Hexose-specific inhibition in vitro of human red cell Ca2+-ATPase activity

Mark R. Deziel, Richard S. Safeer, Susan D. Blas, Faith B. Davis, Paul J. Davis

Research output: Contribution to journalArticlepeer-review

Abstract

In a concentration-dependent manner (5.5-27.5 mmol/l), d-glucose incubated in vitro with human erythrocyte membranes at 37°C for 1 h inhibited membrane Ca2+-ATPase activity by up to 75%. The IC50 was 11 mmol/l, l-Glucose was ineffective, as were 3-O-methylglucose, 2-deoxyglucose, sorbitol and myo-inositol. In contrast, d-fructose decreased Ca2+-ATPase activity nearly as effectively as d-glucose and mannose and galactose at 11 mmol/l were less than 50% as effective as d-glucose. Tunicamycin (12 pmol/l), but not 10 mmol/l aminoguanidine, progressively antagonized in vitro the d-glucose effect on the enzyme. Erythrocyte membrane Ca2+-ATPase activity may be regulated by glycosylation, rather than nonenzymatic glycation.

Original languageEnglish (US)
Pages (from-to)119-122
Number of pages4
JournalBBA - Biomembranes
Volume1110
Issue number1
DOIs
StatePublished - Sep 21 1992
Externally publishedYes

Keywords

  • (Human)
  • ATPase
  • Ca-
  • Red blood cell
  • d-Glucose

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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