Q. Zhou et al., THE HEMORRHAGIN CATROCOLLASTATIN INHIBITS COLLAGEN-INDUCED PLATELET-AGGREGATION BY BINDING TO COLLAGEN VIA ITS DISINTEGRIN-LIKE DOMAIN, Biochemical and biophysical research communications, 219(3), 1996, pp. 720-726
Catrocollastatin, a 50 kDa snake venom protein purified from Crotalus
atrox, specifically inhibits platelet-collagen adhesion and collagen-i
nduced aggregation. Catrocollastatin is composed of an N-terminal doma
in, a metalloproteinase domain. a disintegrin-like domain and a cystei
ne-rich C-terminal domain, The present studies show that catrocollasta
tin exerts its effect by binding to collagen. Based on the amino acid
sequence and homology analysis, a cyclic oligopeptide corresponding to
a conservative fragment containing the sequence SECD in the disintegr
in-like domain has been synthesized. Like its protein parent, the synt
hetic peptide inhibits collagen-induced aggregation and possesses the
ability to bind to collagen. This is the first snake venom protein wit
h a disintegrin-like structure shown to bind to an integrin ligand mat
rix molecule instead of an integrin. (C) 1996 Academic Press, Inc.