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Journal articles on the topic 'Syndecans'

Author: Grafiati

Published: 4 June 2021

Last updated: 30 January 2023

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1

CAREY, David J. "Syndecans: multifunctional cell-surface co-receptors." Biochemical Journal 327, no. 1 (1997): 1–16. http://dx.doi.org/10.1042/bj3270001.

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This review will summarize our current state of knowledge of the structure, biochemical properties and functions of syndecans, a family of transmembrane heparan sulphate proteoglycans. Syndecans bind a variety of extracellular ligands via their covalently attached heparan sulphate chains. Syndecans have been proposed to play a role in a variety of cellular functions, including cell proliferation and cell–matrix and cell–cell adhesion. Syndecan expression is highly regulated and is cell-type- and developmental-stage-specific. The main function of syndecans appears to be to modulate the ligand-d

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2

Kim, C. W., O. A. Goldberger, R. L. Gallo, and M. Bernfield. "Members of the syndecan family of heparan sulfate proteoglycans are expressed in distinct cell-, tissue-, and development-specific patterns." Molecular Biology of the Cell 5, no. 7 (1994): 797–805. http://dx.doi.org/10.1091/mbc.5.7.797.

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The syndecans are a gene family of four transmembrane heparan sulfate proteoglycans that bind, via their HS chains, diverse components of the cellular microenvironment. To evaluate the expression of the individual syndecans, we prepared cDNA probes to compare mRNA levels in various adult mouse tissues and cultured mouse cells representing various epithelial, fibroblastic, endothelial, and neural cell types and B cells at various stages of differentiation. We also prepared antibody probes to assess whether the extracellular domains of the individual syndecans are shed into the conditioned media

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Mitsou, Ioli, Hinke A. B. Multhaupt, and John R. Couchman. "Proteoglycans, ion channels and cell–matrix adhesion." Biochemical Journal 474, no. 12 (2017): 1965–79. http://dx.doi.org/10.1042/bcj20160747.

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Cell surface proteoglycans comprise a transmembrane or membrane-associated core protein to which one or more glycosaminoglycan chains are covalently attached. They are ubiquitous receptors on nearly all animal cell surfaces. In mammals, the cell surface proteoglycans include the six glypicans, CD44, NG2 (CSPG4), neuropilin-1 and four syndecans. A single syndecan is present in invertebrates such as nematodes and insects. Uniquely, syndecans are receptors for many classes of proteins that can bind to the heparan sulphate chains present on syndecan core proteins. These range from cytokines, chemo

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Betriu, Nausika, Juan Bertran-Mas, Anna Andreeva, and Carlos E. Semino. "Syndecans and Pancreatic Ductal Adenocarcinoma." Biomolecules 11, no. 3 (2021): 349. http://dx.doi.org/10.3390/biom11030349.

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Pancreatic Ductal Adenocarcinoma (PDAC) is a fatal disease with poor prognosis because patients rarely express symptoms in initial stages, which prevents early detection and diagnosis. Syndecans, a subfamily of proteoglycans, are involved in many physiological processes including cell proliferation, adhesion, and migration. Syndecans are physiologically found in many cell types and their interactions with other macromolecules enhance many pathways. In particular, extracellular matrix components, growth factors, and integrins collect the majority of syndecans associations acting as biochemical,

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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 (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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6

De Rossi, Giulia, and James R. Whiteford. "Syndecans in angiogenesis and endothelial cell biology." Biochemical Society Transactions 42, no. 6 (2014): 1643–46. http://dx.doi.org/10.1042/bst20140232.

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Syndecans are multifunctional heparan sulfate proteoglycans (HSPGs) with roles in cell adhesion, migration, receptor trafficking and growth-factor interactions and signalling. Studies using syndecan null animals have revealed limited roles for syndecans during development; however, under conditions of challenge or insult, several phenotypes have emerged. Angiogenesis is an important process both in development and in wound healing, but also in pathologies such as cancer and chronic inflammatory conditions. In the present paper, we summarize the main studies elucidating the role of syndecans in

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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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8

Finsen, Alexandra Vanessa, Per Reidar Woldbaek, Jian Li, et al. "Increased syndecan expression following myocardial infarction indicates a role in cardiac remodeling." Physiological Genomics 16, no. 3 (2004): 301–8. http://dx.doi.org/10.1152/physiolgenomics.00144.2002.

