Evidence for release of soluble, but not of membrane-integrated, proteins from human platelet alpha-granules.

Proteins released from stimulated platelets were compared to those of a well-defined preparation of alpha-granules and the soluble cytoplasm by crossed immunoelectrophoresis. Nearly all releasable proteins were detected in the alpha-granule, whereas the true proteins of the soluble cytoplasm were not released. The released glycoproteins interacted with lectins similarly to their alpha-granula-located counterparts. The alpha-granules were divided into soluble contents and membranes by ultrasonication followed by ultracentrifugation. The proteins of the soluble content corresponded to those released from the stimulated platelets. This observation was also supported by SDS-polyacrylamide gel electrophoresis. The results indicate that the bulk of the proteins released from stimulated platelets originate from the soluble content of the alpha-granules. Two major alpha-granule antigens as well as the myosin heavy chain were not released and recovered in the alpha-granule membrane. These results support the hypothetical exocytosis mechanism for the release of alpha-granule proteins from platelets.