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Differential effects of 17[3‐estradiol on mitogen‐activated protein kinasepathways in rat cardiomyocytes
Author(s) -
Simone Nuedling,
Stefan Kahlert,
Kerstin Loebbert,
Rainer Meyer,
Hans Vetter,
Christian Grohé
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00816-9
Subject(s) - mapk/erk pathway , p38 mitogen activated protein kinases , kinase , phosphorylation , signal transduction , protein kinase a , microbiology and biotechnology , phosphatase , mitogen activated protein kinase 3 , mitogen activated protein kinase , estrogen , biology , chemistry , medicine , endocrinology
Cardiac myocytes contain functional estrogen receptors, however, the effect of estrogen on growth-related signaling pathways such as mitogen-activated protein kinases (MAPK) in the pathogenesis of cardiac disease is unclear. MAPKs are critically involved in regulatory signaling pathways which ultimately lead to cardiac hypertrophy. Here we show that 17beta-estradiol (E2) activates extracellular signal-regulated kinase (ERK1/2), c-Jun-NH2-terminal protein kinase (JNK) and p38 in rat cardiomyocytes in a distinctive pattern. As shown by immunoblot analysis and phosphorylation assays, E2 (10(-9) M) induced a rapid and transient activation of ERK1/2 and a rapid but sustained increase of JNK phosphorylation. In contrast, E2 had only a marginal effect on p38 activation. Furthermore, MAPK phosphatase expression was induced by E2 and E2-stimulated expression of endothelial and inducible NO synthase was inhibited by PD 98059, an inhibitor of the ERK pathway. These novel observations may help to explain the role of estrogen in gender-based differences found in cardiac disease.