PMID: 9165099Apr 25, 1997Paper

Difference in interaction of fibronectin with type I collagen and type IV collagen

Biochimica Et Biophysica Acta
M ShimizuJ Koga

Abstract

In our studies on fibronectin, difference in binding to type I collagen and type IV collagen was observed and analysed. Four different fragments, which consist of I6-II1-II2-I7-I8-I9, I6-II1-II2-I7, I6-II1-II2, and I8-I9 within the collagen binding domain, have been isolated from proteolytic digests of fibronectin. The N-terminal fragments of the collagen binding domain showed the binding affinity to both of type I and type IV collagens. On the other hand, the C-terminal portion of the domain, I8-I9, only bound to type I collagen. The newly developed monoclonal antibody FN 40, which recognizes type I9 homology repeat of the collagen binding domain, inhibited the binding of fibronectin to type I collagen in a dose-dependent manner. Three overlapping fragments, I6-II1-II2-I7, I6-II1-II2-I7-I8, and I7-I8-I9, which have been expressed in Escherichia coli, showed the similar binding affinity to type IV collagen, whereas the fragment containing type I9 repeat (I7-I8-I9) showed the significantly stronger binding activity to type I collagen. In addition, the expressed fragment lacking I9 competitively inhibited the binding of fibronectin to type IV collagen. In contrast, the interference of this fragment to type I collagen binding acti...Continue Reading

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Citations

Nov 28, 2008·Molecular Biology of the Cell·Laetitia SabatierDieter P Reinhardt
Sep 4, 2012·Comptes rendus biologies·Melissa SgariotoChristophe Egles
Oct 8, 2015·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Xiao YangKaustabh Ghosh
Sep 10, 2002·Laboratory Investigation; a Journal of Technical Methods and Pathology·Shoji KagamiYasuhiro Kuroda
Mar 25, 2021·Graefe's Archive for Clinical and Experimental Ophthalmology = Albrecht Von Graefes Archiv Für Klinische Und Experimentelle Ophthalmologie·Annalisa AlteraEugenio Bertelli

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