The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
G-protein-mediated Ca2+ sensitization of smooth muscle contraction through myosin light chain phosphorylation
Open accessAbstract
The Ca2+ sensitivities of tonic (pulmonary and femoral artery) and phasic (portal vein and ileum) smooth muscles and the effects of guanosine 5'-O-(gamma-thiotriphosphate) (GTP gamma S) and norepinephrine on Ca2+ sensitivity of force development and myosin light chain (MLC20) phosphorylation were determined in permeabilized preparations that retained coupled receptors and endogenous calmodulin. The Ca2+ sensitivity of force was higher (approximately 3-fold) in the tonic than in the phasic smooth muscles. The nucleotide specificity of Ca2+ sensitization was: GTP gamma S much greater than GTP greater than ITP much greater than CTP = UTP. Baseline phosphorylation (7% at pCa greater than 8) and maximal phosphorylation (58% at pCa 5.0) were both lower in portal vein than in femoral artery (20 and 97%). Norepinephrine and GTP gamma S increased phosphorylation at constant [Ca2+] (pCa 7.0-6.5). MLC20 phosphorylation induced by norepinephrine was completely inhibited by guanosine 5'-O-(beta-thiodiphosphate) (GDP beta S). In portal vein at pCa 5, GTP gamma S increased phosphorylation from 58%, the maximal Ca2(+)-activated value, to 75%, and at pCa greater than 8, from 7 to 13%. In femoral artery at pCa 5, neither phosphorylation (97%) nor force was affected by GTP gamma S, while at pCa greater than 8, GTP gamma S caused an increase in force (16% of maximum) with a borderline increase in MLC20 phosphorylation (from 20 to 27%). MLC20 phosphorylation (up to 100%) was positively correlated with force. The major results support the hypothesis that the G-protein coupled Ca2(+)-sensitizing effect of agonists on force development is secondary to increased MLC20 phosphorylation.
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Cites
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Cross-bridge phosphorylation and regulation of latch state in smooth muscle
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Cytosolic heparin inhibits muscarinic and α-adrenergic Ca2+ release in smooth muscle
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Self-citationCell calcium and its regulation in smooth muscle
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Cited by
Jalink, K., van Corven, E. J., Hengeveld, T., Morii, N., Narumiya, S., & Moolenaar, W. H. (1994) · The Journal of cell biology · doi:10.1083/jcb.126.3.801 · Cited by 608
Regulation of Myosin Phosphatase by a Specific Interaction with cGMP- Dependent Protein Kinase Iα
Surks, H. K., Mochizuki, N., Kasai, Y., Georgescu, S. P., Tang, K. M., Ito, M., Lincoln, T. M., & Mendelsohn, M. E. (1999) · Science · doi:10.1126/science.286.5444.1583 · Cited by 527
Involvement of rho p21 in the GTP-enhanced calcium ion sensitivity of smooth muscle contraction.
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Regulation of smooth muscle calcium sensitivity: KCl as a calcium-sensitizing stimulus
Ratz, P. H., Berg, K. M., Urban, N. H., & Miner, A. S. (2005) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00529.2004 · Cited by 287
Metadata
- Authors
- Kitazawa, T., Gaylinn, B. D., Denney, G. H., & Somlyo, A. P.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1991-01
- Volume
- 266
- Issue
- 3
- Pages
- 1708-1715
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1542006519
- Cited by
- 318
- References
- 29
- FWCI
- 7.74
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Kitazawa, T., Gaylinn, B. D., Denney, G. H., & Somlyo, A. P. (1991). G-protein-mediated Ca2+ sensitization of smooth muscle contraction through myosin light chain phosphorylation. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)52353-x
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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