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Human platelet-derived mitogens. II. Subcellular localization of
insulinlike growth factor I to the alpha-granule and release in response to
thrombin
KP Karey and DA Sirbasku
Department of Biochemistry and Molecular Biology, University of Texas
Medical School, Houston 77225.
Platelets contain mitogenic activities for MCF-7 human breast cancer cells
when assayed under serum-free chemically defined conditions. Purification
from outdated human platelets identified insulinlike growth factor I
(IGF-I) as the most potent breast cancer cell mitogen in lysates (Karey KP,
Sirbasku DA: see accompanying article, this issue). In this study the
release and subcellular localization of IGF-I was investigated.
Degranulation of platelets by thrombin treatment caused release of
lysosomal enzymes (beta-glucuronidase and N-acetyl-D- glucosaminidase),
alpha-granule proteins (beta-thromboglobulin and fibrinogen) as well as
mitogenic activity for MCF-7 cells and IGF-I as measured by
radioimmunoassay (RIA) and radioreceptor assay. Release of mitogenic
activity and immunologically identified IGF-I was induced tenfold over
controls by thrombin and was nearly complete as compared to platelets
disrupted by repeated freezing and thawing. Disruption of platelets by
nitrogen cavitation followed by separation of the organelles by sucrose
density gradient sedimentation showed that IGF-I and mitogenic activity
localized predominantly to fractions containing alpha-granules rather than
soluble cellular components, lysosomes, or dense granules. The morphology
of MCF-7 cells in serum-free medium supplemented with supernatants from
thrombin-treated platelets also indicated the release of important
cell-adhesion factors for human breast cancer cells.
Volume 74,
Issue 3,
pp. 1093-1100,
08/15/1989
Copyright © 1989 by The American Society of Hematology
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