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J. Biol. Chem., Vol. 263, Issue 23, 11025-11028, 08, 1988
JC Loftus, EF Plow, LK Jennings and MH Ginsberg
Platelet membrane glycoprotein (GP) IIb-IIIa is a component of a receptor
for the adhesive proteins fibrinogen, fibronectin, and von Willebrand
factor. GPIIb is initially synthesized as a single-chain polypeptide that
is proteolytically processed to yield the two chains of mature GPIIb
present on the cell surface. Analysis of the amino acid sequence
surrounding the proposed light-heavy chain junction of GPIIb suggests a
second potential site following a pair of basic residues 12- 15 residues
upstream from the reported amino terminus of the light chain. We have
utilized anti-peptide antibodies to examine the possibility of alternative
cleavage at these two potential sites. Peptide V43 precedes the dibasic
sequence and is known to reside in the heavy chain. Peptide V41 contains
the sequence between the two potential sites. In immunoblots, anti-V43
reacted only with the heavy chain while anti-V41 reacted only with the
light chain. Immunoprecipitation of surface-labeled platelets indicated 97%
of the GPIIb light chain contains the V41 sequence while approximately 3%
of GPIIb molecules lack the V41 sequence on both the light and heavy
chains. These data indicate that GPIIb is primarily cleaved 12-15 amino
acids upstream from the reported amino terminus of the light chain while in
a minor proportion of GPIIb molecules cleavage occurs at both sites.
Alternative proteolytic processing of platelet membrane glycoprotein IIb
Research Institute of Scripps Clinic, Department of Immunology, La Jolla, California 92037.
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