Functionally Opposing Roles of Extracellular Signal-Regulated Kinase 1/2 and p38 Mitogen-Activated Protein Kinase in the Regulation of Cardiac Contractility
Author(s) -
István Szokodi,
Risto Kerkelä,
AnnaMaria Kubin,
Balázs Sármán,
Sampsa Pikkarainen,
Attila Kónyi,
Iván Horváth,
Lajos Papp,
Miklós Tóth,
Réka Skoumal,
Heikki Ruskoaho
Publication year - 2008
Publication title -
circulation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.795
H-Index - 607
eISSN - 1524-4539
pISSN - 0009-7322
DOI - 10.1161/circulationaha.107.758623
Subject(s) - contractility , mapk/erk pathway , protein kinase a , kinase , p38 mitogen activated protein kinases , phospholamban , microbiology and biotechnology , phosphorylation , signal transduction , ribosomal s6 kinase , endocrinology , medicine , biology , protein kinase b , p70 s6 kinase 1
Extracellular signal-regulated kinase 1/2 (ERK1/2) and p38 mitogen-activated protein kinase (p38-MAPK) have been shown to regulate various cellular processes, including cell growth, proliferation, and apoptosis in the heart. However, the function of these signaling pathways in the control of cardiac contractility is unclear. Here, we characterized the contribution of ERK1/2 and p38-MAPK to the inotropic effect of endothelin-1 (ET-1).
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