhesion and cytoskeletal organization. We show that S2ED is a novel ligand for CD148 and identify the region proximal to the transmembrane domain of syndecan-2 as the site of inte

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Hsueh, Yi-Ping, Fu-Chia Yang, Viktor Kharazia, et al. "Direct Interaction of CASK/LIN-2 and Syndecan Heparan Sulfate Proteoglycan and Their Overlapping Distribution in Neuronal Synapses." Journal of Cell Biology 142, no. 1 (1998): 139–51. http://dx.doi.org/10.1083/jcb.142.1.139.

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CASK, the rat homolog of a gene (LIN-2) required for vulval differentiation in Caenorhabditis elegans, is expressed in mammalian brain, but its function in neurons is unknown. CASK is distributed in a punctate somatodendritic pattern in neurons. By immunogold EM, CASK protein is concentrated in synapses, but is also present at nonsynaptic membranes and in intracellular compartments. This immunolocalization is consistent with biochemical studies showing the presence of CASK in soluble and synaptosomal membrane fractions and its enrichment in postsynaptic density fractions of rat brain. By yeast

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Jang, Bohee, Ayoung Kim, Yejin Lee, et al. "Substituted Syndecan-2-Derived Mimetic Peptides Show Improved Antitumor Activity over the Parent Syndecan-2-Derived Peptide." International Journal of Molecular Sciences 23, no. 11 (2022): 5888. http://dx.doi.org/10.3390/ijms23115888.

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We previously showed that a synthetic peptide (S2-P) corresponding to a portion of the human syndecan-2 (SDC2) sequence can bind to the pro-domain of matrix metalloproteinase-7 (MMP-7) to inhibit colon cancer activities. Since S2-P had a relatively weak binding affinity for the MMP-7 pro-domain, we herein modified the amino acid sequence of S2-P to improve the anticancer potential. On the basis of the interaction structure of S2-P and MMP-7, four peptides were generated by replacing amino acids near Tyr 51, which is critical for the interaction. The SDC2-mimetic peptides harboring an Ala-to-As

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Horowitz, Arie, Eugene Tkachenko, and Michael Simons. "Fibroblast growth factor–specific modulation of cellular response by syndecan-4." Journal of Cell Biology 157, no. 4 (2002): 715–25. http://dx.doi.org/10.1083/jcb.200112145.

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Proteoglycans participate in growth factor interaction with the cell surface through their heparan sulfate chains (HS), but it is not known if they are otherwise involved in growth factor signaling. It appears now that the syndecan-4 core protein, a transmembrane proteoglycan shown previously to bind phosphatidylinositol 4,5-bisphosphate (PIP2) and activate PKCα, participates in mediating the effects of fibroblast growth factor (FGF)2 on cell function. Mutations in the cytoplasmic tail of syndecan-4 that either reduced its affinity to PIP2 (PIP2−) or disrupted its postsynaptic density 95, disk

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Chaves, Maria, Matheus Mendes, Maximilian Schwermann, et al. "Angiopoietin-2: A Potential Mediator of the Glycocalyx Injury in Adult Nephrotic Patients." Journal of Clinical Medicine 7, no. 11 (2018): 401. http://dx.doi.org/10.3390/jcm7110401.

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Introduction: Glomerulopathy is a group of diseases that affect mainly young adults between the ages of 20 and 40 years. Recently, it has been demonstrated that syndecan-1, a biomarker of endothelial glycocalyx damage, is increased in nephrotic patients with near-normal renal function and it is important to endothelial dysfunction in these patients. Angiopoietin-2 (AGPT2) is an endothelial growth factor that promotes cell derangement. Here we evaluated AGPT2 levels in patients with nephrotic syndrome, near-normal renal function and the possible interaction of AGPT2 with endothelial glycocalyx

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Watson, L. N., M. Sasseville, R. B. Gilchrist, and D. L. Russell. "118. CHARACTERISATION OF HEPARAN SULPHATE PROTEOGLYCANS IN THE MATURING CUMULUS OOCYTE COMPLEX." Reproduction, Fertility and Development 21, no. 9 (2009): 37. http://dx.doi.org/10.1071/srb09abs118.

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Many growth factors including members of the transforming growth factor beta (TGFβ) superfamily and epidermal growth factor (Egf)-like ligands signal via interactions with heparan sulphate proteoglycans (HSPGs). Cell surface HSPGs can act by sequestering ligands at their site of action, by presenting a ligand to its signalling receptor, or by preventing ligand-receptor interaction. The oocyte secreted factors (OSF) growth differentiation factor 9 and bone morphogenetic protein 15 are members of the TGFβ superfamily that act selectively on cumulus cells. Conversely Egf-like ligands are secreted

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Sun, Zheng, Shihao Li, Fuhua Li, and Jianhai Xiang. "Bioinformatic Prediction of WSSV-Host Protein-Protein Interaction." BioMed Research International 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/416543.

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WSSV is one of the most dangerous pathogens in shrimp aquaculture. However, the molecular mechanism of how WSSV interacts with shrimp is still not very clear. In the present study, bioinformatic approaches were used to predict interactions between proteins from WSSV and shrimp. The genome data of WSSV (NC_003225.1) and the constructed transcriptome data ofF. chinensiswere used to screen potentially interacting proteins by searching in protein interaction databases, including STRING, Reactome, and DIP. Forty-four pairs of proteins were suggested to have interactions between WSSV and the shrimp.

