Endothelin-1 and fibroblast growth factors stimulate the mitogen-activated protein kinase signaling cascade in cardiac myocytes. The potential role of the cascade in the integration of two signaling pathways leading to myocyte hypertrophy.

Bogoyevitch, Marie A.; Glennon, Peter E.; Andersson, Monica; Clerk, Angela; Lazou, Antigone; Marshall, Christopher J.; Parker, Peter J.; Sugden, Peter H.

doi:10.1016/s0021-9258(17)42228-9

Cited by 355 publications

(15 citation statements)

References 87 publications

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“…In summary, the current studies demonstrate that D3 stimulates MAPK by a PKC-dependent pathway, analogous to the previous observation with D3-stimulated raf activation. Recent studies have identified other agonists that activate MAPK by PKC-dependent mechanisms (48). These agonists utilize heterotrimeric GTP protein-coupled receptors and are unrelated to D3 (48).…”

Section: Mapkmentioning

confidence: 99%

Protein Kinase C and Mitogen-activated Protein Kinase Are Required for 1,25-Dihydroxyvitamin D3-stimulated Egr Induction

Beno

Brady

Bissonnette

et al. 1995

Journal of Biological Chemistry

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Recent studies have demonstrated that 1,25-dihydroxyvitamin D3 (D3) can activate Raf kinase and induce Egr expression in cultured rat hepatic Ito cells (Lissoos, T. W., Beno, D. W. A., and Davis, B. H. (1993) J. Biol. Chem. 268, 25132-25138). Since Raf is an upstream activator of mitogen-activated protein kinase (MAPK), the current study evaluated the ability of D3 to activate MAPK. D3-activated MAPK and induced its cytoplasmic to perinuclear translocation in Ito cells. MAPK activation was found to be protein kinase C-dependent, which was analogous to previous studies of D3 and Raf activation. To further explore the D3 cascade, a series of transient transfections were performed using dominant negative raf and MAPK mutant plasmids which effectively block Ras-induced Raf and MAPK activity, respectively. D3 induced a marked increase in the expression of a chloramphenicol acetyltransferase reporter gene linked to the Egr promoter (egr-CAT). When the dominant negative Raf plasmid was co-transfected, there was no significant reduction in egr-CAT. In contrast, when the dominant negative MAPK plasmid was co-transfected, egr-CAT induction was completely abolished. These results suggest that 1) D3 stimulates MAPK via a protein kinase C-dependent pathway, 2) D3-induced Egr expression can occur via a pathway independent of Ras-induced Raf, and 3) D3 absolutely requires MAPK activity for Egr expression.

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Section: Mapkmentioning

confidence: 99%

Protein Kinase C and Mitogen-activated Protein Kinase Are Required for 1,25-Dihydroxyvitamin D3-stimulated Egr Induction

Beno

Brady

Bissonnette

et al. 1995

Journal of Biological Chemistry

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“…In cultured cardiac myocytes, ERKs are activated by hypertrophic stimuli such as angiotensin II (Ang II) [10], phenylephrine [11,12], endothelin 1 [12][13][14] and PMA [13], as well as cellular stresses such as mechanical stretching [15,16] or osmotic shock [17,18]. Although the role of ERKs in phenylephrineinduced cardiac hypertrophy has been studied by several investigators with different methods, reported roles of ERKs in cardiac hypertrophy vary substantially [19][20][21][22][23].…”

Section: Introductionmentioning

confidence: 99%

Specific role of the extracellular signal-regulated kinase pathway in angiotensin II-induced cardiac hypertrophy in vitro

