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J. Biol. Chem., Vol. 264, Issue 7, 3742-3749, 03, 1989
SC Lam, EF Plow, SE D'Souza, DA Cheresh, AL Frelinger 3d and MH Ginsberg
Glycoprotein IIb-IIIa is the most prominent Arg-Gly-Asp (RGD)-binding
adhesion receptor on platelets. By affinity chromatography on an
immobilized RGD peptide, we have investigated the possible existence of
other platelet-associated adhesion receptors that bind RGD peptides. When
an octyl glucoside extract of surface-radioiodinated platelets was applied
to an affinity matrix of KYGRGDS-coupled Sepharose 4B, a 160- kDa-labeled
protein (P160) and GPIIb-IIIa bound and were specifically eluted by soluble
GRGDSP peptide, but not by the variant GRGESP peptide. Furthermore, a
dodecapeptide corresponding to fibrinogen gamma 400-411 eluted only
GPIIb-IIIa but not P160 from the RGD affinity matrix. Characterization of
P160 by two-dimensional sodium dodecyl sulfate-polyacrylamide gel
electrophoresis and by the O'Farrell gel electrophoresis system indicated
that P160 is a component of platelet GPIc. GoH3, a monoclonal antibody
recognizing the alpha subunit of the very late antigen-6, failed to
immunoprecipitate P160 from the RGD eluate, indicating that it did not
contain the very late antigen-6 alpha subunit. In immunoblots, P160 reacted
specifically with a polyclonal anti-peptide antibody recognizing the alpha
subunit of the vitronectin receptor (VnR), but not with the monoclonal
anti-GPIIb antibody PMI-1, suggesting that P160 is the alpha subunit of
platelet VnR. This possibility was further substantiated by the complete
identity between the determined amino-terminal sequence of P160 and the
known sequence of the VnR alpha subunit. Moreover, direct association of
P160 with a beta subunit having an apparent molecular weight similar to
that of GPIIIa was demonstrated by immunoprecipitation with LM609, an
anti-VnR complex monoclonal antibody. These results indicate that the VnR
complex is present on platelets and may play a functional role in platelet
adhesive reactions.
Isolation and characterization of a platelet membrane protein related to the vitronectin receptor
Department of Immunology, Research Institute of Scripps Clinic, La Jolla, California 92037.
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