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Finsen, Alexandra Vanessa, Per Reidar Woldbaek, Jian Li, Jiaping Wu, Torstein Lyberg, Theis Tonnessen, and Geir Christensen. Increased syndecan expression following myocardial infarction indicates a role in cardiac remodeling. Physiol Genomics 16: 301-308, 2004. First published November 18, 2003; 10.1152/physi-olgenomics. 00144.2002.—The purpose of this study was to identify essential genes involved in myocardial growth and remodeling following myocardial infarction (MI). Left ventricular noninfarcted tissues from six mice subjected to MI under general anesthesia and from six sham-operated mic

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9

Termini, Christina, Michelle Li, Joyce Kim, Liman Zhao, and John P. Chute. "Syndecan-2 Surface Expression Identifies Hematopoietic Stem Cells with Increased Repopulating Capacity." Blood 132, Supplement 1 (2018): 1273. http://dx.doi.org/10.1182/blood-2018-99-110701.

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Abstract Syndecans are transmembrane glycoproteins, which can regulate cell proliferation, growth, and adhesion through interactions with neighboring proteins within the plasma membrane or at the cytoplasmic interface. Although syndecans have been described to regulate aberrant signaling in hematological malignances, the role of syndecans in regulating normal hematopoietic stem cell (HSC) proliferation, differentiation, and self-renewal is largely unknown. We demonstrate that syndecan-1 and syndecan-3 are expressed on the surface of < 10% of murine hematopoietic stem and progenitor cells, w

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Gopal, Sandeep, Pernille Søgaard, Hinke A. B. Multhaupt, et al. "Transmembrane proteoglycans control stretch-activated channels to set cytosolic calcium levels." Journal of Cell Biology 210, no. 7 (2015): 1199–211. http://dx.doi.org/10.1083/jcb.201501060.

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Transmembrane heparan sulfate proteoglycans regulate multiple aspects of cell behavior, but the molecular basis of their signaling is unresolved. The major family of transmembrane proteoglycans is the syndecans, present in virtually all nucleated cells, but with mostly unknown functions. Here, we show that syndecans regulate transient receptor potential canonical (TRPCs) channels to control cytosolic calcium equilibria and consequent cell behavior. In fibroblasts, ligand interactions with heparan sulfate of syndecan-4 recruit cytoplasmic protein kinase C to target serine714 of TRPC7 with subse

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11

Bernfield, Merton, Michael T. Hinkes, and Richard L. Gallo. "Developmental expression of the syndecans: possible function and regulation." Development 119, Supplement (1993): 205–12. http://dx.doi.org/10.1242/dev.119.supplement.205.

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Recent work has made clear that heparan sulfate at the cell surface is essential for a wide variety of interactions of cells with their microenvironment , including the action of growth factors, extracellular matrix, proteases and protease inhibitors. A major source of this cell surface heparan sulfate is a multigene family of proteoglycans, the syndecans that are expressed developmentally in association with changes in tissue organization and morphology and induced during wound repair. In this review, we describe mechanisms underlyin g the differential expression of the syndecans, focusing on

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Araki, Eri, Yutaka Momota, Takeshi Togo та ін. "Clustering of Syndecan-4 and Integrin β1 by Laminin α3 Chain–derived Peptide Promotes Keratinocyte Migration". Molecular Biology of the Cell 20, № 13 (2009): 3012–24. http://dx.doi.org/10.1091/mbc.e08-09-0977.

