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 journalArticle

124 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

Fingerprint Dive into the research topics of 'Phosphorylation of human erythrocyte band 3 by endogenous p72(syk)'. Together they form a unique fingerprint.

Cite this