Phosphate metabolite regulation of spectrin interactions

Michael Sheetz, Joseph Casaly

Research output: Contribution to journalArticle

9 Citations (Scopus)

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 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.

Original languageEnglish (US)
Pages (from-to)117-122
Number of pages6
JournalScandinavian Journal of Clinical and Laboratory Investigation
Volume41
Issue numberS156
DOIs
StatePublished - Jan 1 1981
Externally publishedYes

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2,3-Diphosphoglycerate
Spectrin
Metabolites
Phosphates
Actins
Divalent Cations
Erythrocyte Membrane
Inositol
Formability
Hydrolysis
Erythrocytes
Membranes
Lipids

Keywords

  • Erythrocyte membrane
  • Phosphorylation
  • Spectrin

ASJC Scopus subject areas

  • Clinical Biochemistry

Cite this

Phosphate metabolite regulation of spectrin interactions. / Sheetz, Michael; Casaly, Joseph.

In: Scandinavian Journal of Clinical and Laboratory Investigation, Vol. 41, No. S156, 01.01.1981, p. 117-122.

Research output: Contribution to journalArticle

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