Interaction of Thrombospondin-1 and Heparan Sulfate from Endothelial Cells

Feitsma, Kirsten; Hausser, Heinz; Robenek, Horst; Kresse, Hans; Vischer, Peter

doi:10.1074/jbc.275.13.9396

Cited by 38 publications

(25 citation statements)

References 51 publications

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“…Endothelial cell HS chains accumulated in the cell layer were composed of GlcA/IdoA-GlcNAc (54.1%), GlcA/IdoA-GlcNS (33.3%) and IdoA(2S)-GlcNS (12.6%), while those accumulated in the conditioned medium were composed of GlcA/IdoA-GlcNAc (50.8%), GlcA/IdoAGlcNS (30.8%), IdoA(2S)-GlcNS (15.1%), a trace of GlcA/IdoA-GlcNS(6S) and IdoA(2S)-GlcNS(6S). The high proportion of the N-acetylated disaccharide units (GlcA/IdoA-GlcNAc) together with the low proportion of IdoA(2S)-GlcNS(± 6S) disaccharides is consistent with previous reports 7,23,24) where endothelial cell HS was analyzed by strong anion exchange HPLC. Lead significantly decreased the total number of HS disaccharides accumulated in both the cell layer and the conditioned medium as a result of decrease in the disaccharides of GlcA/IdoAGlcNAc, GlcA/IdoA-GlcNS and IdoA(2S)-GlcNS.…”

Section: Introductionsupporting

confidence: 77%

Disaccharide Composition of Glycosaminoglycan Chains in Growing Vascular Endothelial Cells in Culture after Exposure to Lead

Fujiwara

Kaji

Plaas

2004

JOURNAL OF HEALTH SCIENCE

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Section: Introductionsupporting

confidence: 77%

Disaccharide Composition of Glycosaminoglycan Chains in Growing Vascular Endothelial Cells in Culture after Exposure to Lead

Fujiwara

Kaji

Plaas

2004

JOURNAL OF HEALTH SCIENCE

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“…Since both TSP1 and bFGF bind HSPGs, the ability of TSP1 to inhibit bFGF-induced responses is suggested to occur through competitive inhibition for binding to HSPGs (Vogel et al, 1993). However, whereas both TSP1 and bFGF bind the HSPG perlecan on endothelial cells, the sites mediating these interactions are distinct (Feitsma et al, 2000). In addition, hep I-induced focal adhesion disassembly is insensitive to heparitinase treatment, indicating that hep I does not bind endothelial cell HSPGs and thus does not inhibit bFGF signaling though competition for endogenous HSPGs (Murphy-Ullrich et al, 1993).…”

Section: Discussionmentioning

confidence: 99%

Thrombospondin signaling through the calreticulin/LDL receptor-related protein co-complex stimulates random and directed cell migration

Orr

Elzie

Kucik

et al. 2003

Journal of Cell Science

160

162

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The matricellular extracellular matrix protein thrombospondin-1 (TSP1)stimulates focal adhesion disassembly through a sequence (known as the hep I peptide) in its heparin-binding domain. This mediates signaling through a receptor co-complex involving calreticulin and low-density lipoprotein (LDL)receptor-related protein (LRP). We postulate that this transition to an intermediate adhesive state enhances cellular responses to dynamic environmental conditions. Since cell adhesion dynamics affect cell motility,we asked whether TSP1/hep I-induced intermediate adhesion alters cell migration. Using both transwell and Dunn chamber assays, we demonstrate that TSP1 and hep I gradients stimulate endothelial cell chemotaxis. Treatment with focal adhesion-labilizing concentrations of TSP1/hep I in the absence of a gradient enhances endothelial cell random migration, or chemokinesis,associated with an increase in cells migrating, migration speed, and total cellular displacement. Calreticulin-null and LRP-null fibroblasts do not migrate in response to TSP1/hep I, nor do endothelial cells treated with the LRP inhibitor receptor-associated protein (RAP). Furthermore, TSP1/hep I-induced focal adhesion disassembly is associated with reduced chemotaxis to basic fibroblast growth factor (bFGF) but enhanced chemotaxis to acidic(a)FGF, suggesting differential modulation of growth factor-induced migration. Thus, TSP1/hep I stimulation of intermediate adhesion regulates the migratory phenotype of endothelial cells and fibroblasts, suggesting a role for TSP1 in remodeling responses.

