TY - JOUR
T1 - Phosphorylation of human erythrocyte band 3 by endogenous p72syk
AU - Harrison, Marietta L.
AU - Isaacson, Christina C.
AU - Burg, Debra L.
AU - Geahlen, Robert L.
AU - Low, Philip S.
PY - 1994/1/14
Y1 - 1994/1/14
N2 - 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.
AB - 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.
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M3 - Article
C2 - 7507112
AN - SCOPUS:0028047337
SN - 0021-9258
VL - 269
SP - 955
EP - 959
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 2
ER -