PMID: 9167305Mar 1, 1997Paper

Human erythrocyte antigen expression: its molecular bases

British Journal of Biomedical Science
N D Avent

Abstract

This review summarises the considerable body of information now available on the molecular bases of human blood group-antigen expression. The elucidation of this information has only been possible since the identification, purification, and subsequent cDNA cloning of the mRNAs which encode the blood group active proteins. The surface components which are responsible for antigen expression are divided into two types: carbohydrate and protein. All carbohydrate structures are attached covalently to either glycolipids or glycoproteins, and are synthesised in the Golgi apparatus of erythropoietic cells (or in other cell lines in secreted fluids). As a consequence, the molecular bases of carbohydrate antigens lie in polymorphic variation seen in the genes which synthesise these carbohydrate structures (i.e. glycosyltransferase enzymes). The structural differences in the ABO, Hh and Lewis transferase genes, which alter the substrate specificities of these glycosyltransferases and hence generate the different antigens, have been defined. The molecular bases underlying the P blood glycosyltransferases are unknown. Polymorphism in the remaining 19 blood group systems is defined by amino acid sequence changes in erythrocyte membrane prote...Continue Reading

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