Coordinate Glycosylation and Cell Surface Expression of Glycophorin A During Normal Human Erythropoiesis

• Published in: Blood Vol. 70; no. 6; pp. 1959 - 1961
• Main Authors: Loken, Michael R., Civin, Curt I., Bigbee, William L., Langlois, Richard G., Jensen, Ronald H.
• Format: Journal Article
• Language: English
• Published: Washington, DC Elsevier Inc 01.12.1987; The Americain Society of Hematology
• Subjects: Antibodies, Monoclonal; Biological and medical sciences; Cell differentiation, maturation, development, hematopoiesis; Cell physiology; Epitopes; Erythrocyte Membrane - immunology; Erythrocyte Membrane - metabolism; Erythropoiesis; Flow Cytometry; Fundamental and applied biological sciences. Psychology; Glycophorins - immunology; Glycophorins - metabolism; Glycosylation; Humans; MNSs Blood-Group System - immunology; Molecular and cellular biology; Sialoglycoproteins - metabolism; Erythropoiesis; Human; Flow cytometry; Regulation(control); Erythroid cell; Antigenic determinant; Bone marrow; Glycosylation; Monoclonal antibody; Cell differentiation; Gene expression; Cell surface
• ISSN: 0006-4971; 1528-0020
• DOI: 10.1182/blood.V70.6.1959.1959

The expression of two epitopes on glycophorin A (GPA) during erythroid development was examined on normal human bone marrow using quantitative flow cytometry. The highly correlated binding of two monoclonal antibodies, one sensitive and the other insensitive to glycosylation, indicated that the two epitopes were coordinately expressed during erythroid development. Both antigens reached a maximum expression during the early normoblast stage and were maintained at a constant amount per cell throughout further maturation to erythrocytes. These data suggest that glycosylation of GPA, as detected by antibodies recognizing blood group (M) and (N) antigens, does not increase during erythroid maturation.