ArticleBMC physiology2003
Heat induced HSP20 phosphorylation without increased cyclic nucleotide levels in swine carotid media.
Article in BMC physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed.
- Cyclic GMP signaling in cardiovascular pathophysiology and therapeutics.Pharmacology & therapeutics · 2009Review
- Small heat shock proteins in smooth muscle.Pharmacology & therapeutics · 2008Review
- Physiologic properties and regulation of the actin cytoskeleton in vascular smooth muscle.Journal of cardiovascular pharmacology and therapeutics · 2008Review
- HSP20 phosphorylation and interstitial metabolites in hypoxia-induced dilation of swine coronary arteries.Acta physiologica Scandinavica · 2005Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
backgroundHeat 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.
resultsWe 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.
conclusionThese 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.
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Registered trials
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