H2O2-induced Ca2+overload in NRVM involves ERK1/2 MAP kinases: role for an NHE-1-dependent pathway

Rothstein, Emily C.; Byron, Kenneth L.; Reed, Ryan E; Fliegel, Larry; Lucchesi, Pamela A.

doi:10.1152/ajpheart.00198.2002

Cited by 97 publications

(95 citation statements)

References 42 publications

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“…FBP completely blocked ERK protein phosphorylation and partially inhibited that of p38 MAPK. Previous studies have shown that H 2 O 2 (a direct ROS stimulator) rapidly activated ERK and p38 proteins in PC12 cells [44], and that ROS are involved in cell death via the ERK1/2 signaling pathway [29,36,45]. These data imply that mediation of cell death by ROS may be closely related to MAPK signaling.…”

Section: Discussionmentioning

confidence: 75%

Neuroprotection by fructose-1,6-bisphosphate involves ROS alterations via p38 MAPK/ERK

et al. 2004

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Section: Discussionmentioning

confidence: 75%

Neuroprotection by fructose-1,6-bisphosphate involves ROS alterations via p38 MAPK/ERK

et al. 2004

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“…In cardiac myocytes, candidate enzymes in ROS-and Gα i / o -mediated signal transduction pathways are tyrosine kinase (15,16) and phosphatidylinositol 3-kinase (PI3K) (16,17), because activation of these enzymes might lead to the cardiac pathophysiological processes mentioned above (2). In addition, activation of the Na + / H + exchanger (NHE) via mitogen-activated protein kinase / extracellular signalregulated kinase kinase (MEK) was suggested to be involved in H 2 O 2 -induced NCX activation (18,19). We hypothesized that a Gα i / o -mediated pathway is involved in NCX activation by H 2 O 2 .…”

Section: +mentioning

confidence: 99%

Mechanism of Na+/Ca2+ Exchanger Activation by Hydrogen Peroxide in Guinea-Pig Ventricular Myocytes

et al. 2007

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Abstract. Using the whole-cell voltage clamp, we examined the mechanism of activation of the Na + / Ca 2+ exchanger (NCX) by hydrogen peroxide (H 2 O 2 ) in isolated guinea-pig cardiac ventricular myocytes. Exposure to H 2 O 2 increased the NCX current. The effect was inhibited by cariporide, an inhibitor of the Na + / H + exchanger (NHE), suggesting that there are NHEdependent and -independent pathways in the effect of H 2 O 2 on NCX. In addition, both pathways were blocked by edaravone, a hydroxyl radical (•OH) scavenger; pertussis toxin, a Gα i / o protein inhibitor; and U0126, an inhibitor of mitogen-activated protein kinase / extracellular signalregulated kinase kinase (MEK). On the other hand, wortmannin, a phosphatidylinositol 3-kinase (PI3K) inhibitor, inhibited only the NHE-dependent pathway, while PP2, a Src family protein tyrosine kinase inhibitor, inhibited only the NHE-independent pathway. Taken together, our data suggest that H 2 O 2 increases the NCX current via two signal transduction pathways. The common pathway is the conversion of H 2 O 2 to •OH, which activates Gα i / o protein and a mitogen-activated protein (MAP) kinase signaling pathway. Then, one pathway activates NHE with a PI3K-dependent mechanism and indirectly increases the NCX current. Another pathway involves activation of a Src family tyrosine kinase.

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“…[37][38][39] An appropriate amount of ROS, usually a small amount, activates phosphokinases and increases the intracellular Ca 2+ level. 40,41) However, a large amount induces hyperoxidation of DNA, proteins, and lipids, which results in cell impairment. 42,43) ROS-induced apoptosis is well recognized in tumor cells treated with anticancer drugs and γ-rayirradiation.…”

Section: -7)mentioning

confidence: 99%

Reactive oxygen species (ROS) control the expression of Bcl‐2 family proteins by regulating their phosphorylation and ubiquitination

Li¹,

et al. 2004

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We examined the influence of ROS on the phosphorylation and complex formation of Bcl-2 family proteins in Mn-superoxide dismutase (SOD) antisense-transfected squamous cell carcinoma cells, OSC-4 cells. The increase of intracellular ROS level induced by cis-diamminedichloroplatinum (CDDP) and γ γ γ γ-ray treatment was greater in antisense-transfected cells than in control vector-transfected cells, and apoptosis was more extensively induced in the former. Antisense-transfected cells expressed high levels of Bax and Bak, but low levels of Bcl-2 and Bcl-X L when treated with CDDP, peplomycin, 5-fluorouracil or γ γ γ γ-rays. After treatment with these agents, the phosphorylation of protein kinase A, Bcl-2 (Thr56) and Bad (Ser155) was increased, especially in antioxidant (N-acetylcysteine and pyrrolidine dithiocarbamate)-pretreated control cells, but the phosphorylation levels were very low in the antisense-transfected cells. Bcl-2 ubiquitination was increased, but ubiquitination of Bad and Bax was decreased in the antisense-transfected cells, although their ubiquitination was increased by the antioxidants. These results reveal that ROS induce apoptosis by regulating the phosphorylation and ubiquitination of Bcl-2 family proteins, resulting in increased proapoptotic protein levels and decreased antiapoptotic protein expression. here are multiple signal pathways to induce apoptosis, including those originating from mitochondria and Fas. 1-4)The signal originating from Fas and Fas-associated proteins passes to caspase 3 through caspase 8 and other caspases. 5-7)The mitochondrial signal is also transduced to caspase 3 via cytochrome c, apoptosis protease-activating factor-1, ATP, and caspase 9. 8) These two pathways exhibit cross-talk with a proapoptotic Bcl-2 family protein, Bid. 9) Bcl-2 family proteins including Bid control the release of cytochrome c from mitochondria regulating VDAC. 10)Bcl-2 family proteins are divided into two groups, proapoptotic and antiapoptotic, according to their chemical structure, that is, BH3 and BH4.11, 12) Proapoptotic and antiapoptotic proteins form heterodimers and inhibit each other's activity. [13][14][15] The dimerization is influenced by phosphorylation of the amino acid residues of the proapoptotic members, Bax, Bak, and Bik.14-17) The expression level of each Bcl-2 family protein is controlled by transcription, heterodimerization, and ubiquitination.13-26) Phosphorylation of antiapoptotic Bcl-2 family proteins inhibits the binding of these proteins and polyubiquitin. [27][28][29][30] Apoptosis is therefore deeply associated with the phosphorylation of Bcl-2 family proteins.Recently, it has been established that some growth factors induce survival signal-activating kinases such as PKA and PKB, the MAP family, ERK1/2, and AP-1. [31][32][33][34] The activation of these kinases finally results in an increase in antiapoptotic Bcl-2 expression. 29,35,36) Suppression of these kinase activities is, therefore, required for the induction of apoptosis.ROS possess both cell-impairing and cel...

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H₂O₂-induced Ca²⁺overload in NRVM involves ERK1/2 MAP kinases: role for an NHE-1-dependent pathway

Cited by 97 publications

References 42 publications

Neuroprotection by fructose-1,6-bisphosphate involves ROS alterations via p38 MAPK/ERK

Neuroprotection by fructose-1,6-bisphosphate involves ROS alterations via p38 MAPK/ERK

Mechanism of Na+/Ca2+ Exchanger Activation by Hydrogen Peroxide in Guinea-Pig Ventricular Myocytes

Reactive oxygen species (ROS) control the expression of Bcl‐2 family proteins by regulating their phosphorylation and ubiquitination

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