Phosphorylation of human erythrocyte band 3 by endogenous p72(syk)

M. L. Harrison, C. C. Isaacson, D. L. Burg, R. L. Geahlen, P. S. Low

Research output: Contribution to journalArticlepeer-review

126 Scopus citations

Abstract

The anion transporter, band 3, is the major tyrosine kinase substrate in both red cell membranes and intact human erythrocytes. Using antibodies to various protein-tyrosine kinases, we found that p72syk and p56/53lyn are present in human red cells, while p56lck, pp60src, P59fyn and p55blk are absent. Treatment of intact red cells with a combination of vanadate and hydrogen peroxide dramatically increased the tyrosine phosphorylation of band 3. This treatment increased the tyrosine kinase activity of p72syk and decreased the activity of P56/53lyn in immune complex kinase assays. Band 3 was found to be associated in immune complexes with p72syk but not with p56/53lyn. These findings suggest that p72syk is responsible, at least in part, for the tyrosine phosphorylation of band 3 in human erythrocytes.

Original languageEnglish (US)
Pages (from-to)955-959
Number of pages5
JournalJournal of Biological Chemistry
Volume269
Issue number2
StatePublished - 1994

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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