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CD63 is a component of Weibel-Palade bodies of human endothelial cells
UM Vischer and DD Wagner
Division of Hematology-Oncology, New England Medical Center, Boston, MA
02111.
Weibel-Palade bodies are secretory granules of vascular endothelial cells
specialized in the storage of von Willebrand factor (vWF) and P- selectin,
two adhesion proteins that can be rapidly mobilized to the cell surface by
exocytosis in response to thrombin or other agonists. In this study, we
attempted to identify additional components of Weibel- Palade bodies by
raising monoclonal antibodies to these granules, purified by cell
fractionation. One antibody, 2C6, was found to be specific for CD63, a
membrane glycoprotein previously described in the lysosomes of platelets
and other cell types. The immunopurified 2C6 antigen was recognized by an
anti-CD63 reference antibody, 2.28, by Western blotting. Also, the
biosynthetic profile of the 2C6 antigen in endothelial cells showed a
nascent molecular mass and a glycosylation pattern identical to that of
CD63. Immunofluorescence staining with 2C6 showed the lysosomes, and also
elongated structures identified as Weibel-Palade bodies by their shape,
distribution, and positive staining with anti-vWF antibodies, CD63 was also
found by Western blotting of subcellular fractions highly enriched in
Weibel-Palade bodies. Our results indicate that CD63 colocalizes with vWF
and P- selectin in the Weibel-Palade bodies of endothelial cells, and
together with these adhesion proteins it could be rapidly expressed on the
cell surface in areas of vascular injury and inflammation.
Volume 82,
Issue 4,
pp. 1184-1191,
08/15/1993
Copyright © 1993 by The American Society of Hematology
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