Divergent effects of hyperosmolality on stress-response (heat shock) protein expression in cultured human tumor cells: an immunocytochemical study.
Exposing cells to adverse conditions usually elicits expression of stress-response (heat shock) proteins (srp). Here we show that hyperosmolar growth conditions do not uniformly affect srp expression in MCF-7 and HeLa S3 cells, derived from carcinoma of the breast and cervix, respectively. Thus, whereas srp 27 expression was increased in MCF-7, but not in HeLa S3, the opposite was the case with srp 72. On the other hand, hyperosmolality did not induce alpha B-crystallin or ubiquitin in either cell line. These findings show that srp expression by the human tumor cells studied is non-coordinate, suggesting that each srp is independently modulated.
Kato
M
M
Department of Pathology, Montefiore Medical Center, Albert Einstein College of Medicine, Bronx, New York 10467.
Herz
F
F
Brijlall
D
D
Kato
S
S
D001943:Breast Neoplasms; D002460:Cell Line; D003459:Crystallins / Q000032:analysis / Q000096:biosynthesis; D005260:Female; D006367:HeLa Cells; D006360:Heat-Shock Proteins / Q000032:analysis / Q000096:biosynthesis*; D006801:Humans; D006982:Hypertonic Solutions; D015151:Immunoblotting; D007150:Immunohistochemistry / Q000379:methods; D013012:Sorbitol; D013395:Sucrose; D014407:Tumor Cells, Cultured; D014452:Ubiquitins / Q000032:analysis / Q000096:biosynthesis; D002583:Uterine Cervical Neoplasms
D003459:Crystallins; D006360:Heat-Shock Proteins; D006982:Hypertonic Solutions; D014452:Ubiquitins; D013012:Sorbitol; D013395:Sucrose