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“…The inhibitory effects of sodium chlorate on cell adhesion to CTGF was reversed by the inclusion of 10 mM Na 2 SO 4 in the culture medium, verifying that this inhibitory effect is mediated through a sulfation block (29). To substantiate the finding that cell surface sulfated proteoglycans are required for cell adhesion to CTGF, fibroblasts were treated with heparinase I, an enzyme that targets highly sulfated heparan sulfate proteoglycans (33,34). Heparinase I-treated cells were unable to adhere to CTGF, whereas the same treated cells adhered to fibronectin or vitronectin indifferently (Fig.…”

Section: Adhesion Of Primary Human Skinmentioning

confidence: 99%

The Angiogenic Factors Cyr61 and Connective Tissue Growth Factor Induce Adhesive Signaling in Primary Human Skin Fibroblasts

Chen

Lau

2001

Journal of Biological Chemistry

288

279

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The angiogenic inducers cysteine-rich angiogenic protein 61 (Cyr61) and connective tissue growth factor (CTGF) are structurally related, extracellular matrixassociated heparin-binding proteins. Both can stimulate chemotaxis and promote proliferation in endothelial cells and fibroblasts in culture and induce neovascularization in vivo. Encoded by inducible immediate early genes, Cyr61 and CTGF are synthesized upon growth factor stimulation in cultured fibroblasts and during cutaneous wound healing in dermal fibroblasts. Recently, we have shown that adhesion of primary human fibroblasts to immobilized Cyr61 is mediated through integrin ␣ 6 ␤ 1 and cell surface heparan sulfate proteoglycans (HSPGs) (Chen, N., Chen, C.-C., and Lau, L.F. (2000) J. Biol. Chem. 275, 24953-24961), providing the first demonstration of an absolute requirement for HSPGs in integrin-mediated cell attachment. We show in this study that CTGF also mediates fibroblast adhesion through the same mechanism and demonstrate that fibroblasts adhesion to immobilized Cyr61 or CTGF induces distinct adhesive signaling responses consistent with their biological activities. Compared with fibroblast adhesion to fibronectin, laminin, or type I collagen, cell adhesion to Cyr61 or CTGF induces 1) more extensive and prolonged formation of filopodia and lamellipodia, concomitant with formation of integrin ␣ 6 ␤ 1 -containing focal complexes localized at leading edges of pseudopods; 2) activation of intracellular signaling molecules including focal adhesion kinase, paxillin, and Rac with similar rapid kinetics; 3) sustained activation of p42/p44 MAPKs lasting for at least 9 h; and 4) prolonged gene expression changes including up-regulation of MMP-1 (collagenase-1) and MMP-3 (stromelysin-1) mRNAs and proteins sustained for at least 24 h. Together, these results establish Cyr61 and CTGF as bona fide adhesive substrates with specific signaling capabilities, provide a molecular basis for their activities in fibroblasts through integrin ␣ 6 ␤ 1 and HSPG-mediated signaling during attachment and indicate that these proteins may function in matrix remodeling through the activation of metalloproteinases during angiogenesis and wound healing.

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Interaction of Thrombospondin-1 and Heparan Sulfate from Endothelial Cells

Cited by 38 publications

References 51 publications

Disaccharide Composition of Glycosaminoglycan Chains in Growing Vascular Endothelial Cells in Culture after Exposure to Lead

Disaccharide Composition of Glycosaminoglycan Chains in Growing Vascular Endothelial Cells in Culture after Exposure to Lead

Thrombospondin signaling through the calreticulin/LDL receptor-related protein co-complex stimulates random and directed cell migration

The Angiogenic Factors Cyr61 and Connective Tissue Growth Factor Induce Adhesive Signaling in Primary Human Skin Fibroblasts

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