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J. Biol. Chem., Vol. 266, Issue 5, 2824-2830, Feb, 1991
D Seiffert and DJ Loskutoff
The interaction between type 1 plasminogen activator inhibitor (PAI-1) and
fragments of vitronectin (Vn) was investigated. The PAI-1-binding domain
was not destroyed when Vn was cleaved by treatment with either acid or
CNBr. Acid-cleaved Vn was fractionated by sodium dodecyl
sulfate-polyacrylamide gel electrophoresis and analyzed by PAI-1 ligand
binding. The smallest fragment (Mr 40,000) that retained PAI-1 binding
function was sequenced and shown to contain the NH2 terminus of the
molecule. Further cleavage of this fragment by treatment with CNBr
generated a Mr 35,000 fragment (Pro52-Asp239) that did not interact with
PAI-1, and a Mr 6,000 NH2-terminal fragment (Asp1-Met51) that spanned the
somatomedin B domain and contained the RGD (cell binding) sequence. The
purified Mr 6,000 fragment competed with immobilized Vn for PAI-1 binding,
and formed complexes with activated PAI-1. These complexes could be
immunoprecipitated by antibodies to PAI-1. Synthetic peptides containing
the RGD sequence had no effect on the binding of this fragment to PAI-1.
These results suggest that the cell-binding and PAI-1 binding sequences of
Vn occupy distinct regions in the NH2- terminal somatomedin B domain of the
molecule.
Evidence that type 1 plasminogen activator inhibitor binds to the somatomedin B domain of vitronectin
Committee on Vascular Biology, Research Institute of Scripps Clinic, La Jolla, California 92037.
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