Heat shock-induced, caspase-3-independent rapid breakdown of Akt and consequent alteration of its total phosphorylation/activity level.
The immediate effect of a 15-min heat shock was examined on the level and the activity of Akt. Following heat shock, the Akt level decreased by 15-70% in a temperature-dependent and phosphorylation status-independent manner. This decrease of Akt level was not prevented by caspase inhibitors. At 48 degrees C, the extent of the breakdown was so immense that the total phosphorylation/activity level of Akt was not increased over the control level, implying that the total cellular activity of Akt governed by the level and the molar activity does not necessarily undergo the ensuing change.
Mo
H J
HJ
Department of Pharmacology, College of Medicine, Konkuk University, 322 Danwol-dong, Chungju-city, Chungchongbuk-do, 380-701, Korea.
Lee
H C
HC
Choi
H S
HS
Yang
S I
SI
D000818:Animals; D019556:COS Cells; D053148:Caspase 3; D020169:Caspases / Q000378:metabolism*; D018274:Electroporation; D018869:Heat-Shock Response; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases; D011518:Proto-Oncogene Proteins / Q000378:metabolism*; D051057:Proto-Oncogene Proteins c-akt
D011518:Proto-Oncogene Proteins; D017346:Protein Serine-Threonine Kinases; D051057:Proto-Oncogene Proteins c-akt; D053148:Caspase 3; D020169:Caspases