Control of band 3 lateral and rotational mobility by band 4.2 in intact erythrocytes: release of band 3 oligomers from low-affinity binding sites
نویسندگان
چکیده
منابع مشابه
Increased rotational mobility and extractability of band 3 from protein 4.2-deficient erythrocyte membranes: evidence of a role for protein 4.2 in strengthening the band 3-cytoskeleton linkage.
Band 3 (anion-exchange protein 1-[AE1]) is the major integral membrane protein of human erythrocytes and links the membrane to the underlying cytoskeleton via high-affinity binding to ankyrin. It is unclear whether other cytoskeletal proteins participate in strengthening the ankyrin-band 3 linkage, but a putative role for protein 4.2 (P4.2) has been proposed based on the increased osmotic fragi...
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In this paper, an ultra-low-noise amplifier with frequency band switching capability is designed, simulated and fabricated. The two frequency ranges of this amplifier consist of the 2.4 to 2.5 GHz and 3.1 GHz to 3.15 GHz frequency bands. The designed amplifier has a noise figure of less than 1dB, a minimum gain of 23 dB and a VSWR of less than 2 in the whole frequency band. The design process s...
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First, consider the basic band 3 molecule (B3M), it is the third band seen when erythrocyte membrane proteins are examined by gel electrophoresis and it is a transmebrane protein important in the erythrocyte’s structure that functions as a channel for exchanging bicarbonate ions for chloride ions [1]. The B3M’s are normally dispersed on the erythrocytes surface but in senescent erythrocytes som...
متن کاملAbsence of high-affinity band 4.1 binding sites from membranes of glycophorin C- and D-deficient (Leach phenotype) erythrocytes.
We investigated the role of glycophorins C and D in the association of band 4.1 with the erythrocyte membrane by measuring the binding of band 4.1 to erythrocyte inside-out vesicles stripped of endogenous band 4.1. Vesicles were prepared from either normal erythrocytes or erythrocytes completely lacking glycophorins C and D (Leach phenotype). Band 4.1 binding to vesicles from normal erythrocyte...
متن کاملCa2+ promotes erythrocyte band 3 tyrosine phosphorylation via dissociation of phosphotyrosine phosphatase from band 3.
The anion-exchange band 3 protein is the main erythrocyte protein that is phosphorylated by protein tyrosine kinase (PTK). We have previously identified a band 3-associated phosphotyrosine phosphatase (PTP) that is normally highly active and prevents the accumulation of band 3 phosphotyrosine. Band 3 tyrosine phosphorylation can be induced by inhibition of PTP (vanadate, thiol oxidation), activ...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 1996
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(96)79717-5