Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor

Yayon, Avner; Klagsbrun, Michael; Esko, Jeffrey D.; Leder, Philip; Ornitz, David M.

doi:10.1016/0092-8674(91)90512-w

Cited by 2,339 publications

(1,453 citation statements)

References 34 publications

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“…Loss of SDC3 in satellite cells prevents self‐renewal and rehoming of satellite cells to their niche, maintaining a pool of activated, proliferating cells that largely ameliorate muscular dystrophy in mdx mice 40. It has been shown that the binding of FGF2 to its receptor requires prior binding to heparan sulfate 15, and heparan sulfate is required for BMP‐7 signalling 41.…”

Section: Discussionmentioning

confidence: 99%

Syndecan‐4 influences mammalian myoblast proliferation by modulating myostatin signalling and G1/S transition

et al. 2018

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Myostatin, a TGF‐β superfamily member, is a negative regulator of muscle growth. Here we describe how myostatin activity is regulated by syndecan‐4, a ubiquitous transmembrane heparan sulfate proteoglycan. During muscle regeneration the levels of both syndecan‐4 and promyostatin decline gradually after a sharp increase, concurrently with the release of mature myostatin. Promyostatin and syndecan‐4 co‐immunoprecipitate, and the interaction is heparinase‐sensitive. ShRNA‐mediated silencing of syndecan‐4 reduces C2C12 myoblast proliferation via blocking the progression from G1‐ to S‐phase of the cell cycle, which is accompanied by elevated levels of myostatin and p21(Waf1/Cip1), and decreases in cyclin E and cyclin D1 expression. Our results suggest that syndecan‐4 functions as a reservoir for promyostatin regulating the local bioavailability of mature myostatin.

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Section: Discussionmentioning

confidence: 99%

Syndecan‐4 influences mammalian myoblast proliferation by modulating myostatin signalling and G1/S transition

et al. 2018

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“…Among these, some may be considered "HS-dependent", since in vitro manipulations that remove, or prevent the sulfation of, cellular HS result in greatly decreased growth factor binding to, and activation of, signaling receptors. The best characterized HS-dependent growth factors are FGF-1 and FGF-2, but other FGFs, HB-EGF, wingless (a member of the Wnt family) and probably several other growth factors belong to this group (Rapraeger et al, 1991;Yayon et al, 1991;Aviezer and Yayon, 1994;Tessler et al, 1994;Zioncheck et al, 1995;Reichsman et al, 1996). Models that have been put forth to explain HS-dependence include ones in which binding of HS to growth factor, receptor, or both directly alters affinity (e.g., through cross-linking, dimerization, or induction of a conformational change [Kan et al, 1993;Pantoliano et al, 1994;Spivak-Kroizman et al, 1994]).…”

Section: Rotes Of Pgs In Growth Factor Signatingmentioning

confidence: 99%

Proteoglycans: Master regulators of molecular encounter?

Lander

1998

Matrix Biology

103

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“…Cell response to FGF-2 is mediated by a dual receptor system consisting of low and high a nity binding sites (Yayon et al, 1991). The latter belongs to the FGF tyrosine kinase receptor (RTK) family, which consists of four distinct members named FGFR-1 through FGFR-4 (Kavanaugh and Williams, 1994;Vainikka et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

Functional Rac-1 and Nck signaling networks are required for FGF-2-induced DNA synthesis in MCF-7 cells

Liu

Chevet

Kebache³

et al. 1999

Oncogene

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The e ects of Fibroblast Growth Factor-2 (FGF-2) on breast cancer cell DNA synthesis are controversial. To elucidate the mechanisms by which FGF-2 stimulates or inhibits DNA synthesis, we analysed FGF-2 signaling pathways in breast cancer MCF-7 and MCF-7 cells overexpressing Ha-Ras (MCF-7ras). We found that FGF-2-induction of DNA synthesis correlates with Ras transient activation, FRS-2 tyrosine phosphorylation and low level of expression of p66 Shc . In addition, Nckassociated proteins are highly tyrosine phosphorylated and JNK reaches a higher level of activation when FGF-2 triggers DNA synthesis. Interestingly upon FGF-2 treatment, JNK activation and DNA synthesis are dependent on Rac-1 activity. These results con®rm that in MCF-7 cells, induction of DNA synthesis by FGF-2 requires a transient activation of the Ras/MAPK cascade and demonstrates for the ®rst time that intact Rac-1 and Nck signaling networks are required.

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Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor

Cited by 2,339 publications

References 34 publications

Syndecan‐4 influences mammalian myoblast proliferation by modulating myostatin signalling and G1/S transition

Syndecan‐4 influences mammalian myoblast proliferation by modulating myostatin signalling and G1/S transition

Proteoglycans: Master regulators of molecular encounter?

Functional Rac-1 and Nck signaling networks are required for FGF-2-induced DNA synthesis in MCF-7 cells

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