Phosphorylation of human erythrocyte band 3 by endogenous p72syk

J Biol Chem. 1994 Jan 14;269(2):955-9.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Anion Exchange Protein 1, Erythrocyte / metabolism*
  • Enzyme Precursors / blood*
  • Erythrocyte Membrane / metabolism*
  • Erythrocytes / enzymology
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Peptide Mapping
  • Phosphotyrosine
  • Protein-Tyrosine Kinases / blood*
  • Syk Kinase
  • Tyrosine / analogs & derivatives
  • Tyrosine / metabolism
  • src-Family Kinases*

Substances

  • Anion Exchange Protein 1, Erythrocyte
  • Enzyme Precursors
  • Intracellular Signaling Peptides and Proteins
  • Phosphotyrosine
  • Tyrosine
  • Protein-Tyrosine Kinases
  • SYK protein, human
  • Syk Kinase
  • lyn protein-tyrosine kinase
  • src-Family Kinases