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Expression of platelet glycoprotein Ib by cultured human megakaryocytes:
ultrastructural localization and biosynthesis
N Debili, N Kieffer, M Nakazawa, J Guichard, M Titeux, E Cramer, J Breton- Gorius and W Vainchenker
INSERM U91, Hopital Henri Mondor, Creteil, France.
Glycoprotein Ib (GPIb), the receptor for von Willebrand factor, is a
two-chain member constituent of the platelet/megakaryocytic lineage.
Studies on its expression have been hampered by the difficulties in
obtaining purified megakaryocytes in a sufficient number. We report a
suspension liquid culture procedure that allowed isolation of more than 1 x
10(6) megakaryocytes with a purity ranging from 3% to 88% from the blood of
patients with chronic myeloid leukemia, from fetal liver or from normal
human bone marrow. GPIb was detected on the plasma membrane of all maturing
megakaryocytes and also of promegakaryoblasts devoid of demarcation
membranes. GPIb was detected on demarcation membranes of maturing
megakaryocytes but was absent from all other organelles, including alpha
granules. Biosynthesis of 35S-methionine labeled megakaryocytes showed that
GPIb with similar electrophoretic mobility to the platelet molecule was
synthesized and that it was also composed of two chains, since its
molecular weight shifted in reducing conditions from 170 Kd to 145 Kd. The
beta chain remained undetectable after methionine metabolic labeling, but
it was immunoprecipitated after 3H-leucine metabolic labeling, confirming
that this subunit is devoid of methionine. GPIb was associated with GPIX,
as it is in platelets, since anti-GPIb antibodies coprecipitated a 17 Kd
polypeptide.
Volume 76,
Issue 2,
pp. 368-376,
07/15/1990
Copyright © 1990 by The American Society of Hematology
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