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J. Biol. Chem., Vol. 263, Issue 10, 4882-4890, 04, 1988
JE Fox, LP Aggerbeck and MC Berndt
The glycoprotein Ib.IX complex is a major component of the platelet
membrane. It mediates the adhesion of platelets to exposed subendothelium
and provides an attachment site for the membrane skeleton on the plasma
membrane. The present study was designed to characterize the structure of
the glycoprotein Ib.IX complex. Electron microscopy of purified
glycoprotein Ib.IX complex in detergent showed that each complex existed as
a flexible rod with a globular domain on either end. The overall length of
the complex was approximately 59.5 nm. The smaller globular domain had a
diameter of approximately 8.9 nm; the larger, a diameter of approximately
15.9 nm. In the absence of detergent, the glycoprotein Ib.IX complexes
tended to self-associate through the larger globular domain, suggesting
that this domain contained the hydrophobic region that inserts into the
membrane. Proteases known to cleave glycoprotein Ib alpha close to its
membrane- insertion site released the larger globular domain. Sodium
dodecyl sulfate-polyacrylamide gel electrophoresis showed that this domain
was composed of glycoprotein Ib beta, glycoprotein IX, and a Mr = 25,000
fragment of glycoprotein Ib alpha. Proteolysis at the external end of
glycoprotein Ib alpha reduced the size of the smaller globular domain. This
study shows that the glycoprotein Ib.IX complex has an elongated shape,
with a globular domain on the end that inserts into the membrane and a
smaller globular domain on the end of glycoprotein Ib alpha that is
oriented external to the plasma membrane.
Structure of the glycoprotein Ib.IX complex from platelet membranes
Gladstone Foundation Laboratories for Cardiovascular Disease, University of California, San Francisco 94140-0608.
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