Vitronectin is a multifunctional serum protein which provides a unique
regulatory link between cell adhesion, humoral defense mechanism and
the hemostatic system, and the heparin-binding properties of vitronect
in are thought to have participated in various functional aspects, In
addition to the carboxy-terminal glycosaminoglycan-binding motif, we r
eport on two novel heparin-binding domains which were identified using
phage display technique, One heparin-binding domain is located betwee
n amino acids Asp(82) and Cys(137) at the end of the connector region,
while the other is in the second hemopexin-type repeat, between amino
acids Lys(175) and Asp(219) of the vitronectin molecule, Our findings
may shed new light to the activities of vitronectin and its binding t
o cells, which could not be explained solely on the basis of the known
heparin-binding domain. (C) 1997 Federation of European Biochemical S
ocieties.