Effects of hydrogen peroxide on stimulatory guanine nucleotide-binding protein in rat heart.

Masuda, Hisamichi; Kaneko, Masanori; Bang, Hong Rong; Ikegaya, Takayoshi; Hayashi, Hideharu; Kobayashi, Akira; Yamazaki, Noboru

doi:10.1253/jcj.57.1007

Cited by 10 publications

(7 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Will-Shahab et al [63], Shimke et al [64], and we [62] showed that adenylate cyclase activity was depressed by oxygen free radicals. Furthermore, in the presence of oxygen free radical-generating systems, cAMP productions after stimulation with GTP, GTP + (1)-isoproterenol, Gpp(NH)p, and Gpp(NH)p + (1)-isoproterenol were reduced [62]. Therefore, it seems that the changes in [3-adrenergic receptor systems under oxidative stress may not lead to Ca 2+ overload in the heart.…”

Section: Adrenergic Receptorssupporting

confidence: 60%

“…We also examined the direct effects of hydrogen peroxide on Gs activity, and observed that hydrogen peroxide (0.1 to 10 mM) did not cause any significant effects on both Gs activity and the coupling in the 13-adrenergic receptor -Gs -adenylate cyclase system in rat cardiac membranes [62]. Will-Shahab et al [63], Shimke et al [64], and we [62] showed that adenylate cyclase activity was depressed by oxygen free radicals. Furthermore, in the presence of oxygen free radical-generating systems, cAMP productions after stimulation with GTP, GTP + (1)-isoproterenol, Gpp(NH)p, and Gpp(NH)p + (1)-isoproterenol were reduced [62].…”

Section: Adrenergic Receptorsmentioning

confidence: 69%

“…When a hydrophilic ligand, [3H]-CGP-12177, was used for the [3-adrenergic receptor assay, an increase in Kd value without any significant changes in Bmax was seen on treating the membrane with xanthine plus xanthine oxidase [61]. We also examined the direct effects of hydrogen peroxide on Gs activity, and observed that hydrogen peroxide (0.1 to 10 mM) did not cause any significant effects on both Gs activity and the coupling in the 13-adrenergic receptor -Gs -adenylate cyclase system in rat cardiac membranes [62]. Will-Shahab et al [63], Shimke et al [64], and we [62] showed that adenylate cyclase activity was depressed by oxygen free radicals.…”

Section: Adrenergic Receptorsmentioning

confidence: 95%

See 2 more Smart Citations

Oxygen free radicals and calcium homeostasis in the heart

et al. 1994

Self Cite

View full text Add to dashboard Cite

Many experiments have been done to clarify the effects of oxygen free radicals on Ca 2+ homeostasis in the hearts. A burst of oxygen free radicals occurs immediately after reperfusion, but we have to be reminded that the exact levels of oxygen free radicals in the hearts are yet unknown in both physiological and pathophysiological conditions. Therefore, we should give careful consideration to this point when we perform the experiments and analyze the results.It is, however, evident that Ca 2+ overload occurs when the hearts are exposed to an excess amount of oxygen free radicals. Though ATP-independent Ca 2+ binding is increased, Ca 2+ influx through Ca 2 § channel does not increase in the presence of oxygen free radicals. Another possible pathway through which Ca 2. can enter the myocytes is Na+-Ca 2+ exchanger. Although, the activities ofNa § + ATPase and Na+-H + exchange are inhibited by oxygen free radicals, it is not known whether intracellular Na § level increases under oxidative stress or not. The question has to be solved for the understanding of the importance of Na § Ca z+ exchange in Ca 2+ influx process from extracellular space. Another question is 'which way does Na+-Ca 2+ exchange work under oxidative stress? Net influx or efflux of Ca 2 § ?' Membrane permeability for Ca 2+ may be maintained in a relatively early phase of free radical injury. Since sarcolemmal Ca2+-pumpATPase activity is depressed by oxygen free radicals, Ca 2 § extrusion from cytosol to extracellular space is considered to be reduced. It has also been shown that oxygen free radicals promote Ca 2 § release from sarcoplasmic reticulum and inhibit Ca 2+ sequestration to sarcoplasmic reticulum. Thus, these changes in Ca 2+ handling systems could cause the Ca 2+ overload due to oxygen free radicals. (Mol Cell Biochem 139: 91-100, 1994)

show abstract

Section: Adrenergic Receptorssupporting

confidence: 60%

Section: Adrenergic Receptorsmentioning

confidence: 69%

Section: Adrenergic Receptorsmentioning

confidence: 95%

See 1 more Smart Citation

Oxygen free radicals and calcium homeostasis in the heart

et al. 1994

Self Cite

View full text Add to dashboard Cite

show abstract

“…A reduction in H 2 O 2 levels can activate adenylyl cyclase and hence elevate cAMP levels (27). Because PDTC has been shown to alter the cellular oxidative status, in part by decreasing endogenous H 2 O 2 levels (4), increased cAMP levels may initiate the observed post-translational effects of this antioxidant.…”

