Heat induced HSP20 phosphorylation without increased cyclic nucleotide levels in swine carotid media.
Heat induced HSP20 phosphorylation without increased cyclic nucleotide levels in swine carotid media.
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DOI:
10.1186/1472-6793-3-3
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发表时间:
2003-04-25
期刊:
影响因子:
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通讯作者:
Kaufman E
中科院分区:
文献类型:
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作者:
Rembold CM;Kaufman E
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. 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. 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.