The retarded electrophoretic migration of p56lck induced by vanadate in lymphoma cells correlates with modified kinase activity.
p56lck is a src related lymphocyte specific tyrosine protein kinase which undergoes specific changes during T-cell activation, particularly the appearance of slow migrating forms. To analyze these forms, LSTRA cells were treated with vanadate. This resulted in increased phosphorylation of p56lck with the appearance of slow migrating forms. Renaturation of the p56lck bands after gel migration showed that vanadate mostly increased the activity of the lower band of p56lck. The upper bands had a reduced specific activity. In addition, the upper bands from vanadate treated cells displayed additional phosphorylated sites.
Danielian
S
S
INSERM U 332, Paris, France.
Fagard
R
R
Boulet
I
I
Fischer
S
S
D000818:Animals; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D019860:Lymphocyte Specific Protein Tyrosine Kinase p56(lck); D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000502:physiology*; D012697:Serine Endopeptidases; D013601:T-Lymphocytes / Q000201:enzymology*; D014407:Tumor Cells, Cultured; D014638:Vanadates / Q000494:pharmacology*
D014638:Vanadates; D011505:Protein-Tyrosine Kinases; D019860:Lymphocyte Specific Protein Tyrosine Kinase p56(lck); D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase