Heat shock induces protein tyrosine phosphorylation in cultured cells.
We examined the effect of heat shock on protein tyrosine phosphorylation in cultured animal cells using antiphosphotyrosine antibodies in immunoblotting and immunofluorescence microscopy experiments. Heat shock significantly elevated the level of phosphotyrosine in proteins in most of the cultured cells examined, including fibroblasts, epithelial cells, nerve cells, and muscle cells, but not in Rous sarcoma virus-transformed fibroblasts. The increase in protein tyrosine phosphorylation induced by heat shock occurred in proteins with a wide range of molecular masses and was dependent on the temperature and duration of the heat shock.
Maher
P A
PA
Biology Department, University of California, San Diego, La Jolla 92093.
Pasquale
E B
EB
D000818:Animals; D002460:Cell Line; D002645:Chickens; D003513:Cycloheximide / Q000494:pharmacology; D005455:Fluorescent Antibody Technique; D006358:Hot Temperature; D015151:Immunoblotting; D008322:Mammals; D008970:Molecular Weight; D010750:Phosphoproteins / Q000378:metabolism*; D019000:Phosphotyrosine; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000378:metabolism; D014639:Vanadium / Q000494:pharmacology
D010750:Phosphoproteins; D014639:Vanadium; D019000:Phosphotyrosine; D014443:Tyrosine; D003513:Cycloheximide; D011505:Protein-Tyrosine Kinases