et al. 2000

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Although MAP (mitogen-activated protein) kinases are implicated in cell proliferation and differentiation in many cell types, the role of MAP kinases in cardiac hypertrophy remains unclear. We examined the role of extracellular signal-regulated protein kinase (ERK), c-Jun N-terminal kinase (JNK) and p38 MAP kinase in angiotensin II (Ang II)-induced hypertrophy compared with phenylephrine-induced hypertrophy in neonatal rat cardiac myocytes. Both Ang II and phenylephrine activated ERKs to a similar extent, whereas phenylephrine caused stronger and more sustained activation of JNK and p38 than Ang II. PD98059, a specific inhibitor of MAPK/ERK kinase (MEK),inhibited Ang II-induced, but not phenylephrine-induced, expression of atrial natriuretic factor (ANF) at both the mRNA and polypeptide levels. SB203580, a specific inhibitor of p38 and some JNK isoforms, did not show significant effects on ANF expression induced by Ang II or phenylephrine. Although PD98059 and dominant-negative MEK1 blocked Ang II-induced activation of the ANF promoter, SB203580 or dominant-negative MEK kinase 1 (MEKK1) showed no effect. Phenylephrine-induced ANF promoter activation was significantly inhibited by SB203580 and dominant-negative MEKK1, but not by PD98059 or dominant-negative MEK1. Dominant-negative Ras inhibited both ERK activation and ANF up-regulation by Ang II, whereas constitutively active forms of Ras and MEK were sufficient to activate the ANF promoter. Dominant-negative Ras also partly inhibited the phenylephrine-induced activation of ANF promoter. PD98059 did not affect other markers of Ang II-induced hypertrophy, such as skeletal alpha-actin and c-fos expression, increases in the rate of protein synthesis or rapid sarcomeric actin organization. These results suggest that Ang II uses ERK for ANF expression, whereas phenylephrine uses other pathways. The Ras/ERK pathway selectively mediates ANF expression in various phenotypes observed in Ang II-induced hypertrophy. The ERK pathway mediates an agonist-specific and phenotype-specific response in cardiac hypertrophy.

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“…ET-1 may be the culprit of pathologically increased vascular resistance both in the lung and in the arterial circulation. In addition ET-1 triggers intracellular events leading to long-term expression of fetal genes and protein synthesis, promoting growth and hypertrophy both in myocardium and in vascular smooth muscle (28,29); thus, it may well be involved in the progressive vascular and cardiac remodeling seen in CHF. Elevated plasma and tissue ET-1 levels and changes in ET receptor density and activity have been demonstrated in CHF (for a recent review see Ref.…”

Section: Congestive Heart Failure (Chf)mentioning

confidence: 99%

Endothelin-1 and Endothelin Receptor Antagonists in Cardiovascular Remodeling

Kirchengast¹,

Munter²

1999

Experimental Biology and Medicine

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Endothelins build a peptide family composed of three isoforms, each of them containing 21 amino acids. Endothelin-1 is the isoform mainly responsible for any cardiovascular action and therefore the sole scope of this review. Endothelin-1 is the most potent endogenous vasoconstrictor known; in addition it acts as a potent (co)mitogen. There is a substantial body of experimental evidence that endothelin-1 may contribute not only to sustained vasoconstriction, but also to remodeling within the cardiovascular system. Thus, with the help of endothelin receptor antagonists (available for a few years) the involvement of mainly ET A receptors in structural diseases such as heart failure, pulmonary hypertension, atherosclerosis, restenosis, systemic hypertension, and chronic renal failure has been shown. These data make endothelin receptor antagonists, and especially those selective for the ET A receptor, promising agents for the treatment of chronic cardiovascular diseases associated with remodeling. Currently several chemically distinct, orally available members of this novel class of therapeutic agents are under clinical investigation.

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Endothelin-1 and fibroblast growth factors stimulate the mitogen-activated protein kinase signaling cascade in cardiac myocytes. The potential role of the cascade in the integration of two signaling pathways leading to myocyte hypertrophy.

Cited by 355 publications

References 87 publications

Protein Kinase C and Mitogen-activated Protein Kinase Are Required for 1,25-Dihydroxyvitamin D3-stimulated Egr Induction

Protein Kinase C and Mitogen-activated Protein Kinase Are Required for 1,25-Dihydroxyvitamin D3-stimulated Egr Induction

Specific role of the extracellular signal-regulated kinase pathway in angiotensin II-induced cardiac hypertrophy in vitro

Endothelin-1 and Endothelin Receptor Antagonists in Cardiovascular Remodeling

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