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PADGEM (GMP140) is a component of Weibel-Palade bodies of human endothelial
cells
R Bonfanti, BC Furie, B Furie and DD Wagner
Center for Hemostasis and Thrombosis Research, New England Medical Center,
Boston, MA 02111.
PADGEM protein (PADGEM), also known as GMP140, is a platelet alpha- granule
membrane protein that is translocated to the external membrane after
platelet activation. Although the biosynthesis of this protein was
originally thought to be confined to megakaryocytes, the synthesis of
PADGEM in endothelial cells was recently demonstrated (McEver et al: Blood
70:1974a, 1987). We now describe the subcellular localization of this
protein in endothelial cells. Immunofluorescence staining of permeabilized
human umbilical vein endothelial cells with KC4, a well characterized
monoclonal antibody to PADGEM, showed positively stained elongated
structures similar in distribution and shape to Weibel-Palade bodies. Their
identity as Weibel-Palade bodies was confirmed by double label
immunofluorescence using KC4 and a polyclonal antiserum to von Willebrand
factor (vWf), a protein known to be specifically stored in these
organelles. All Weibel-Palade bodies were found to contain PADGEM. In
contrast to strong perinuclear staining produced with anti- vWf antibodies,
no significant perinuclear staining was obtained with KC4, indicating that
relatively little PADGEM is present in the endoplasmic reticulum and in the
Golgi apparatus. In endothelial cells treated with secretagogues that
stimulate vWf release the elongated structures positive for PADGEM
disappeared, further identifying these structures as Weibel-Palade bodies.
This observation extends the parallels between Weibel-Palade bodies and
alpha-granules and suggests a possible functional association between vWf
and PADGEM.
Volume 73,
Issue 5,
pp. 1109-1112,
04/01/1989
Copyright © 1989 by The American Society of Hematology
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