Platelets deficient in glycoprotein IIIb aggregate normally to collagens type I and III but not to collagen type V

Autor:	B Schwippert, U. Niehues, D Niesing-Bresch, J Kardoeus, J van de Loo, J. Rauterberg, Beate E. Kehrel, KJ Clemetson, A Kronenberg, D Tschope
Rok vydání:	1993
Předmět:	chemistry.chemical_classification biology CD36 Immunology Cell Biology Hematology Platelet membrane glycoprotein Biochemistry Molecular biology Collagen receptor chemistry Hemostasis biology.protein Secretion Platelet Glycoprotein Platelet factor 4
Zdroj:	Blood. 82:3364-3370
ISSN:	1528-0020 0006-4971
DOI:	10.1182/blood.v82.11.3364.3364
Popis:	The aggregation of platelets induced by collagens is considered an important step in primary hemostasis. Glycoprotein (GP) IIIb (GPIIIb, GPIV, CD36) has been proposed as a blood platelet receptor for collagen. Platelets from three healthy blood donors were shown to be clearly deficient in GPIIIb. These platelets aggregated normally in response to type I and III collagens. In addition, platelet factor 4, beta-thromboglobulin, and adenosine triphosphate (ATP) secretion in response to type I and III collagens was normal. The findings indicate that GPIIIb is not the major, essential collagen receptor for type I and III collagens. This would explain why all individuals with GPIIIb- deficient platelets examined so far are healthy and, in particular, show no apparent evidence of hemostatic problems. However, in contrast to control platelets, no aggregation and impaired platelet factor 4, beta-thromboglobulin, and ATP secretion was observed in response to type V collagen. Therefore, it is postulated that for type V collagen- induced aggregation both GPIa/IIa and GPIIIb are essential.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c02fcbb11aaf6e5350f2360b1f65e96 https://doi.org/10.1182/blood.v82.11.3364.3364 Zobrazit plný text záznamu