{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,11]],"date-time":"2026-02-11T17:25:51Z","timestamp":1770830751155,"version":"3.50.1"},"reference-count":0,"publisher":"American Physiological Society","issue":"1","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Cell Physiology"],"published-print":{"date-parts":[[1994,7,1]]},"abstract":"<jats:p> The family of 70-kDa heat-shock proteins (HSP-70) is evolutionarily highly conserved and has been shown to enhance cell survival from thermal injury. This study characterized HSP-72 induction in human epidermoid A-431 cells exposed to 45 degrees C for 10 min and determined the relationship between HSP-72, intracellular pH (pHi), adenosine 3',5'-cyclic monophosphate (cAMP), G proteins, and intracellular cytosolic free Ca2+ concentration ([Ca2+]i). Heat shock induced HSP-72 production, which was dependent on both temperature and the duration of heating. This HSP-72 induction was confirmed by Western blot analysis. HSP-72 levels in cells that had been heated then returned to 37 degrees C were elevated at 2 h (1.5 +\/- 0.1 x control), reached a maximum at 8 h (2.7 +\/- 0.1 x control), and remained above baseline for up to 4 days. Levels of HSP-72 mRNA, determined by dot-blot analysis, reached a maximum at 2 h and returned to baseline within 8 h. Both actinomycin D and cycloheximide blocked HSP-72 induction. Because heating causes intracellular acidification and increases in cAMP and [Ca2+]i, we studied the effect of pHi, cellular cAMP, and [Ca2+]i on HSP-72 induction. The reduction of pHi to 6.9 by acid loading did not affect the basal level of HSP-72 in unheated cells. Treatment with pertussis toxin, cholera toxin, or forskolin, but not 8-bromo-cAMP, 3-isobutyl-1-methylxanthine, or N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide potentiated heat-induced HSP-72 production. Inhibition of the heat-induced increase in [Ca2+]i attenuated, but failed to completely block, heat-induced HSP-72 production, mRNA synthesis, and the heat-shock transcriptional factor-heat-shock element binding complex formation, which suggests there are Ca(2+)-dependent and -independent processes involved in HSP-72 synthesis. Our results show that an increase in [Ca2+]i or activation of G proteins, but not pHi and cAMP, enhances HSP-72 induction. <\/jats:p>","DOI":"10.1152\/ajpcell.1994.267.1.c104","type":"journal-article","created":{"date-parts":[[2017,12,24]],"date-time":"2017-12-24T17:59:10Z","timestamp":1514138350000},"page":"C104-C114","source":"Crossref","is-referenced-by-count":57,"title":["HSP-72 synthesis is promoted by increase in [Ca2+]i or activation of G proteins but not pHi or cAMP"],"prefix":"10.1152","volume":"267","author":[{"given":"J. G.","family":"Kiang","sequence":"first","affiliation":[{"name":"Department of Clinical Physiology, Walter Reed Army Institute of Research, Washington, District of Columbia."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"F. E.","family":"Carr","sequence":"additional","affiliation":[{"name":"Department of Clinical Physiology, Walter Reed Army Institute of Research, Washington, District of Columbia."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M. R.","family":"Burns","sequence":"additional","affiliation":[{"name":"Department of Clinical Physiology, Walter Reed Army Institute of Research, Washington, District of Columbia."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"D. E.","family":"McClain","sequence":"additional","affiliation":[{"name":"Department of Clinical Physiology, Walter Reed Army Institute of Research, Washington, District of Columbia."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"24","container-title":["American Journal of Physiology-Cell Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.physiology.org\/doi\/pdf\/10.1152\/ajpcell.1994.267.1.C104","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,6,17]],"date-time":"2024-06-17T19:40:10Z","timestamp":1718653210000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.physiology.org\/doi\/10.1152\/ajpcell.1994.267.1.C104"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1994,7,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1994,7,1]]}},"alternative-id":["10.1152\/ajpcell.1994.267.1.C104"],"URL":"https:\/\/doi.org\/10.1152\/ajpcell.1994.267.1.c104","relation":{},"ISSN":["0363-6143","1522-1563"],"issn-type":[{"value":"0363-6143","type":"print"},{"value":"1522-1563","type":"electronic"}],"subject":[],"published":{"date-parts":[[1994,7,1]]}}}