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Horiguchi, Kotaro, Tom Kouki, Ken Fujiwara, et al. "Expression of the proteoglycan syndecan-4 and the mechanism by which it mediates stress fiber formation in folliculostellate cells in the rat anterior pituitary gland." Journal of Endocrinology 214, no. 2 (2012): 199–206. http://dx.doi.org/10.1530/joe-12-0156.

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Folliculostellate (FS) cells in the anterior pituitary gland appear to have multifunctional properties. FS cells connect to each other at gap junctions and thereby form a histological and functional network. We have performed a series of studies on network formation in FS cells and recently reported that FS cells markedly prolong their cytoplasmic processes and form numerous interconnections with neighboring FS cells in the presence of laminin, an extracellular matrix (ECM) component of the basement membrane. In this study, we investigated the mechanism of this extension of FS cell cytoplasmic

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Urbinati, Chiara, Maria Milanesi, Nicola Lauro, et al. "HIV-1 Tat and Heparan Sulfate Proteoglycans Orchestrate the Setup of in Cis and in Trans Cell-Surface Interactions Functional to Lymphocyte Trans-Endothelial Migration." Molecules 26, no. 24 (2021): 7488. http://dx.doi.org/10.3390/molecules26247488.

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HIV-1 transactivating factor Tat is released by infected cells. Extracellular Tat homodimerizes and engages several receptors, including integrins, vascular endothelial growth factor receptor 2 (VEGFR2) and heparan sulfate proteoglycan (HSPG) syndecan-1 expressed on various cells. By means of experimental cell models recapitulating the processes of lymphocyte trans-endothelial migration, here, we demonstrate that upon association with syndecan-1 expressed on lymphocytes, Tat triggers simultaneously the in cis activation of lymphocytes themselves and the in trans activation of endothelial cells

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Hohenester, E., S. Hussain, and J. A. Howitt. "Interaction of the guidance molecule Slit with cellular receptors." Biochemical Society Transactions 34, no. 3 (2006): 418–21. http://dx.doi.org/10.1042/bst0340418.

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Slits are large secreted glycoproteins characterized by an unusual tandem of four LRR (leucine-rich repeat) domains in their N-terminal half. Slit proteins were initially described as repulsive guidance cues in neural development, but it has become clear that they have additional important functions, for instance in the vasculature and immune system. Genetic studies have identified two types of cellular receptors for Slits: Robos (Roundabout) and the HS (heparan sulphate) proteoglycan syndecan. The intracellular signalling cascade downstream of Robo activation is slowly being elucidated, but t

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Zimmermann, Pascale, Zhe Zhang, Gisèle Degeest, et al. "Syndecan Recyling Is Controlled by Syntenin-PIP2 Interaction and Arf6." Developmental Cell 9, no. 3 (2005): 377–88. http://dx.doi.org/10.1016/j.devcel.2005.07.011.

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Zimmermann, Pascale, Zhe Zhang, Gisèle Degeest, et al. "Syndecan Recycling Is Controlled by Syntenin-PIP2 Interaction and Arf6." Developmental Cell 9, no. 5 (2005): 721. http://dx.doi.org/10.1016/j.devcel.2005.10.011.

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Arnold, Katelyn, Yongmei Xu, Erica M. Sparkenbaugh, et al. "Design of anti-inflammatory heparan sulfate to protect against acetaminophen-induced acute liver failure." Science Translational Medicine 12, no. 535 (2020): eaav8075. http://dx.doi.org/10.1126/scitranslmed.aav8075.

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Acetaminophen/paracetamol (APAP) overdose is the leading cause of drug-induced acute liver failure (ALF) in the United States and Europe. The progression of the disease is attributed to sterile inflammation induced by the release of high mobility group box 1 (HMGB1) and the interaction with receptor for advanced glycation end products (RAGE). A specific, effective, and safe approach to neutralize the proinflammatory activity of HMGB1 is highly desirable. Here, we found that a heparan sulfate (HS) octadecasaccharide (18-mer-HP or hepatoprotective 18-mer) displays potent hepatoprotection by targ

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Zhao, Tingting, Li Cui, Xiangqian Yu, Zhonghai Zhang, Qi Chen, and Xiuguo Hua. "Proteome Analysis Reveals Syndecan 1 Regulates Porcine Sapelovirus Replication." International Journal of Molecular Sciences 21, no. 12 (2020): 4386. http://dx.doi.org/10.3390/ijms21124386.

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Porcine sapelovirus A (PSV) is a single stranded, positive-sense, non-enveloped RNA virus that causes enteritis, pneumonia, polioencephalomyelitis, and reproductive disorders in pigs. Research on PSV infection and interaction with host cells is unclear. In this study, we applied tandem mass tag proteomics analysis to investigate the differentially expressed proteins (DEPs) in PSV-infected pig kidney (PK)-15 cells and explored the interactions between PSV and host cells. Here we mapped 181 DEPs, including 59 up-regulated and 122 down-regulated DEPs. Among them, osteopontin (SPP1), induced prote

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Keller-Pinter, A., L. Mendler, and L. Dux. "EM.P.1.05 Heparan sulfate-dependent interaction of myostatin and syndecan-4." Neuromuscular Disorders 19, no. 8-9 (2009): 550. http://dx.doi.org/10.1016/j.nmd.2009.06.026.

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Kim, Heeyoun, Jiho Yoo, Inhwan Lee, Ying Jin Kang, Hyun-Soo Cho, and Weontae Lee. "Crystal structure of syndesmos and its interaction with Syndecan-4 proteoglycan." Biochemical and Biophysical Research Communications 463, no. 4 (2015): 762–67. http://dx.doi.org/10.1016/j.bbrc.2015.06.010.

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