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Updated: Sep 26, 2026
Standardized Methods for Measuring Induction of the Heat Shock Response in Caenorhabditis elegans
Published on: July 3, 2020
Heat induced HSP20 phosphorylation without increased cyclic nucleotide levels in swine carotid media
Christopher M Rembold1, Elizabeth Kaufman
1Cardiovascular Division, Department of Internal Medicine, University of Virginia Health System, Charlottesville, Virginia 22908 USA. crembold@virginia.edu
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 degrees C and 46 degrees C. The increased ser16-HSP20 phosphorylation persisted up to 16 hours after 44.5 degrees C heat treatment. Pretreatment of swine carotid media at 44.5 degrees 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 degrees 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.
