Cell surface heparan sulfate mediates some adhesive responses to glycosaminoglycan-binding matrices, including fibronectin.

Laterra, John; Silbert, Jeremiah E.; Culp, Lloyd A.

doi:10.1083/jcb.96.1.112

Cited by 266 publications

(153 citation statements)

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“…This molecule has a core protein that is rooted in the lipid bilayer of the plasma membrane of most types of vertebrate and invertebrate cells (41,51). A number of studies have indicated the potential roles of heparan sulfate proteoglycans in the regulation of cell growth and transformation (15,61,77,84), differentiation processes (10), cell adhesion (12,44), and neuromuscular junction formation (3). In addition, heparan sulfate acts as a receptor, not only for viruses, but also for bacteria and parasites (11,62,65,69).…”

Section: Discussionmentioning

confidence: 99%

Genogroup II Noroviruses Efficiently Bind to Heparan Sulfate Proteoglycan Associated with the Cellular Membrane

Tamura

Natori

Kobayashi

et al. 2004

J Virol

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Norovirus (NV), a member of the family Caliciviridae, is one of the important causative agents of acute gastroenteritis. In the present study, we found that virus-like particles (VLPs) derived from genogroup II (GII) NV were bound to cell surface heparan sulfate proteoglycan. Interestingly, the VLPs derived from GII were more than ten times likelier to bind to cells than were those derived from genogroup I (GI). Heparin, a sulfated glycosaminoglycan, and suramin, a highly sulfated derivative of urea, efficiently blocked VLP binding to mammalian cell surfaces. The reagents known to bind to cell surface heparan sulfate, as well as the enzymes that specifically digest heparan sulfate, markedly reduced VLP binding to the cells. Treatment of the cells with chlorate revealed that sulfation of heparan sulfate plays an important role in the NV-heparan sulfate interaction.

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Section: Discussionmentioning

confidence: 99%

Genogroup II Noroviruses Efficiently Bind to Heparan Sulfate Proteoglycan Associated with the Cellular Membrane

Tamura

Natori

Kobayashi

et al. 2004

J Virol

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“…It is evident that heparan sulfate proteoglycans also play a role in FN-mediated fibroblast attachment and spreading (23)(24)(25)(26)(27)34), since they are found at cell-substrate attachment sites (23,26,27). Thus it is possible that both the heparinbinding and cell-binding FN domains are involved in fibroblast adhesion, FC formation, microfilament bundle development, and fibronexus morphogenesis.…”

Section: F Ibronectin (Fn) ~ Is a Large Glycoprotein Found Inmentioning

confidence: 99%

The fibronectin cell attachment sequence Arg-Gly-Asp-Ser promotes focal contact formation during early fibroblast attachment and spreading.

Singer¹,

Kawka²,

Scott³

et al. 1987

The Journal of Cell Biology

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Abstract. Cultured fibroblasts form focal contacts (FCs) associated with actin microfilament bundles (MFBs) during attachment and spreading on serum-or fibronectin (FN)-coated substrates. To determine if the minimum cellular adhesion receptor recognition signal Arg-Gly-Asp-Ser (RGDS) is sufficient to promote FC and MFB formation, rat (NRK), hamster (Nil 8), and mouse (Balb/c 3T3) fibroblasts in serum-free media were plated on substrates derivatized with small synthetic peptides containing RGDS. These cultures were studied with interference reflection microscopy to detect FCs, Normarski optics to identify MFBs, and immunofluorescence microscopy to observe endogenous FN fiber formation. By 1 h, 72-78 % of the NRK and Nil 8 cells plated on RGDS-containing peptide had focal contacts without accompanying FN fibers, while these fibroblasts lacked FCs on control peptide. This early FC formation was followed by the appearance of coincident MFBs and colinear FN fbers forming fibronexuses at 4 h. NRK and Nil 8 cultures on substrates coated with native FN or 75,000-D FN-cell binding fragment showed similar kinetics of FC and MFB formation. In contrast, the Balb/c 3T3 mouse fibroblasts plated on Gly-Arg-Gly-Asp-Ser peptidederivatized substrates, or on coverslips coated with 75,000-D FN cell-binding fragment, were defective in FC formation. These results demonstrate that the apparent binding of substrate-linked RGDS sequences to cell surface adhesion receptors is sufficient to promote early focal contact formation followed by the appearance of fibronexuses in some, but not all, fibroblast lines. F IBRONECTIN (FN) ~ is a large glycoprotein found in plasma and the connective tissue extracellular matrix, which functions primarily in promoting cellular adhesion to solid substrates. It is composed of several protease-resistant functional domains that can bind independently to a number of important substrates, including fibrin, collagen, heparin, and various cell surface components (18,35). The FN cell-attachment domain has recently been shown to bind to a 140-kD FN receptor complex (1, 2, 33) that codistributes with microfilament bundles at cell-substrate adhesion sites (4, 5). Through the use of small synthetic peptides deduced from the primary structure of the FN cellattachment domain, the tetrapeptide Arg-Gly-Asp-Ser has been found to be the minimal FN sequence with cell attachment activity (29-31).Arg-Gly-Asp-Val, a sequence closely related to Arg-GlyAsp-Ser, is present in vitronectin, another protein with potent cell-adhesive properties that is localized with FN in the extracellular matrix (15,16,44). The vitronectin receptor has a different molecular mass than the FN receptor, and specifi-1. Abbreviations used in this paper: DIC, differential interference contrast; FC, focal contact(s); FN, fibronectin; HBSA, heat denatured BSA; IFM, immunofluorescence microscopy; IRM, interference reflection microscopy; SPDP, 3-(2-pyridol-dithio) propionic acid N-hydroxy-succinimide ester.cally binds vitronectin rather than FN. However, bo...

