HSP-72 Synthesis is Promoted by Increase in (Ca2+)i or Activation of G Proteins but not pHi of cAMP
Abstract
The family of 70-kDa heat-shock proteins (HSP70) 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 deg 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 deg C were elevated at 2 h (1.5 + or - 0.1x control), reached a maximum at 8 h (2.7 + or - 0.1x control), and remained above baseline for up to 4 days. Pertussis toxin, Cholera toxin, 1,2'bis(2-aminophenoxy) ethane-N,N,N,N -tetraacetic acid
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 01, 1994
- Accession Number
- ADA283785
Entities
People
- David E. Mcclain
- Frances E. Carr
- Juliann G Kiang
- Maureen R. Burns
Organizations
- Walter Reed Army Institute of Research