Enhanced tyrosine phosphorylation in B lymphocytes upon complexing of membrane immunoglobulin.
Activation of normal human peripheral blood B-enriched lymphocytes with antiserum reacting with membrane immunoglobulin was associated with increased phosphorylation of cellular proteins, particularly in the Triton-insoluble cytoskeletal fraction. At least two proteins (56K and 60K) were labeled predominantly at tyrosine residues. These findings may indicate another specialized membrane structure which upon specific ligand binding stimulates tyrosine phosphorylation in association with cellular proliferation.
D001402:B-Lymphocytes / Q000201:enzymology* / Q000276:immunology; D001798:Blood Proteins / Q000378:metabolism*; D002455:Cell Division; D003599:Cytoskeleton / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007106:Immune Sera; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D008970:Molecular Weight; D010766:Phosphorylation; D011494:Protein Kinases / Q000097:blood*; D011505:Protein-Tyrosine Kinases; D011971:Receptors, Immunologic / Q000276:immunology*
D001798:Blood Proteins; D007106:Immune Sera; D011971:Receptors, Immunologic; D008345:Manganese; D011494:Protein Kinases; D011505:Protein-Tyrosine Kinases; D008274:Magnesium