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PMID: 6948372 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Phosphate metabolite regulation of spectrin interactions.

Scandinavian journal of clinical and laboratory investigation. Supplementum ·Vol. 156 ·1981-00-00 ·Pages 117-22

Sheetz MP, Casaly J

Abstract

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 dephosphorylation. 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.

MeSH Terms
2,3-Diphosphoglycerate Adenosine Triphosphate/pharmacology Animals Cytidine Triphosphate/pharmacology Diphosphoglyceric Acids/pharmacology Erythrocyte Membrane/metabolism Fructosediphosphates/pharmacology Guanosine Triphosphate/pharmacology Humans Hydrogen-Ion Concentration Membrane Proteins/metabolism Molecular Conformation Phosphates/metabolism,pharmacology Rabbits Spectrin/metabolism Temperature
Chemicals
Diphosphoglyceric Acids Fructosediphosphates Membrane Proteins Phosphates Spectrin 2,3-Diphosphoglycerate Cytidine Triphosphate Guanosine Triphosphate Adenosine Triphosphate
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Sheetz M P
Casaly J
Article Info
Journal
Scandinavian journal of clinical and laboratory investigation. Supplementum
Abbr.
Scand J Clin Lab Invest Suppl
ISSN
0085-591X
Published
1981-00-00
Pages
117-22
Language
English
Region
Norway
NLM ID
2984789R
Subset
IM
Grants
NHLBI NIH HHS · HL-23359 · United States
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