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PubMed · 6551238

Erythrocyte membrane structure and function.

M J Tanner
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Abstract

The structure and function of the proteins of the human erythrocyte membrane are discussed. The major integral proteins comprise the anion transport protein (band 3), the glucose transporter and four sialic acid-rich polypeptides. The anion transport protein equilibrates Cl- and HCO-3 between the plasma and red cell and also provides an anchorage site for peripheral proteins including those in the red cell cytoskeleton. The sialic acid-rich proteins are predominantly exposed at the surface of the cell. The bulk of the peripheral proteins are organized in a complex fashion to form a skeletal meshwork at the cytoplasmic surface of the membrane which maintains the shape and deformability of the red cell. The changes in membrane components during differentiation of the red cell are discussed.

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Anion Exchange Protein 1, ErythrocyteBlood GlucoseBlood ProteinsCarbohydrate ConformationCarbohydrate SequenceCarrier ProteinsCell DifferentiationErythrocyte MembraneErythrocytesGlycoproteinsHumansMembrane ProteinsMonosaccharide Transport ProteinsOligosaccharidesSialoglycoproteinsJournal Article

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M J Tanner. 1983. Erythrocyte membrane structure and function.. https://doi.org/10.1002/9780470715444.ch2

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Anion Exchange Protein 1, Erythrocyte↗
PubMed1992

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PubMed1992

Band 3 Memphis: a widespread polymorphism with abnormal electrophoretic mobility of erythrocyte band 3 protein caused by substitution AAG----GAG (Lys----Glu) in codon 56.

Band 3 Memphis (b3M) is a variant of the erythrocyte band 3 protein detected in individuals of virtually all ethnic groups and characterized by a reduced mobility of proteolytic fragments derived from the N-terminus of the cytoplasmic domain of band 3 (cdb3). We have sequenced band 3 cDNA corresponding to cdb3 in 12 heterozygotes for the b3M polymorphism including one white, one black, one Chinese, one Philippino, one Malay, and seven Melanesian subjects. In all individuals, we found a single-base substitution in codon 56 of one band 3 allele changing lysine to glutamic acid (AAG----GAG) which, in some of them, was linked with an additional mutation in cdb3. Since the change of codon 56 from AAG to GAG was the only mutation in the studied individuals found within the cDNA segment coding for the abnormally migrating fragment of cdb3, we conclude that it represents the underlying molecular basis of the b3M polymorphism. We further support this conclusion by showing that electrophoresis in the presence of 4 mol/L urea abolished the difference in migration between proteolytic products of b3M and normal band 3, and that a fusion protein prepared from cDNA coding for the b3M allele again exhibits reduced electrophoretic mobility compared with the normal fusion protein. Finally, since most of the previously cloned mouse, rat, and chicken band 3 and band 3-related proteins contain glutamic acid in the position corresponding to amino acid 56 in the human band 3, we propose that the Memphis variant is the evolutionarily older form of band 3.

Anion Exchange Protein 1, Erythrocyte↗