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MJ Metzelaar, HF Heijnen, JJ Sixma and HK Nieuwenhuis
Department of Haematology, University Hospital Utrecht, The Netherlands.
To identify antigens on the platelet plasma membrane that are exposed after
activation, we developed a monoclonal antibody (MoAb) designated RUU-SP
1.77. The RUU-SP 1.77 antigen is present on the membrane of resting
platelets at a basal level and is strongly expressed on the plasma membrane
after thrombin activation. Freshly fixed platelets bound 4,150 +/- 1,935
(mean +/- SD) RUU-SP 1.77 molecules per platelet; on fixed
thrombin-stimulated platelets the number of binding sites was upregulated
to 19,050 +/- 5,120 (kd 4.5 +/- 0.8 nmol/L). MoAb RUU-SP 1.77 recognized a
major protein of 33 Kd and a minor 28-Kd protein, both under nonreduced and
reduced conditions. Immunoelectron microscopic studies showed the presence
of the protein associated with the membrane of alpha-granules. Due to the
localization associated with the alpha-granule membrane, we have designated
it GMP-33 (granule membrane protein with a molecular weight of 33 Kd).
Based on structural properties, we conclude that GMP-33 is a protein
associated with the alpha-granule membrane that has not been described
before.
This article has been cited by other articles:
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| Copyright © 1992 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||