Human Platelet Antigen 3 (HPA-3): Localization of the Determinant of the Alloantibody Leka (HPA-3a) to the C-Terminus of Platelet Glycoprotein IIb Heavy Chain and Contribution of O-Linked Carbohydrates
| Autor: | Jean-Luc Wautier, Dominique Pidard, Isabelle Djaffar, Didier Vilette, Jean-Philippe Rosa |
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| Rok vydání: | 1993 |
| Předmět: |
endocrine system
Antigenicity Glycosylation Fibrinogen receptor Molecular Sequence Data Carbohydrates Platelet Membrane Glycoproteins Polymerase Chain Reaction Epitope Epitopes chemistry.chemical_compound Isoantibodies Humans Antigens Human Platelet Platelet RNA Messenger chemistry.chemical_classification Base Sequence biology C-terminus Antibodies Monoclonal Hematology Human platelet antigen Amino acid chemistry Biochemistry biology.protein Protein Processing Post-Translational |
| Zdroj: | Europe PubMed Central |
| ISSN: | 2567-689X 0340-6245 |
| DOI: | 10.1055/s-0038-1651638 |
| Popis: | SummaryThe human platelet antigen (HPA) 3 system is expressed on GPIIb, one subunit of GPIIb-IIIa, the platelet fibrinogen receptor. It was recently shown that HPA-3 was associated with an Ile843/Ser polymorphism. To investigate further HPA-3 determinant structure, we localized an HPA-3a determinant, recognized by the alloantiserum Leka, within the last 29 amino acids of GPIIbα. This region encompasses the polymorphic Ile843, which, as expected, is substituted into Ser in Leka-negative individuals, as shown by DNA sequence after polymerase chain reaction on platelet RNA. In addition, contribution of glycosylation to the determinant structure was demonstrated since the Leka antigenicity was strongly decreased after specifically removing nonterminal O-linked sugars, but not terminal sialic acids. We have thus refined the localization of an HPA-3a determinant within the last 29 amino acids, including Ile843, of GPIIb heavy chain, and shown that the Leka HPA-3a determinant is dependent, in part, upon the serine-linked carbohydrates adjacent to Ile/Ser843. |
| Databáze: | OpenAIRE |
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