Abstract:
:Telokin, a 17 kDa smooth muscle specific protein, consists of the C-terminal domain of MLCK, is phosphorylated by PKA and PKG at Ser13 in vivo (Wu et al. (1998) J Biol Chem 273: 11362-11369; Walker et al. (2001) J. Biol Chem 276: 24519-24524) and is proposed to induce Ca2+-desensitization through activation of myosin phosphatase (Wu et al. (1998) J. Biol Chem 273: 11362-11369). Telokin is reported to be highly expressed in phasic with only trace amounts in tonic smooth muscle. In alpha-toxin permeabilized femoral artery, 5 microM 8-Br-cGMP induced a two-fold increase in telokin phosphorylation and a maximal 30% relaxation of Ca2+-activated force compared to a 90% relaxation in phasic ileum muscle consistent with the relative amounts of telokin expressed in ileum, 27+/-4.6 microM SEM compared to 6+/-1.7 microM SEM, in femoral artery. Recombinant Wt telokin and the phospho-telokin mutant, S13D relaxed telokin-depleted femoral artery, by 38+/-8% SEM and 60+/-20% SEM, respectively. 8-Br-cGMP increased the rate and decreased the amplitude of force development initiated by photolysis of caged ATP in alpha-toxin permeabilized ileum and femoral artery smooth muscle, consistent with a cGMP-induced increase in phosphatase activity. Similarly, in telokin depleted ileum, recombinant S13D mutant telokin significantly increased the rate (0.08+/-0.01 s-1 vs. 014+/-0.02 s-1) and decreased force amplitude. In conclusion, our data support a role for telokin in cyclic nucleotide-induced relaxation of not only phasic, but also tonic smooth muscle and that this relaxation is mediated by activation of myosin phosphatase activity leading to a decrease in myosin light chain phosphorylation.
journal_name
J Muscle Res Cell Motiljournal_title
Journal of muscle research and cell motilityauthors
Choudhury N,Khromov AS,Somlyo AP,Somlyo AVdoi
10.1007/s10974-004-7807-xkeywords:
subject
Has Abstractpub_date
2004-01-01 00:00:00pages
657-65issue
8eissn
0142-4319issn
1573-2657journal_volume
25pub_type
杂志文章abstract::Protein kinase C (PKC) is known to play important roles in integrin mediated cell spreading. This study investigated the role of PKC during insulin mediated muscle cell spreading, which was independent of integrin alpha5. We found that PKC-alpha becomes active and localise to membrane during insulin mediated cell spre...
journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
pub_type: 杂志文章
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
pub_type: 杂志文章,评审
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
pub_type: 杂志文章
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journal_title:Journal of muscle research and cell motility
pub_type: 杂志文章
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journal_title:Journal of muscle research and cell motility
pub_type: 杂志文章
doi:10.1007/BF00115451
更新日期:1993-04-01 00:00:00
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journal_title:Journal of muscle research and cell motility
pub_type: 杂志文章,评审
doi:10.1007/s10974-015-9438-9
更新日期:2015-12-01 00:00:00
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journal_title:Journal of muscle research and cell motility
pub_type: 杂志文章
doi:10.1007/s10974-010-9237-2
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
pub_type: 杂志文章,评审
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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