Stress-Activated Protein Kinases in Cardiovascular Disease

Force, Thomas; Pombo, Celia M.; Avruch, Joseph; Bonventre, Joseph V.; Kyriakis, John

doi:10.1161/01.res.78.6.947

Cited by 213 publications

(146 citation statements)

References 36 publications

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“…9,10 Recently, AP-1 has been reported to be rapidly activated in balloon-injured artery and this activated AP-1 contained c-Jun, 11 and similar findings have been also obtained by our recent work. 12 Furthermore, in rats, vascular AP-1, composed of c-Jun, is also significantly activated in vivo by acute hypertension or angiotensin II administration.…”

Section: Of Dn-c-jun Was Examined On Balloon Injury-induced Intimal Hsupporting

confidence: 89%

Dominant negative c-Jun gene transfer inhibits vascular smooth muscle cell proliferation and neointimal hyperplasia in rats

et al. 2001

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Section: Of Dn-c-jun Was Examined On Balloon Injury-induced Intimal Hsupporting

confidence: 89%

Dominant negative c-Jun gene transfer inhibits vascular smooth muscle cell proliferation and neointimal hyperplasia in rats

et al. 2001

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“…Activation of the SAPK/JNK is believed to be critical for the cell's response to environmental insults, such as heat stress. Evidence obtained from study of cultured cells indicates that SAPK/JNK is involved in mediating cell growth or hypertrophy via activation of transcription factor activator protein-1 (AP-1) (30,31), and in cell apoptosis (32,33). Our findings demonstrated that heat stress selectively induces SAPK activation in tissues of intact animals, suggesting a physiological relevance of these protein kinases in response to Possible Mechanisms of SAPK/JNK Activation-Although it is established that heat stress activates SAPK/JNK kinases in cultured cells in vitro, the initiating signals responsible for such activation remain to be clarified.…”

Section: Time Course Of Sapk Activation-sapk/jnk Phosphorylatementioning

confidence: 99%

“…Elk-1, together with serum response factor, controls transcription from the serum response element. These transcription factors regulate gene expression, including matrix metalloproteinase, adhesion molecule E-selectin, NO synthase, interleukin-8, and proliferating cell nuclear antigen (31). These genes have been demonstrated to play a key role in cell growth and cellular homeostasis.…”

Section: Time Course Of Sapk Activation-sapk/jnk Phosphorylatementioning

confidence: 99%

Discordant Activation of Stress-activated Protein Kinases or c-Jun NH2-terminal Protein Kinases in Tissues of Heat-stressed Mice

Metzler

1997

Journal of Biological Chemistry

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Stress-activated protein kinases (SAPK) or c-Jun NH 2 -terminal protein kinases (JNK) are believed to be crucial signal transducers between stress stimuli and genetic responses in mammalian cells. These kinases are activated in various types of in vitro cultured cells by heat shock, but a similar activation of SAPK/JNK in tissues in vivo has yet to be shown. In the present study, C57BL/6 mice were exposed to elevated ambient temperature for various time periods, and SAPK/JNK activities determined in protein extracts of brain, heart, liver, spleen, lung, and kidney using protein kinase assay and Western blot analyses. The time course and relative magnitude of the heat-induced SAPK/JNK activity differed among tissues of the same animal. Significant activation of SAPK/JNK was achieved in heart, liver, and kidney at 60 or 90 min of heat stress. This increased activity of SAPK/JNK kinases was demonstrated to result from activation or phosphorylation of existing proteins in tissues. The maximal activation of these kinases showed no direct relationship with the elevation in body temperature (38 -40.5°C). Interestingly, SAPK/JNK activation did not occur in lung, brain, or spleen of the same heat-stressed mouse. Although elevated body temperature (40.5°C) did not result in SAPK/JNK activation in spleen and lung tissues, heat stress induced SAPK/JNK activation in cultured organs or fibroblasts derived from spleen or lung of C57BL/6 mice. Furthermore, activity and amount of SAPK/JNK proteins were the most abundant in brain among tissues examined. Thus, our findings demonstrated that heat shock-induced SAPK/ JNK activation in vivo lacks much of the characteristic coordinate control of activation of cultured cell lines, and suggests that the mechanisms controlling SAPK/ JNK activation are influenced by physiologic factors that cannot be studied in vitro.

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“…Several parallel kinase cascades lead to the activation of different members of the MAP kinase family, including extracellular signal-regulated protein kinase (ERK), c-Jun N-terminal kinase (JNK) and p38. Recent studies have shown that ERKs mediate cellular responses initiated by growth factors, whereas JNK and p38 predominantly mediate cellular responses induced by environmental stress or proinflammatory cytokines, although some cross-talk exists between extracellular stimuli and the kinases activated (reviewed in [1][2][3][4][5]). Many growth factors activate ERKs via Ras-dependent mechanisms.…”

Section: Introductionmentioning

confidence: 99%

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

Aoki

Richmond

Izumo

et al. 2000

Biochemical Journal

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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 α-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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Stress-Activated Protein Kinases in Cardiovascular Disease

Cited by 213 publications

References 36 publications

Dominant negative c-Jun gene transfer inhibits vascular smooth muscle cell proliferation and neointimal hyperplasia in rats

Dominant negative c-Jun gene transfer inhibits vascular smooth muscle cell proliferation and neointimal hyperplasia in rats

Discordant Activation of Stress-activated Protein Kinases or c-Jun NH2-terminal Protein Kinases in Tissues of Heat-stressed Mice

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

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