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Thromb Haemost 2001; 86(03): 887-893
DOI: 10.1055/s-0037-1616152
Review Articles
Schattauer GmbH

The 33-kDa Platelet α-granule Membrane Protein (GMP-33) Is an N-terminal Proteolytic Fragment of Thrombospondin

Conchi Damas
1   Department of Haematology and Graduate School for Biomembranes, University of Utrecht, The Netherlands
,
Tom Vink
1   Department of Haematology and Graduate School for Biomembranes, University of Utrecht, The Netherlands
,
Karel H. Nieuwenhuis
1   Department of Haematology and Graduate School for Biomembranes, University of Utrecht, The Netherlands
,
Jan J. Sixma
1   Department of Haematology and Graduate School for Biomembranes, University of Utrecht, The Netherlands
› InstitutsangabenThis work was financially supported by the Dutch Heart Foundation (NHS) (grant no. 43.051).
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Publikationsverlauf

Received 12. Dezember 2000

Accepted after revision 07. Mai 2001

Publikationsdatum:
14. Dezember 2017 (online)

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Summary

GMP-33 is a platelet membrane associated protein that is recognised by RUU-SP 1.77, an antibody raised against activated platelets. GMP-33 is predominantly associated with the membrane of platelet α-granules and it is translocated to the plasma membrane upon platelet activation (Metzelaar et al. Blood 1992; 79: 372-9). In this study we have isolated the protein by immunoaffinity chromatography. The N-terminus was sequenced and was identical to the N-terminal sequence of human thrombospondin. The protein was N-glycosylated and bound to heparin as would be expected of the N-terminal part of thrombospondin. RUU-SP 1.77 reacted only with reduced thrombospondin. Plasmin and trypsin digestion of thrombospondin yielded fragments of approximately the same size as GMP 33 that reacted with RUU-SP 1.77 after reduction. No evidence for alternative splicing was found. We postulate that GMP 33 is an N-terminal proteolytic fragment of thrombospondin that is membrane associated.

Keywords

Thrombospondin - platelet α-granule - platelet activation - platelet membrane
 

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