Cell surface phosphatidylinositol-anchored heparan sulfate proteoglycan initiates mouse melanoma cell adhesion to a fibronectin-derived, heparin-binding synthetic peptide

Drake, Sandra L.; Klein, David J.; Mickelson, Daniel J.; Oegema, Theodore R.; Furcht, Leo T.; McCarthy, James B.

doi:10.1083/jcb.117.6.1331

Cited by 85 publications

(68 citation statements)

References 53 publications

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“…The present study findings, which showed that addition of heparan sulfate or treatment of the cell surface of SC with heparitinase reduced adhesion of SC onto EDA+ FN, suggest that heparan sulfate proteoglycans are responsible for the adhesion of (30). Furthermore, adhesion of murine melanoma cells or of human embryo fibroblasts onto the HepZderived peptide was inhibited by the addition of heparin or the treatment of cells with heparitinase (31).…”

Section: Discussionsupporting

confidence: 52%

Adherence of synovial cells on EDA‐containing fibronectin

Hino

Maeda

Sekiguchi

et al. 1996

Arthritis & Rheumatism

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Objective. To investigate the role of EDAcontaining fibronectin (EDA+ FN), a splice variant of FN detectable in association with cellular transformation, in the adherence of synovial cells (SC) on rheumatoid cartilage surface.Methods. migration, wound healing, and oncogenic transformation (1). FN is mainly composed of 2 subunits of protein that each have a molecular weight of -250 kd and are connected by disulfide bonds near the carboxyl terminus (2) (Figure 1). Multiple isoforms of FN are produced from a single gene by alternative splicing at 3 distinct sites, EDA, EDB, and IIICS (3). FN produced by hepatocytes and commonly found in plasma, i.e., plasma FN (pFN), lacks the EDA and EDB regions. However, FN produced by most other tissues, i.e., cellular FN, contains the EDA and/or EDB regions of FN in various combinations (4).Previous studies have shown that the level of FN that contains the EDA and/or EDB regions is especially increased during the early stage of fetal development (5), malignant transformation (6), and wound healing (7). Furthermore, studies have indicated that the plasma level of EDA-containing FN (EDA+ FN) is increased in patients with vascular injury (S), malignant tumor (9), and, particularly, rheumatoid arthritis (RA) (10

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Section: Discussionsupporting

confidence: 52%

Adherence of synovial cells on EDA‐containing fibronectin

Hino

Maeda

Sekiguchi

et al. 1996

Arthritis & Rheumatism

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“…A second class of molecules capable of mediating cellmatrix interactions is the cell surface heparan sulfate and chondroitin sulfate PGs. Cell surface heparan sulfate and chondroitin sulfate have been implicated in cell adhesion to several sites in the III 12-14 domains of HBFN-f (25)(26)(27)(28)(29), suggesting that binding of HBFN-f to cell surface PGs may trigger collagenase induction.…”

Section: Discussionmentioning

confidence: 99%

“…Several sites in the heparin-binding domain that are COOH-terminal to the central cell-binding domain also interact with the cell surface. Several peptides from domain III 12-14 support cell attachment with varying affinities (24)(25)(26)(27)(28)(29). The IIICS, or the variable (V) region, contains the integrin-binding sites, CS-1 and CS-5 (30)(31)(32)(33)(34).…”

mentioning

confidence: 99%

A fibronectin fragment induces type II collagen degradation by collagenase through an interleukin-1?mediated pathway

Yasuda¹,

Poole²

2002

Arthritis & Rheumatism

116

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“…Alternatively, MMP induction by COOH-HBFNf-stimulated RSF may involve other mechanisms. Because cell surface heparan sulfate and chondroitin sulfate are implicated in cell adhesion to several sites in the III12 to 14 domains of COOH-HBFN-f (Drake et al, 1992;Iida et al, 1992), binding of COOH-HBFN-f with cell surface proteoglycans may contribute to MMP induction, which is under investigation.…”

Section: Yasuda Et Almentioning

confidence: 99%

Matrix Metalloproteinase Production by COOH-Terminal Heparin-Binding Fibronectin Fragment in Rheumatoid Synovial Cells

Yasuda

Shimizu

Nakagawa

et al. 2003

Laboratory Investigation

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SUMMARY:Fibronectin with IIICS region is present in rheumatoid synovium, and fibronectin fragments are increased in rheumatoid joints. We investigated the ability of COOH-terminal heparin-binding fibronectin fragment (COOH-HBFN-f) containing IIICS to induce matrix metalloproteinase (MMP) production and the role of mitogen-activated protein kinase (MAPK) pathway and CS-1 sequence that can bind ␣4␤1 integrin in MMP induction by COOH-HBFN-f in rheumatoid synovial fibroblasts (RSF). When RSF in monolayer culture were incubated with COOH-HBFN-f, COOH-HBFN-f stimulated the production of MMP-1, MMP-3, and MMP-13 by RSF in association with activation of extracellular signal-regulated kinase, p38 MAPK, and c-Jun NH 2 -terminal kinase. Immunoprecipitation of cell lysates demonstrated the presence of ␣4 integrin in cultured RSF. Similar to COOH-HBFN-f, treatment with CS-1 synthetic peptide derived from IIICS resulted in increased MMP production and activation of the kinases, although the MMP levels were low. Preincubation of RSF with anti-␣4 integrin antibody resulted in partial suppression of the COOH-HBFN-f-stimulated MMP production. Inhibition studies using protein kinase inhibitors (PD98059 and SB203580) showed that those MAPK pathways contributed to MMP up-regulation by COOH-HBFN-f and CS-1. Thus, the present results have clearly shown that COOH-HBFN-f and CS-1 stimulate MMP production in association with activation of MAPK pathways in RSF. Integrin ␣4␤1 may be partially involved in the MMP induction by COOH-HBFN-f. (Lab Invest 2003, 83:153-162).

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Cell surface phosphatidylinositol-anchored heparan sulfate proteoglycan initiates mouse melanoma cell adhesion to a fibronectin-derived, heparin-binding synthetic peptide

Cited by 85 publications

References 53 publications

Adherence of synovial cells on EDA‐containing fibronectin

Adherence of synovial cells on EDA‐containing fibronectin

A fibronectin fragment induces type II collagen degradation by collagenase through an interleukin-1?mediated pathway

Matrix Metalloproteinase Production by COOH-Terminal Heparin-Binding Fibronectin Fragment in Rheumatoid Synovial Cells

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