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Syndecans function as receptors for extracellular matrix (ECM) with integrins in cell spreading. However, the molecular mechanism of their specific involvement in cell migration or in wound healing has not been elucidated yet. Here, we report that a synthetic peptide, PEP75, which contains the syndecan-binding sequence of the laminin α3LG4 module, induces keratinocyte migration in in vitro and in vivo. Soluble PEP75 induced the clustering of syndecan-4 and conformation-modified integrin β1 colocalized with syndecan-4 in soluble PEP75-induced clusters. Treatment of cells in solution with PEP75

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Tkachenko, Eugene, John M. Rhodes, and Michael Simons. "Syndecans." Circulation Research 96, no. 5 (2005): 488–500. http://dx.doi.org/10.1161/01.res.0000159708.71142.c8.

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Iba, Kousuke, Reidar Albrechtsen, Brent Gilpin та ін. "The Cysteine-Rich Domain of Human Adam 12 Supports Cell Adhesion through Syndecans and Triggers Signaling Events That Lead to β1 Integrin–Dependent Cell Spreading". Journal of Cell Biology 149, № 5 (2000): 1143–56. http://dx.doi.org/10.1083/jcb.149.5.1143.

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The ADAMs (a disintegrin and metalloprotease) family of proteins is involved in a variety of cellular interactions, including cell adhesion and ecto- domain shedding. Here we show that ADAM 12 binds to cell surface syndecans. Three forms of recombinant ADAM 12 were used in these experiments: the cys-teine-rich domain made in Escherichia coli (rADAM 12-cys), the disintegrin-like and cysteine-rich domain made in insect cells (rADAM 12-DC), and full-length human ADAM 12-S tagged with green fluorescent protein made in mammalian cells (rADAM 12-GFP). Mesenchymal cells specifically and in a dose-dep

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15

Huang, Chun-Ping, Chao-Min Cheng, Hong-Lin Su та Yi-Wen Lin. "Syndecan-4 Promotes Epithelial Tumor Cells Spreading and Regulates the Turnover of PKCα Activity under Mechanical Stimulation on the Elastomeric Substrates". Cellular Physiology and Biochemistry 36, № 4 (2015): 1291–304. http://dx.doi.org/10.1159/000430297.

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Background: Heparan sulfate proteoglycans (HSPGs) at the cell surface play an important role in cell adhesion, spreading, formation of focal adhesion complexes (FACs), and sensing mechanical stress. Syndecans are members of the HSPGs family and are highly expressed in various tumor cells. Syndecan-4 (SDC4) is a unique member of syndecans that activates protein kinase C alpha (PKCα). However, syndecan-4 in tumor cells development is not clear when receiving mechanical stress. Aims: Here we investigate the role of syndecan-4 in tumor cells spreading and its downstream kinases under mechanical st

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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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17

Hillemeyer, Lara, Nancy Adriana Espinoza-Sanchez, Burkhard Greve, et al. "The Cell Surface Heparan Sulfate Proteoglycan Syndecan-3 Promotes Ovarian Cancer Pathogenesis." International Journal of Molecular Sciences 23, no. 10 (2022): 5793. http://dx.doi.org/10.3390/ijms23105793.

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Syndecans are transmembrane heparan sulfate proteoglycans that integrate signaling at the cell surface. By interacting with cytokines, signaling receptors, proteases, and extracellular matrix proteins, syndecans regulate cell proliferation, metastasis, angiogenesis, and inflammation. We analyzed public gene expression datasets to evaluate the dysregulation and potential prognostic impact of Syndecan-3 in ovarian cancer. Moreover, we performed functional in vitro analysis in syndecan-3-siRNA-treated SKOV3 and CAOV3 ovarian cancer cells. In silico analysis of public gene array datasets revealed

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18

Whiteford, James R., and John R. Couchman. "A Conserved NXIP Motif Is Required for Cell Adhesion Properties of the Syndecan-4 Ectodomain." Journal of Biological Chemistry 281, no. 43 (2006): 32156–63. http://dx.doi.org/10.1074/jbc.m605553200.

