|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1-2
|
|
pubmed:dateCreated |
1992-1-15
|
|
pubmed:abstractText |
Smooth muscle myosin light chain (LC) can be phosphorylated by myosin light chain kinase (MLCK) at Ser19 and Thr18 and by protein kinase C (PKC) at Thr9 and Ser1 or Ser2 under the in vitro assay conditions. Conversion of PKC to the spontaneously active protein kinase M (PKM) by proteolysis resulted in a change in the substrate specificity of the kinase. PKM phosphorylated both sets of sites in LC recognized by MLCK and PKC as analyzed by peptide mapping analysis. The PKM-catalyzed phosphorylation of these sites was not greatly affected by a MLCK inhibitor, ML-9, nor by the activators of MLCK, Ca2+ and calmodulin.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Dec
|
|
pubmed:issn |
0014-5793
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
2
|
|
pubmed:volume |
294
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
144-8
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:1743284-Amino Acid Sequence,
pubmed-meshheading:1743284-Animals,
pubmed-meshheading:1743284-Binding Sites,
pubmed-meshheading:1743284-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:1743284-Gizzard,
pubmed-meshheading:1743284-Isoelectric Focusing,
pubmed-meshheading:1743284-Kinetics,
pubmed-meshheading:1743284-Molecular Sequence Data,
pubmed-meshheading:1743284-Muscle, Smooth,
pubmed-meshheading:1743284-Myosin-Light-Chain Kinase,
pubmed-meshheading:1743284-Myosins,
pubmed-meshheading:1743284-Peptide Fragments,
pubmed-meshheading:1743284-Peptide Mapping,
pubmed-meshheading:1743284-Protein Kinase C,
pubmed-meshheading:1743284-Substrate Specificity,
pubmed-meshheading:1743284-Trypsin,
pubmed-meshheading:1743284-Turkeys
|
|
pubmed:year |
1991
|
|
pubmed:articleTitle |
Catalytic fragment of protein kinase C exhibits altered substrate specificity toward smooth muscle myosin light chain.
|
|
pubmed:affiliation |
Endocrinology and Reproduction Research Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892.
|
|
pubmed:publicationType |
Journal Article
|
