| pubmed-article:2850799 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2850799 | lifeskim:mentions | umls-concept:C0008051 | lld:lifeskim |
| pubmed-article:2850799 | lifeskim:mentions | umls-concept:C1510668 | lld:lifeskim |
| pubmed-article:2850799 | lifeskim:mentions | umls-concept:C0006746 | lld:lifeskim |
| pubmed-article:2850799 | lifeskim:mentions | umls-concept:C0813988 | lld:lifeskim |
| pubmed-article:2850799 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:2850799 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:2850799 | pubmed:dateCreated | 1989-2-13 | lld:pubmed |
| pubmed-article:2850799 | pubmed:abstractText | Caldesmon, an actin- and calmodulin-binding protein of smooth muscle, is a protein serine/threonine kinase capable of Ca2+/calmodulin-dependent autophosphorylation [Scott-Woo & Walsh (1988) Biochem. J. 252, 463-472]. Phosphorylation nullifies the inhibitory effect of caldesmon on the actin-activated Mg2+-ATPase activity of smooth-muscle myosin [Ngai & Walsh (1987) Biochem. J. 244, 417-425]. We have characterized the kinase activity of caldesmon of chicken gizzard smooth muscle. Autophosphorylation requires Ca2+/calmodulin, but is unaffected by other second messengers (Ca2+/phospholipid/diacylglycerol, cyclic AMP or cyclic GMP), and is inhibited by the calmodulin antagonists chlorpromazine and compound 48/80, with 50% inhibition at 39.8 microM and 12.0 ng/ml respectively. Half-maximal activation of autophosphorylation occurs at 60-80 nM-Ca2+ and 0.14 microM-calmodulin, and maximal activity at 0.14-0.18 microM-Ca2+ and 1 microM-calmodulin; activation is gradually lost at higher Ca2+ and calmodulin concentrations. Autophosphorylation is pH-dependent, with maximal activity over the range pH 7-9, and requires free Mg2+ in addition to the MgATP2- substrate. The Km for ATP is 15.6 +/- 4.1 microM (mean +/- S.D., n = 4), and kinase activity is inhibited by increasing ionic strength [half-maximal inhibition at I = 0.094 +/- 0.009 M (mean +/- S.D., n = 4)]. Autophosphorylation does not affect the rate of hydrolysis of caldesmon (free or bound to calmodulin) by alpha-chymotrypsin. However, a slight difference in peptides generated from phospho- and dephospho-forms of caldesmon is observed. The binding of phospho- or dephospho-caldesmon to F-actin protects the protein against chymotryptic digestion, but does not alter the pattern of peptide generation. Characterization of proteolytic fragments of caldesmon generated by alpha-chymotrypsin and Staphylococcus aureus V8 protease enables localization of the phosphorylation sites and the kinase active site within the caldesmon molecule. | lld:pubmed |
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| pubmed-article:2850799 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2850799 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2850799 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2850799 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2850799 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:2850799 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:2850799 | pubmed:author | pubmed-author:WalshM PMP | lld:pubmed |
| pubmed-article:2850799 | pubmed:author | pubmed-author:Scott-WooG... | lld:pubmed |
| pubmed-article:2850799 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2850799 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:2850799 | pubmed:volume | 255 | lld:pubmed |
| pubmed-article:2850799 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2850799 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2850799 | pubmed:pagination | 817-24 | lld:pubmed |
| pubmed-article:2850799 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2850799 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2850799 | pubmed:articleTitle | Characterization of the autophosphorylation of chicken gizzard caldesmon. | lld:pubmed |
| pubmed-article:2850799 | pubmed:affiliation | Department of Medical Biochemistry, Faculty of Medicine, University of Calgary, Alberta, Canada. | lld:pubmed |
| pubmed-article:2850799 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2850799 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2850799 | lld:pubmed |
