Source:http://linkedlifedata.com/resource/pubmed/id/10821688
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
20
|
pubmed:dateCreated |
2000-6-21
|
pubmed:abstractText |
Hsp27 kinase activities were studied in adult rat ventricular myocytes following sequential chromatography on Mono Q and Mono S. A basal level of activity was present following cell isolation. FPLC on Mono Q revealed three peaks of activity, peaks 'a', 'b', and 'c'. A fourth peak, 'd', was detected upon subsequent chromatography of the Mono Q flow-through on Mono S. Immunoblotting revealed that peaks 'a', 'b', and 'c' contained predominantly a 49 kDa form of MAPKAP kinase-2. Peak 'd' contained a 43 kDa form. 'In-gel' kinase assays using hsp27 indicated both forms of MAPKAP kinase-2 were active. No other bands of hsp27 kinase activity were detected. Both forms of hsp27 kinase immunoprecipitated with a MAPKAP kinase-2 antibody and have therefore been named MAPKAP kinase-2alpha (p49) and MAPKAP kinase-2beta (p43). MAPKAP kinase-2beta chromatographed on Superose 12 as a 60.7 kDa monomer whereas the behavior of MAPKAP kinase-2alpha suggested both a 65.7 kDa monomer and higher molecular mass complexes. Both activities phosphorylated hsp27 on serine residues, and two-dimensional phosphopeptide mapping indicated the same sites were phosphorylated. A tumor-promoting phorbol ester, phorbol 12-myristate 13-acetate (PMA), stimulated both MAPKAP kinase-2alpha and MAPKAP kinase-2beta activity. Inhibition of MEK activation with PD 98059 or p38alpha/beta MAP kinase activity with SB203580 blocked activation by PMA. However, whereas PD 98059 inhibited only the PMA-stimulated activation, SB203580 inhibited both PMA-stimulated and basal hsp27 phosphorylation. These data demonstrate the presence of two forms of MAPKAP kinase-2 in adult ventricular myocytes. Both forms are activated indirectly by the ERK MAP kinase pathway and directly by p38 MAP kinase but independently regulated.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/HSP27 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSPB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hspb1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/MAP-kinase-activated kinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0006-2960
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
23
|
pubmed:volume |
39
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
6145-56
|
pubmed:dateRevised |
2010-10-4
|
pubmed:meshHeading |
pubmed-meshheading:10821688-Amino Acid Sequence,
pubmed-meshheading:10821688-Animals,
pubmed-meshheading:10821688-Chromatography, Ion Exchange,
pubmed-meshheading:10821688-Dogs,
pubmed-meshheading:10821688-HSP27 Heat-Shock Proteins,
pubmed-meshheading:10821688-HeLa Cells,
pubmed-meshheading:10821688-Heat-Shock Proteins,
pubmed-meshheading:10821688-Humans,
pubmed-meshheading:10821688-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:10821688-Isoenzymes,
pubmed-meshheading:10821688-Male,
pubmed-meshheading:10821688-Molecular Sequence Data,
pubmed-meshheading:10821688-Myocardium,
pubmed-meshheading:10821688-Neoplasm Proteins,
pubmed-meshheading:10821688-PC12 Cells,
pubmed-meshheading:10821688-Phosphorylation,
pubmed-meshheading:10821688-Precipitin Tests,
pubmed-meshheading:10821688-Protein-Serine-Threonine Kinases,
pubmed-meshheading:10821688-Rabbits,
pubmed-meshheading:10821688-Rats,
pubmed-meshheading:10821688-Rats, Sprague-Dawley
|
pubmed:year |
2000
|
pubmed:articleTitle |
Two distinct forms of MAPKAP kinase-2 in adult cardiac ventricular myocytes.
|
pubmed:affiliation |
Institut de Cardiologie de Montréal, Centre de Recherche, 5000 rue Bélanger est, Montréal, PQ, Canada, H1T 1C8.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|