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Syndecans are cell surface proteoglycans involved in cell adhesion and motility. Syndecan-4 is an important component of focal adhesions and is involved in cytoskeletal reorganization. Previous work has shown that the syndecan-4 ectodomain can support cell attachment. Here, three vertebrate syndecan-4 ectodomains were compared, including that of the zebrafish, and we have demonstrated that the cell binding activity of the syndecan-4 ectodomain is conserved. Cell adhesion to the syndecan-4 ectodomain appears to be a characteristic of mesenchymal cells. Comparison of syndecan-4 ectodomain sequen

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MUNESUE, Seiichi, Yuri KUSANO, Kayoko OGURI, et al. "The role of syndecan-2 in regulation of actin-cytoskeletal organization of Lewis lung carcinoma-derived metastatic clones." Biochemical Journal 363, no. 2 (2002): 201–9. http://dx.doi.org/10.1042/bj3630201.

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Syndecans, a family of transmembrane heparan sulphate proteoglycans, contribute to various biological processes, including adhesion, motility, proliferation, differentiation and morphogenesis. We document here the involvement of syndecan-2 acting alone or co-operatively with integrin α5β1, for regulation of actin-cytoskeletal organization on cell adhesion to fibronectin, using fibronectin-recombinant polypeptides containing the ligands for either or both of these receptors as substrata. Lewis lung carcinoma-derived low-metastatic P29 cells binding to the substrata by both receptors formed acti

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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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Kalia, Manjula, Vivek Chandra, Sheikh Abdul Rahman, Deepak Sehgal, and Shahid Jameel. "Heparan Sulfate Proteoglycans Are Required for Cellular Binding of the Hepatitis E Virus ORF2 Capsid Protein and for Viral Infection." Journal of Virology 83, no. 24 (2009): 12714–24. http://dx.doi.org/10.1128/jvi.00717-09.

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ABSTRACT The hepatitis E virus (HEV), a nonenveloped RNA virus, is the causative agent of hepatitis E. The mode by which HEV attaches to and enters into target cells for productive infection remains unidentified. Open reading frame 2 (ORF2) of HEV encodes its major capsid protein, pORF2, which is likely to have the determinants for virus attachment and entry. Using an ∼56-kDa recombinant pORF2 that can self-assemble as virus-like particles, we demonstrated that cell surface heparan sulfate proteoglycans (HSPGs), specifically syndecans, play a crucial role in the binding of pORF2 to Huh-7 liver

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Götte, Martin. "Syndecans in inflammation." FASEB Journal 17, no. 6 (2003): 575–91. http://dx.doi.org/10.1096/fj.02-0739rev.

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Bobardt, Michael D., Udayan Chatterji, Suganya Selvarajah, et al. "Cell-Free Human Immunodeficiency Virus Type 1 Transcytosis through Primary Genital Epithelial Cells." Journal of Virology 81, no. 1 (2006): 395–405. http://dx.doi.org/10.1128/jvi.01303-06.

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ABSTRACT Although the transport of human immunodeficiency virus type 1 (HIV-1) through the epithelium is critical for HIV-1 colonization, the mechanisms controlling this process remain obscure. In the present study, we investigated the transcellular migration of HIV-1 as a cell-free virus through primary genital epithelial cells (PGECs). The absence of CD4 on PGECs implicates an unusual entry pathway for HIV-1. We found that syndecans are abundantly expressed on PGECs and promote the initial attachment and subsequent entry of HIV-1 through PGECs. Although CXCR4 and CCR5 do not contribute to HI

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Luyten, Annouck, Eva Mortier, Claude Van Campenhout, et al. "The Postsynaptic Density 95/Disc-Large/Zona Occludens Protein Syntenin Directly Interacts with Frizzled 7 and Supports Noncanonical Wnt Signaling." Molecular Biology of the Cell 19, no. 4 (2008): 1594–604. http://dx.doi.org/10.1091/mbc.e07-08-0832.

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Wnt signaling pathways are essential for embryonic patterning, and they are disturbed in a wide spectrum of diseases, including cancer. An unresolved question is how the different Wnt pathways are supported and regulated. We previously established that the postsynaptic density 95/disc-large/zona occludens (PDZ) protein syntenin binds to syndecans, Wnt coreceptors, and known stimulators of protein kinase C (PKC)α and CDC42 activity. Here, we show that syntenin also interacts with the C-terminal PDZ binding motif of several Frizzled Wnt receptors, without compromising the recruitment of Dishevel

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Ding, Kan, Martha Lopez-Burks, José Antonio Sánchez-Duran, Murray Korc, and Arthur D. Lander. "Growth factor–induced shedding of syndecan-1 confers glypican-1 dependence on mitogenic responses of cancer cells." Journal of Cell Biology 171, no. 4 (2005): 729–38. http://dx.doi.org/10.1083/jcb.200508010.

