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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1992-7-16
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pubmed:abstractText |
The high molecular weight form of caldesmon (h-caldesmon) is phosphorylated in vascular smooth muscle. The stoichiometry of caldesmon phosphorylation increases in response to stimulation of the muscle by several contractile agonists; however, the responsible kinase has not been identified. In this study, we have sequenced the phosphopeptides prepared from h-caldesmon phosphorylated in vitro by protein kinase C (PKC) as well as the phosphopeptides prepared from caldesmon phosphorylated in intact canine aortas that were stimulated to contract with PDBu. PKC phosphorylated three sites located in the C terminus: GSS*LKIEE, AEFLNKS*VQK and NLWEKQS*VDK, while h-caldesmon from intact tissue was phosphorylated at two separate sites also in the C terminus: VTS*PTKV and S*PAPK. By comparison to known substrate consensus sequences for various protein kinases these data suggest that h-caldesmon is directly phosphorylated by a proline-directed protein kinase and not by PKC.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
302
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
223-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1601129-Amino Acid Sequence,
pubmed-meshheading:1601129-Animals,
pubmed-meshheading:1601129-Aorta,
pubmed-meshheading:1601129-Binding Sites,
pubmed-meshheading:1601129-Calmodulin-Binding Proteins,
pubmed-meshheading:1601129-Dogs,
pubmed-meshheading:1601129-Molecular Sequence Data,
pubmed-meshheading:1601129-Molecular Weight,
pubmed-meshheading:1601129-Muscle, Smooth, Vascular,
pubmed-meshheading:1601129-Phorbol 12,13-Dibutyrate,
pubmed-meshheading:1601129-Phosphoproteins,
pubmed-meshheading:1601129-Phosphorylation,
pubmed-meshheading:1601129-Proline-Directed Protein Kinases,
pubmed-meshheading:1601129-Protein Kinase C,
pubmed-meshheading:1601129-Protein Kinases,
pubmed-meshheading:1601129-Swine
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pubmed:year |
1992
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pubmed:articleTitle |
Phosphorylation sequences in h-caldesmon from phorbol ester-stimulated canine aortas.
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pubmed:affiliation |
Department of Medicine, Indiana University School of Medicine, Indianapolis 46202.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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