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  • Title: Gerbich blood groups and minor glycophorins of human erythrocytes.
    Author: Colin Y.
    Journal: Transfus Clin Biol; 1995; 2(4):259-68. PubMed ID: 8542024.
    Abstract:
    Four main glycophorins which can be specifically detected by periodic-acid-Schiff (PAS) staining after separation of red cell membranes by SDS-polyacrylamide gel electrophoresis have been identified and are known under different nomenclatures. Here, the designation of glycophorins A, B and C and glycophorin D will be used. A new member designated glycophorin E (GPE) has been recently identified in the course of molecular genetic studies. These glycophorins represent about 2% of the total erythrocyte membrane protein mass and have been fully characterized both at the protein and at the DNA level. Accordingly, these molecules can be subdivided into two groups that are distinguished by distinct properties such as blood group antigenic properties, apparent M(r), copy number, attached glycans, detergent solubility, and gene structure. GPC and GPD are minor sialoglycoproteins contributing to 4 and 1% to the PAS-positive material and are present at about 2.0 and 0.5 x 10(5) copies/cell, respectively. Both carry blood group Gerbich (Ge) antigens. Protein and nucleic acid analysis indicated that GPD is a truncated form of GPC in its N-terminal region and that both proteins are produced by a unique gene which is present as a single copy on chromosome 2q14-q21. GPC and GPD are produced from the same gene through use of alternative translation initiation sites. These proteins and the GYPC gene share no homology with the GPA, GPB and GPE proteins and the GYPA gene cluster, respectively. Thus, the glycophorin name, which suggests that all these sialoglycopropteins have a common genetic origin, might be now considered as a misnomer. As a further difference between the two groups of membrane proteins, GPC and GPD are expressed both in erythroid and non erythroid tissues, but the level of transcription is much higher in erythroid than in non erythroid tissues and in addition the proteins are differently glycosylated in the two cell types. Increasing evidence suggests a significant role for GPC and GPD in the regulation of the red cell shape and the membrane mechanical properties by providing a membrane linkage site for cytoskeletal proteins, especially proteins 4.1 and p55. The total lack of GPC and GPD in the red cell membrane is associated with hereditary ellyptocytosis in the Leach phenotype and the molecular basis of these defects have been elucidated.(ABSTRACT TRUNCATED AT 400 WORDS)
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