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The cell surface heparan sulfate proteoglycan (HSPG) glypican-1 is up-regulated by pancreatic and breast cancer cells, and its removal renders such cells insensitive to many growth factors. We sought to explain why the cell surface HSPG syndecan-1, which is also up-regulated by these cells and is a known growth factor coreceptor, does not compensate for glypican-1 loss. We show that the initial responses of these cells to the growth factor FGF2 are not glypican dependent, but they become so over time as FGF2 induces shedding of syndecan-1. Manipulations that retain syndecan-1 on the cell surfa

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Okayama, Minoru, Seiichi Munesue, Masato Komaki, Yuri Kusano, and Kayoko Oguri. "Functional Specificity of Syndecans." Trends in Glycoscience and Glycotechnology 10, no. 52 (1998): 211–21. http://dx.doi.org/10.4052/tigg.10.211.

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Lunde, Ida G., Kate M. Herum, Cathrine C. Carlson, and Geir Christensen. "Syndecans in heart fibrosis." Cell and Tissue Research 365, no. 3 (2016): 539–52. http://dx.doi.org/10.1007/s00441-016-2454-2.

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Beauvais, DeannaLee M., Brandon J. Burbach та Alan C. Rapraeger. "The syndecan-1 ectodomain regulates αvβ3 integrin activity in human mammary carcinoma cells". Journal of Cell Biology 167, № 1 (2004): 171–81. http://dx.doi.org/10.1083/jcb.200404171.

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The αvβ3 integrin participates in cell morphogenesis, growth factor signaling, and cell survival. Activation of the integrin is central to these processes and is influenced by specific ECM components, which engage both integrins and syndecans. This paper demonstrates that the αvβ3 integrin and syndecan-1 (S1) are functionally coupled. The integrin is dependent on the syndecan to become activated and to mediate signals required for MDA-MB-231 and MDA-MB-435 human mammary carcinoma cell spreading on vitronectin or S1-specific antibody. Coupling of the syndecan to αvβ3 requires the S1 ectodomain

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Baciu, P. C., and P. F. Goetinck. "Protein kinase C regulates the recruitment of syndecan-4 into focal contacts." Molecular Biology of the Cell 6, no. 11 (1995): 1503–13. http://dx.doi.org/10.1091/mbc.6.11.1503.

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Cell surface heparan sulfate proteoglycans have been implicated as co-receptors facilitating cell adhesion and growth factor binding. Recent studies on the role of a family of transmembrane heparan sulfate proteoglycans, syndecans, in cell adhesion has identified one member, syndecan-4, to be present within focal contacts. The current study investigates the mechanisms regulating the association of syndecan-4 with focal contacts based upon its immunolocalization with vinculin in quiescent, serum-stimulated, and 12-0-tetradecanoylphorbol 13-acetate (TPA)-induced cultures. In quiescent cells, syn

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Ridley, RC, H. Xiao, H. Hata, J. Woodliff, J. Epstein, and RD Sanderson. "Expression of syndecan regulates human myeloma plasma cell adhesion to type I collagen." Blood 81, no. 3 (1993): 767–74. http://dx.doi.org/10.1182/blood.v81.3.767.767.

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Abstract The syndecans comprise a family of integral membrane proteoglycans that regulate cell behaviors by binding to extracellular matrix and binding growth factors. In mouse blood cells, syndecan expression is restricted to cells of the B-cell lineage where it is expressed by pre-B cells and plasma cells, but is absent from circulating B cells. In the present study, we examined the expression, structure, and function of syndecan on human myeloma cell lines and myeloma patient bone marrow cells. On myeloma cells, syndecan is a small (modal relative molecular mass [M(r)] = 120 Kd) heparan sul

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Ridley, RC, H. Xiao, H. Hata, J. Woodliff, J. Epstein, and RD Sanderson. "Expression of syndecan regulates human myeloma plasma cell adhesion to type I collagen." Blood 81, no. 3 (1993): 767–74. http://dx.doi.org/10.1182/blood.v81.3.767.bloodjournal813767.

