Mutations in band 3 and cation leaky red cells.
We have recently shown that amino acid substitutions in the membrane domain of band 3 (anion exchanger 1, SLC4A1) are associated with hereditary stomatocytosis (HSt), a red cell condition in which the cells leak sodium and potassium ions. These substitutions appear to convert band 3 from an anion exchanger into a cation channel. In this review, I will first give some background on the structure and function of normal band 3 and describe our findings in red cells from HSt patients. Then I will compare the properties of the HSt band 3 to those of Southeast Asian Ovalocytosis (SAO) band 3 and discuss the implications for the structure of band 3, the quality control of protein expression in red cells and the cation permeability of normal human red cells.
Bruce
Lesley
L
Bristol Institute for Transfusion Sciences, National Blood Service, Southmead, Bristol BS10 5ND, UK. lesley.bruce@nbs.nhs.uk
D001457:Anion Exchange Protein 1, Erythrocyte / Q000235:genetics* / Q000378:metabolism*; D004612:Elliptocytosis, Hereditary / Q000235:genetics* / Q000378:metabolism* / Q000473:pathology; D004910:Erythrocyte Membrane / Q000235:genetics / Q000378:metabolism; D004913:Erythrocytes, Abnormal / Q000378:metabolism*; D006801:Humans; D017354:Point Mutation; D011188:Potassium / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000235:genetics; D012964:Sodium / Q000378:metabolism; D013329:Structure-Activity Relationship
D001457:Anion Exchange Protein 1, Erythrocyte; C454201:SLC4A1 protein, human; D012964:Sodium; D011188:Potassium