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MNSs Blood Groups and Major Glycophorins

Molecular Basis for Allelic Variation
  • Cheng-Han Huang
  • Olga O. Blumenfeld
Part of the Blood Cell Biochemistry book series (BLBI, volume 6)

Abstract

Glycophorins A and B (GPA and GPB) of the erythrocyte membrane are unique compared with membrane glycoproteins of all other cells in that they carry the antigens of a blood group system, the MNSs blood group system, and therefore are readily identifiable in all human populations. The protein and carbohydrate structures of the glycophorins and their disposition in the membrane were among the first to be studied and be firmly established (Huang et al., 1991a). This was made possible because they are the major sialoglycoproteins of the mature erythrocyte, a relatively simple cell lacking all internal organelles; thus, the surface membrane is relatively easy to obtain and yields pure glycophorins using extraction protocols designed for carbohydrate-rich components. Over the years the interest in these molecules was both as the major antigens of the MNSs blood group system and as classical models of integral membrane glycoproteins. More recently, the structure and organization of genes encoding GPA, GPB, and the third member, GPE, were established, and some understanding obtained of factors involved in regulation of their expression in the erythroid cells (Cartron et al., 1990; Cartron and Rahuel, 1992). The nature of glycophorins as blood group antigens and the knowledge that serological variants of the common antigens occur among various populations (Race and Sanger, 1975) prompted investigations of the nature of polymorphism in this family of membrane glycoproteins. These studies revealed a common pattern of molecular mechanisms for protein diversification, and the glycophorin gene family can now serve as a prototype for human gene rearrangements.

Keywords

Splice Site Blood Group Gene Conversion Hybrid Gene Donor Splice Site 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Cheng-Han Huang
    • 1
  • Olga O. Blumenfeld
    • 2
  1. 1.Lindsley F. Kimball Research InstituteNew York Blood CenterNew YorkUSA
  2. 2.Department of BiochemistryAlbert Einstein College of MedicineBronxUSA

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