TY - JOUR
T1 - Phosphate metabolite regulation of spectrin interactions
AU - Sheetz, Michael P.
AU - Casaly, Joseph
N1 - Funding Information:
We would like to thank P. Cosgrove and D. Koppel for their helpful comments on the manuscript. This research was supported in part by a grant from NIH (HL-23359).
PY - 1981
Y1 - 1981
N2 - The deformability of the erythrocyte membrane is believed to depend upon component interactions in the spectrin, actin and band 4.1 complex. Phosphate metabolites, such as 2,3-diphosphoglycerate (2,3 DPG) will dissociate spectrin from actin and band 4.1. This dissociation by 2,3 DPG is highly pH dependent but does not involve divalent cations, 2,3 DPG hydrolysis or spectrin dephos-phorylation. In intact erythrocytes the concentrations of 2,3 DPG and the lipid, triphosphatidyl inositol, are sufficient to cause increased labilization in the spectrin, actin and band 4.1 network.
AB - The deformability of the erythrocyte membrane is believed to depend upon component interactions in the spectrin, actin and band 4.1 complex. Phosphate metabolites, such as 2,3-diphosphoglycerate (2,3 DPG) will dissociate spectrin from actin and band 4.1. This dissociation by 2,3 DPG is highly pH dependent but does not involve divalent cations, 2,3 DPG hydrolysis or spectrin dephos-phorylation. In intact erythrocytes the concentrations of 2,3 DPG and the lipid, triphosphatidyl inositol, are sufficient to cause increased labilization in the spectrin, actin and band 4.1 network.
KW - Erythrocyte membrane
KW - Phosphorylation
KW - Spectrin
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U2 - 10.3109/00365518109097443
DO - 10.3109/00365518109097443
M3 - Article
C2 - 6948372
AN - SCOPUS:0019738508
SN - 0036-5513
VL - 41
SP - 117
EP - 122
JO - Scandinavian Journal of Clinical and Laboratory Investigation
JF - Scandinavian Journal of Clinical and Laboratory Investigation
IS - S156
ER -