Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2006-1-25
pubmed:abstractText
AMP-activated kinase (AMPK) is a highly conserved heterotrimeric kinase that functions as a metabolic regulator of cellular enzymes involved in carbohydrate and fat metabolism, which regulate ATP conservation and synthesis. Here, we investigated whether AMPK signaling has a role in the regulation of angiotensin II (Ang II)-induced proliferation in rat cardiac fibroblasts. Aminoimidazole-4-carboxamide-1-beta-ribofuranoside (AICAR) activated AMPK in rat cardiac fibroblasts and increased Ang II-induced extracellular signal-regulated kinase 1/2 phosphorylation and activity. AICAR also increased Ang II-induced c-fos mRNA expression in the cells. [3H]-thymidine and [3H]-proline incorporation by cardiac fibroblasts treated with Ang II was enhanced when the cells were pretreated with AICAR. Inhibition of AMPK by small interfering RNA for AMPKalpha1 suppressed Ang II-induced extracellular signal-regulated kinase activity, c-fos mRNA expression, and cell proliferation. Treatment of rats with AICAR (1 mg/g body weight per day) for 1 week significantly enhanced Ang II-induced hypertrophy of the myocardium. Our findings indicate that AMPK works as a stimulator of the Ang II-induced proliferative pathway in cardiac fibroblasts. Inhibition of AMPK signaling might serve as a new therapeutic target of remodeling of the hypertrophic myocardium.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/AICA ribonucleotide, http://linkedlifedata.com/resource/pubmed/chemical/AMP-Activated Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Aminoimidazole Carboxamide, http://linkedlifedata.com/resource/pubmed/chemical/Angiotensin II, http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Signal-Regulated MAP..., http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Proline, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-fos, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering, http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleotides, http://linkedlifedata.com/resource/pubmed/chemical/Thymidine
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1524-4563
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
265-70
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:16380538-AMP-Activated Protein Kinases, pubmed-meshheading:16380538-Aminoimidazole Carboxamide, pubmed-meshheading:16380538-Angiotensin II, pubmed-meshheading:16380538-Animals, pubmed-meshheading:16380538-Cardiomegaly, pubmed-meshheading:16380538-Cell Proliferation, pubmed-meshheading:16380538-Cells, Cultured, pubmed-meshheading:16380538-Drug Synergism, pubmed-meshheading:16380538-Enzyme Activation, pubmed-meshheading:16380538-Extracellular Signal-Regulated MAP Kinases, pubmed-meshheading:16380538-Fibroblasts, pubmed-meshheading:16380538-Multienzyme Complexes, pubmed-meshheading:16380538-Myocardium, pubmed-meshheading:16380538-Organ Size, pubmed-meshheading:16380538-Proline, pubmed-meshheading:16380538-Protein-Serine-Threonine Kinases, pubmed-meshheading:16380538-Proto-Oncogene Proteins c-fos, pubmed-meshheading:16380538-RNA, Messenger, pubmed-meshheading:16380538-RNA, Small Interfering, pubmed-meshheading:16380538-Rats, pubmed-meshheading:16380538-Rats, Wistar, pubmed-meshheading:16380538-Ribonucleotides, pubmed-meshheading:16380538-Signal Transduction, pubmed-meshheading:16380538-Thymidine
pubmed:year
2006
pubmed:articleTitle
Activation of AMP-activated protein kinase enhances angiotensin ii-induced proliferation in cardiac fibroblasts.
pubmed:affiliation
Department of Endocrinology and Metabolism, Dokkyo University School of Medicine, Mibu, Tochigi 321-0293, Japan. yhattori@dokkyomed.ac.jp
pubmed:publicationType
Journal Article