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The syndecans comprise a family of integral membrane proteoglycans that regulate cell behaviors by binding to extracellular matrix and binding growth factors. In mouse blood cells, syndecan expression is restricted to cells of the B-cell lineage where it is expressed by pre-B cells and plasma cells, but is absent from circulating B cells. In the present study, we examined the expression, structure, and function of syndecan on human myeloma cell lines and myeloma patient bone marrow cells. On myeloma cells, syndecan is a small (modal relative molecular mass [M(r)] = 120 Kd) heparan sulfate prot

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Couchman, John R. "Syndecan-1 (CD138), Carcinomas and EMT." International Journal of Molecular Sciences 22, no. 8 (2021): 4227. http://dx.doi.org/10.3390/ijms22084227.

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Cell surface proteoglycans are known to be important regulators of many aspects of cell behavior. The principal family of transmembrane proteoglycans is the syndecans, of which there are four in mammals. Syndecan-1 is mostly restricted to epithelia, and bears heparan sulfate chains that are capable of interacting with a large array of polypeptides, including extracellular matrix components and potent mediators of proliferation, adhesion and migration. For this reason, it has been studied extensively with respect to carcinomas and tumor progression. Frequently, but not always, syndecan-1 levels

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Hudák, Anett, Gareth Morgan, Jaromir Bacovsky, et al. "Biodistribution and Cellular Internalization of Inactivated SARS-CoV-2 in Wild-Type Mice." International Journal of Molecular Sciences 23, no. 14 (2022): 7609. http://dx.doi.org/10.3390/ijms23147609.

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Despite the growing list of identified SARS-CoV-2 receptors, the human angiotensin-converting enzyme 2 (ACE2) is still viewed as the main cell entry receptor mediating SARS-CoV-2 internalization. It has been reported that wild-type mice, like other rodent species of the Muridae family, cannot be infected with SARS-CoV-2 due to differences in their ACE2 receptors. On the other hand, the consensus heparin-binding motif of SARS-CoV-2’s spike protein, PRRAR, enables the attachment to rodent heparan sulfate proteoglycans (HSPGs), including syndecans, a transmembrane HSPG family with a well-establis

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Hozumi, Kentaro, Nobuharu Suzuki, Peter K. Nielsen, Motoyoshi Nomizu та Yoshihiko Yamada. "Laminin α1 Chain LG4 Module Promotes Cell Attachment through Syndecans and Cell Spreading through Integrin α2β1". Journal of Biological Chemistry 281, № 43 (2006): 32929–40. http://dx.doi.org/10.1074/jbc.m605708200.

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The laminin α1 chain is a subunit of laminin-1, a heterotrimeric basement membrane protein. The LG4-5 module at the C terminus of laminin α1 contains major binding sites for heparin, sulfatide, and α-dystroglycan and plays a critical role in early embryonic development. We previously identified active synthetic peptides AG73 and EF-1 from the sequence of lamininα1 LG4 for binding to syndecan and integrin α2β1, respectively. However, their activity and functional relationship within the laminin-1 and LG4 as well as the functional relation between these sites and α-dystroglycan binding sites in

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Nasi, S., J. Bertrand, M. Bollmann, R. Stange, and T. Pap. "THU0435 CALCIUM PYROPHOSPHATE DIHYDRATE (CPPD) CRYSTALS BUT NOT BASIC CALCIUM PHOSPHATE (BCP) CRYSTALS INDUCE SYNDECAN-4 EXPRESSION IN CARTILAGE." Annals of the Rheumatic Diseases 79, Suppl 1 (2020): 454.2–455. http://dx.doi.org/10.1136/annrheumdis-2020-eular.2772.

