GMP-140, A PLATELET ALPHA-GRANULE MEMBRANE-PROTEIN, IS ALSO SYNTHESIZED BY VASCULAR ENDOTHELIAL-CELLS AND IS LOCALIZED IN WEIBEL-PALADE BODIES
GMP-140, A PLATELET ALPHA-GRANULE MEMBRANE-PROTEIN, IS ALSO SYNTHESIZED BY VASCULAR ENDOTHELIAL-CELLS AND IS LOCALIZED IN WEIBEL-PALADE BODIES
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DOI:
10.1172/jci114175
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发表时间:
1989-07-01
影响因子:
15.9
通讯作者:
BAINTON, DF
中科院分区:
文献类型:
--
作者:
MCEVER, RP;BECKSTEAD, JH;BAINTON, DF
We used an immunoperoxidase procedure to examine the tissue distribution of the platelet .alpha.-granule membrane protein, GMP-140. In addition to its presence in megakaryocytes and platelets, GMP-140 antigen was found in vascular endothelial cells of diverse human organs, but it was not detected in other types of secretory cells. [35S]Cysteine-labeled human umbilical vein endothelial cells synthesized a GMP-140 molecule containing complex N-linked oligosaccharides similar to those previously demonstrated in platelets and the megakaryocytic HEL cell line. Using an immunogold procedure on frozen thin sections of endothelial cells, we found GMP-140 antigen to be localized to membranes of electron-dense storage granules. In double-label experiments there was colocalization of GMP-140 with vWf, indicating that these granules are Weibel-Palade bodies. When endothelial cells were stimulated with histamine, GMP-140 rapidly redistribution to the plasma membrane. Immunoassays of cell lysates indicated that, relative to total cell protein, less GMP-140 is present in human umbilical vein endothelial cells than in platelets. The restricted expression of GMP-140 in secretory granules of platelets and endothelium suggests that it has a specific function in the vascular system rather than a general role related to inducible secretion.