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- Title
Heat induced HSP20 phosphorylation without increased cyclic nucleotide levels in swine carotid media.
- Authors
Rembold, Christopher M.; Kaufman, Elizabeth
- Abstract
Background: Heat pretreatment of swine carotid artery has been shown to increase ser16-heat shock protein 20 (HSP20) phosphorylation and suppress force, i.e., reduce force with only minimal reduction in ser19-myosin regulatory light chain (MRLC)phosphorylation. Results: We further investigated this response in intact histamine stimulated swine carotid artery rings. There was a heat threshold such that increased ser16-HSP20 phosphorylation and force suppression were observed between 43°C and 46°C. The increased ser16-HSP20 phosphorylation persisted up to 16 hours after 44.5°C heat treatment. Pretreatment of swine carotid media at 44.5°C increased ser16-HSP20 phosphorylation without increases in [cAMP] or [cGMP], suggesting an alternate mechanism, perhaps phosphatase inhibition, for the increase in ser16-HSP20 phosphorylation. Heat pretreatment at 47.5°C reduced force by decreasing MRLC phosphorylation rather than by large increases in ser16-HSP20 phosphorylation. HSP20 phosphorylation at the putative PKC site did not change with any treatment. Conclusion: These results demonstrate that multiple mechanisms can induce force suppression that is correlated with ser16-HSP20 phosphorylation: 1) nitrovasodilators via cGMP, 2) forskolin via cAMP, and 2) thermal stress in a cyclic nucleotide independent manner.
- Subjects
PHOSPHORYLATION; CAROTID artery; ARTERIES; HISTAMINE; NUCLEOTIDES
- Publication
BMC Physiology, 2003, Vol 3, p3
- ISSN
1472-6793
- Publication type
Article
- DOI
10.1186/1472-6793-3-3