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Background:Chondrocalcinosis is a painful rheumatic condition caused by the deposition of calcium pyrophosphate dihydrate crystals (CPPD) in joint tissues, and especially in cartilage. It is known that CPPD crystals cause inflammation and degenerative changes in joint, but the underlying mechanisms remain poorly understood. In particular, nothing is known about how these crystals regulates transmembrane heparan sulphate proteoglycans (HSPGs). Our attention focused on one family of HSPGs called syndecans as they have important roles both as adhesion molecules, by mediating chondrocyte-extracell

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Yamashita, Yoshio, Kenji Oritani, Erina K. Miyoshi, Randolph Wall, Merton Bernfield, and Paul W. Kincade. "Syndecan-4 Is Expressed by B Lineage Lymphocytes and Can Transmit a Signal for Formation of Dendritic Processes." Journal of Immunology 162, no. 10 (1999): 5940–48. http://dx.doi.org/10.4049/jimmunol.162.10.5940.

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Abstract Our previous studies indicated that stromal cell-derived syndecan-4 might mediate some form of communication with pre-B cells in bone marrow. We now report additional aspects of this recognition and show that syndecan-4 is also present on pre-B cells. Indeed, the molecule is acquired at an early stage of differentiation and retained until mature B cells undergo Ig isotype switching. mAbs developed to two portions of the syndecan-4 protein core were used to probe possible functions on B lineage lymphocytes. Syndecan-4 ligation had no obvious influence on B lymphocyte formation or activ

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37

Kopper, László. "Syndecans and the Lymphoid System." Leukemia & Lymphoma 38, no. 3-4 (2000): 271–81. http://dx.doi.org/10.3109/10428190009087018.

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38

Nelson, Axel, Joakim Johansson, Jonas Tydén, and Mikael Bodelsson. "Circulating syndecans during critical illness." APMIS 125, no. 5 (2017): 468–75. http://dx.doi.org/10.1111/apm.12662.

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39

Romarı́s, Manuel, Christien Coomans, Helga Ceulemans, Anne-Mie Bruystens, Sylvie Vekemans, and Guido David. "Molecular Polymorphism of the Syndecans." Journal of Biological Chemistry 274, no. 26 (1999): 18667–74. http://dx.doi.org/10.1074/jbc.274.26.18667.

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40

Gallay, Philippe. "Syndecans and HIV-1 pathogenesis." Microbes and Infection 6, no. 6 (2004): 617–22. http://dx.doi.org/10.1016/j.micinf.2004.02.004.

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Letoha, Tamás, Anikó Keller-Pintér, Erzsébet Kusz, et al. "Cell-penetrating peptide exploited syndecans." Biochimica et Biophysica Acta (BBA) - Biomembranes 1798, no. 12 (2010): 2258–65. http://dx.doi.org/10.1016/j.bbamem.2010.01.022.

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Gondelaud, Frank, and Sylvie Ricard‐Blum. "Structures and interactions of syndecans." FEBS Journal 286, no. 15 (2019): 2994–3007. http://dx.doi.org/10.1111/febs.14828.

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Couchman, John R., and Anne Woods. "Syndecans, signaling, and cell adhesion." Journal of Cellular Biochemistry 61, no. 4 (1996): 578–84. http://dx.doi.org/10.1002/(sici)1097-4644(19960616)61:4<578::aid-jcb11>3.0.co;2-c.

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Carey, DJ, RC Stahl, G. Cizmeci-Smith, and VK Asundi. "Syndecan-1 expressed in Schwann cells causes morphological transformation and cytoskeletal reorganization and associates with actin during cell spreading." Journal of Cell Biology 124, no. 1 (1994): 161–70. http://dx.doi.org/10.1083/jcb.124.1.161.

