Portal de Periódicos da CAPES

Role of type III homology repeats in cell adhesive function within the cell-binding domain of fibronectin.

1991; Elsevier BV; Volume: 266; Issue: 5 Linguagem: Inglês

10.1016/s0021-9258(18)49952-8

1083-351X

Fusao Kimizuka, Yoichi Ohdate, Yasutoshi Kawase, Tomoko Shimojo, Yuzuru Taguchi, Kimikazu Hashino, S Goto, Hidetaka Hashi, Itaru Kato, Kiyotoshi Sekiguchi,

Monoclonal and Polyclonal Antibodies Research

Recombinant fibronectin (FN) fragments and their mutant proteins were produced to elucidate the role of type I11 homology repeats in cell adhesive activity within the cell-binding domain of FN. Cell adhesive activity of the 11.5-kDa fragment, the cell attachment site of the cell-binding domain, was <0.1% that of native FN despite the presence of the Arg-Gly-Asp-Ser sequence.The activity increased as type I11 homology repeats were added to the N terminus of the 11.5-kDa fragment, and a 52-kDa fragment with four additional type I11 repeats had almost the same activity of native FN.Deletion of Arg-Gly-Asp from the fully active fragments completely abolished the cell adhesive activity.Deletion of one or two repeats from the 52-kDa fragment affected the extent of the cell adhesive activity, the degree of the effect being inversely correlated with the distance of the deletion from the type I11 repeat containing Arg-Gly-Asp-Ser.Rearrangement of type I11 repeats caused much loss of activity.These results suggest that the number and kinds of type I11 repeats and their correct alignment rather than the putative synergistic site decide the extent of the spe- cific cell adhesive activity.