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“…These substrata support cell adhesion through heparan sulfate proteoglycanmediated interactions (Laterra et al, 1983;Lark et al, 1985;Izzard et al, 1986). The heparin-binding domain of fibronectin did not support H9c2 cell attachment.…”

Section: Jc Adams Molecular Biology Of the Cell 2348mentioning

confidence: 99%

Characterization of Cell–Matrix Adhesion Requirements for the Formation of Fascin Microspikes

Adams

1997

MBoC

106

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Cell adhesion to thrombospondin-1 (TSP-1) correlates with assembly of cell-substratum contact structures that contain fascin microspikes. In this analysis, cell-matrix requirements for assembly of fascin microspikes were examined in detail. In six cell lines, cell spreading on a TSP-1 substratum correlated with expression of fascin protein and formation of fascin microspikes. Microspikes were not formed by H9c2 cells adherent on fibronectin, vitronectin, collagen IV, or platelet factor 4. However, both fascin microspikes and focal contacts were assembled by cells adherent on laminin-1. Using mixed substrata containing different proportions of TSP-1, and fibronectin, fascin microspike formation by H9c2 and C2C12 cells was found to be reduced on substrata containing 25% fibronectin and abolished on substrata containing 75% fibronectin. Adhesion to intermediate mixtures of TSP-1 and fibronectin resulted in coassembly of fascin microspikes and focal contacts, colocalization of fascin with actin stress fiber bundles and altered distributions of ␤1 integrins, cortical ␣-actinin, and tropomyosin. In cells adherent on 50% TSP-1:50% fibronectin, GRGDSP peptide treatment decreased focal contact assembly and altered cytoskeletal organization but did not inhibit microspike assembly. Treatment with chondroitin sulfate A or p-nitrophenol ␤-d-xylopyranoside decreased microspike formation and modified cytoskeletal organization but did not inhibit focal contact formation. In polarized migratory and postmitotic C2C12 cells, fascin microspikes and ruffles were localized at leading edges and TSP matrix deposition was also concentrated in this region. Depletion of matrix TSP by heparin treatment correlated with decreased microspike formation and cell motility. Thus, the balance of adhesive receptors ligated at the cell surface during initial cell-matrix attachment serves to regulate the type of substratum adhesion contact assembled and subsequent cytoskeletal organization. A role for fascin microspikes in cell motile behavior is indicated. INTRODUCTIONIt has long been appreciated that the interactions of cells with extracellular matrix (ECM) macromolecules play a role in regulating cell adhesion, shape, and movement: processes that are central to tissue organization in metazoan organisms and that contribute to many pathological conditions if disregulated (reviewed by Hynes and Lander, 1992;Gumbiner, 1996).To date, the cell-substratum contact structure most thoroughly studied in vitro has been the focal contact, or focal adhesion, that corresponds morphologically to a site of very close apposition between the ventral plasma membrane of a cell and its substratum (Abercrombie et al., 1971;Izzard and Lochner, 1976;Heath and Dunn, 1978). In molecular terms, focal contacts are distinguished by the colocalization of ligand-occupied clustered integrins on the cell surface with the termini of actin microfilament bundles and a characteristic assembly of intracellular proteins including talin, vinculin, paxillin, and focal adhesion kinase (FAK...

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Cell surface heparan sulfate mediates some adhesive responses to glycosaminoglycan-binding matrices, including fibronectin.

Cited by 266 publications

References 50 publications

Genogroup II Noroviruses Efficiently Bind to Heparan Sulfate Proteoglycan Associated with the Cellular Membrane

Genogroup II Noroviruses Efficiently Bind to Heparan Sulfate Proteoglycan Associated with the Cellular Membrane

The fibronectin cell attachment sequence Arg-Gly-Asp-Ser promotes focal contact formation during early fibroblast attachment and spreading.

Characterization of Cell–Matrix Adhesion Requirements for the Formation of Fascin Microspikes

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