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To investigate the biological functions of transmembrane proteoglycans we have produced clonal cell lines of rat Schwann cells that express the hybrid proteoglycan syndecan-1. This was done by transfection of newborn rat Schwann cells with a plasmid vector bearing the rat syndecan-1 cDNA sequence under transcriptional control of the constitutively active cytomegalovirus promoter, and a neomycin resistance gene. Stably expressing cells were selected by growth in G418. Expression of syndecan-1 was verified by Northern and immunoblot analysis and immunoprecipitation of 35SO4-labeled proteoglycans

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CHEN, Ligong, John R. COUCHMAN, Jacqueline SMITH, and Anne WOODS. "Molecular characterization of chicken syndecan-2 proteoglycan." Biochemical Journal 366, no. 2 (2002): 481–90. http://dx.doi.org/10.1042/bj20020711.

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A partial syndecan-2 sequence (147bp) was obtained from chicken embryonic fibroblast poly(A)+ RNA by reverse transcription–PCR. This partial sequence was used to produce a 5′-end-labelled probe. A chicken liver cDNA library was screened with this probe, and overlapping clones were obtained encompassing the entire cDNA of 3kb. The open reading frame encodes a protein of 201 amino acids. The cytoplasmic domain is identical with that of mammalian syndecan-2, and highly similar to those of Xenopus laevis and zebrafish syndecan-2. The transmembrane domain is identical with that of mammalian and zeb

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Steinfeld, R., H. Van Den Berghe, and G. David. "Stimulation of fibroblast growth factor receptor-1 occupancy and signaling by cell surface-associated syndecans and glypican." Journal of Cell Biology 133, no. 2 (1996): 405–16. http://dx.doi.org/10.1083/jcb.133.2.405.

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The formation of distinctive basic FGF-heparan sulfate complexes is essential for the binding of bFGF to its cognate receptor. In previous experiments, cell-surface heparan sulfate proteoglycans extracted from human lung fibroblasts could not be shown to promote high affinity binding of bFGF when added to heparan sulfate-deficient cells that express FGF receptor-1 (FGFR1) (Aviezer, D., D. Hecht, M. Safran, M. Eisinger, G. David, and A. Yayon. 1994. Cell 79:1005-1013). In alternative tests to establish whether cell-surface proteoglycans can support the formation of the required complexes, K562

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SCHOFIELD, Karen P., John T. GALLAGHER, and Guido DAVID. "Expression of proteoglycan core proteins in human bone marrow stroma." Biochemical Journal 343, no. 3 (1999): 663–68. http://dx.doi.org/10.1042/bj3430663.

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Heparan sulphate proteoglycans (HSPGs) present on the surface of bone marrow stromal cells and in the extracellular matrix (ECM) have important roles in the control of adhesion and growth of haemopoietic stem and progenitor cells. The two main groups of proteoglycans which contain heparan sulphate chains are members of the syndecan and glypican families. In this study we have identified the main surface membrane and matrix-associated HSPGs present in normal human bone marrow stroma formed in long-term culture. Proteoglycans were extracted from the adherent stromal layers and treated with hepar

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Chappell, Daniel, Matthias Jacob, Markus Rehm, et al. "Heparinase selectively sheds heparan sulphate from the endothelial glycocalyx." Biological Chemistry 389, no. 1 (2008): 79–82. http://dx.doi.org/10.1515/bc.2008.005.

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Abstract A healthy vascular endothelium is coated by the endothelial glycocalyx. Its main constituents are transmembrane syndecans and bound heparan sulphates. This structure maintains the physiological endothelial permeability barrier and prevents leukocyte and platelet adhesion, thereby mitigating inflammation and tissue oedema. Heparinase, a bacterial analogue to heparanase, is known to attack the glycocalyx. However, the exact extent and specificity of degradation is unresolved. We show by electron microscopy, immunohistological staining and quantitative measurements of the constituent par

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Teel, A. L., and H. J. Yost. "Embryonic expression patterns of Xenopus syndecans." Mechanisms of Development 59, no. 2 (1996): 115–27. http://dx.doi.org/10.1016/0925-4773(96)00584-9.

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Woods, Anne, and John R. Couchman. "Syndecans: synergistic activators of cell adhesion." Trends in Cell Biology 8, no. 5 (1998): 189–92. http://dx.doi.org/10.1016/s0962-8924(98)01244-6.

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