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Am J Physiol Cell Physiol 264: C1561-C1569, 1993;
0363-6143/93 $5.00
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AJP - Cell Physiology, Vol 264, Issue 6 C1561-C1569, Copyright © 1993 by American Physiological Society

ARTICLES

Effect of heat shock, [Ca2+]i, and cAMP on inositol trisphosphate in human epidermoid A-431 cells

J. G. Kiang and D. E. McClain
Department of Clinical Physiology, Walter Reed Army Institute of Research, Washington, District of Columbia 20307-5100.

The basal levels of inositol monophosphate, inositol bisphosphate, and inositol trisphosphate (InsP3) in A-431 cells incubated in Na(+)-Hanks' solution were, respectively, 1.23 +/- 0.18, 0.17 +/- 0.03, and 0.69 +/- 0.07% of the total radioactivity in the cell. When cells were heated, InsP3 increased in a temperature-dependent manner related to the duration of heating. The active form of InsP3, inositol 1,4,5-trisphosphate, increased 237 +/- 17% after heating (45 degrees C, 20 min) then returned to baseline within 15 min after the return to 37 degrees C. The heat-induced increase in InsP3 was not observed in the absence of extracellular Ca2+ or with amiloride treatment. Treatment with the nonhydrolyzable GTP analogue 5'-guanylylimidodiphosphate stimulated that component of the InsP3 increase due to G proteins. U-73122, an inhibitor of phospholipase C-mediated processes, blocked the increase in InsP3 resulting from heat exposure. Both pertussis toxin (30 ng/ml, 24 h), an inhibitor of G inhibitory protein, and cholera toxin (1 microgram/ml, 1 h), a stimulator of G stimulatory protein, increased InsP3 in unheated cells, and heating failed to induce a further increase, suggesting that heat activates G proteins. Likewise, 8-bromoadenosine 3',5'-cyclic monophosphate (8-BrcAMP), 3-isobutyl-1-methylxanthine, Ro 20-1724, or forskolin increased InsP3 in unheated cells, and heat did not cause an additional increase. The InsP3 increase induced by 8-BrcAMP was inhibited by removal of extracellular Ca2+ or treatment with verapamil, suggesting that an influx of extracellular Ca2+ stimulates InsP3 production.(ABSTRACT TRUNCATED AT 250 WORDS)


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H.-J. Kim, E. J. Song, and K.-J. Lee
Proteomic Analysis of Protein Phosphorylations in Heat Shock Response and Thermotolerance
J. Biol. Chem., June 21, 2002; 277(26): 23193 - 23207.
[Abstract] [Full Text] [PDF]


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