Section: Ebp␤ (Lane 14) But Not C/ebp␣ (Lane 13) or C/ebp␦ (Lane 15) mentioning

confidence: 99%

Antioxidant-induced Nuclear Translocation of CCAAT/Enhancer-binding Protein β

Chinery

Brockman

Dransfield

et al. 1997

Journal of Biological Chemistry

127

View full text Add to dashboard Cite

Antioxidants have been associated with a diminished risk of cancer at various anatomical sites, including the colon (1, 2). The primary mechanism of chemoprevention by antioxidants is through the reduction of DNA-damaging free radicals (3). We have reported that two antioxidants, pyrrolidinedithiocarbamate (PDTC) 1 and vitamin E, induce G 1 cell cycle arrest and apoptosis in various human cancer lines including breast, colon, and lung (4). These cell cycle perturbations were mediated by induction of p21, a powerful inhibitor of the cell cycle, through a mechanism involving activation and binding of C/ EBP␤ to the p21 promoter.C/EBP␤ is a member of a diverse group of nuclear transcription factors that contain a leucine zipper motif required for dimer formation and a basic DNA-binding domain that facilitates interactions between these factors and the regulatory domains of promoters and/or enhancers of target genes (5-11).C/EBP␤ activates several acute phase protein genes through the NF-IL6 responsive elements (8,12) and also has been implicated in adipocyte differentiation and inflammatory and immune responses (13). Thus, C/EBP␤ is a pleiotropic transactivator involved in a myriad of signal transduction and cell differentiation events.Control of C/EBP␤ expression and activity is complex and poorly understood. It is known that C/EBP␤ gene is transcriptionally activated by IL-1 and lipopolysaccharide (5), whereas in other instances its binding to cognate DNA sequences is enhanced by cytokines (5, 11). Additionally, C/EBP␤ can be a target for post-translational modification. Various kinases, including cAMP-dependent protein kinase (PKA) (14), protein kinase C (PKC) (15), a Ras-dependent MAP kinase (16), and a calcium calmodulin-dependent kinase (17) have been shown to phosphorylate C/EBP␤ in vitro. These phosphorylation events modulate DNA binding and transcriptional activity of C/EBP␤. However, it is unknown if the phosphorylation status of C/ EBP␤ influences its subcellular compartmentalization. Elevation of cAMP levels in PC-12 cells or activation of tumor necrosis factor receptors in hepatocytes leads to a redistribution of C/EBP␤ from the cytosolic to nuclear compartment (9, 18). As a first step toward understanding the antioxidant-mediated increase in C/EBP␤ DNA binding activities, we evaluated the effect of the antioxidant PDTC on the post-translational modification and subcellular localization of C/EBP␤ in DKO-1 cells, a human colorectal cancer cell line. Our results indicate that PDTC induces a rapid and sustained translocation of C/EBP␤ protein from the cytoplasm to the nucleus, resulting in induction of p21. Moreover, we demonstrate that these antioxidantmediated events are regulated by PKA-mediated phosphorylation of Ser 299 in C/EBP␤. EXPERIMENTAL PROCEDURESMaterials-DKO-1 cells were obtained from Dr. Takehiko Sasazuki (Department of Genetics, Kyushu University, Fukuoka, Japan). FLAG antibodies were purchased from Amersham, and antibodies raised against p21 and the C/EBP proteins ␣ (14AA), ␤ (C-19), and ...

show abstract

“…An important role for cyclic GMP in the butyrate-induced relaxation seems unlikely, however, in that RP-cAMPS completely abolished this effect of butyrate. It is relevant in this regard that H202 (Matsuda et al, 1993) has been shown to inhibit, rather than stimulate, adenylyl cyclase, and that butyrate and other SCFA did not increase cyclic GMP in rat caudal artery (Nutting et al, 1991).…”

Section: Discussionmentioning

confidence: 99%

Mechanism of butyrate‐induced vasorelaxation of rat mesenteric resistance artery

Aaronson

McKinnon

Poston

1996

British J Pharmacology

View full text Add to dashboard Cite

4 Sodium butyrate (50 mmol I`) caused pHi to decrease from 7.25 0.02 to 6.89 + 0.08 (n = 4, P<0.001). However, the vasorelaxant effect of butyrate on the submaximal NA contracture was not significantly modified when this fall in intracellular pH was prevented by the simultaneous application of NH4Cl. 5 Butyrate-induced relaxation was also unaffected by endothelial denudation and inhibition of NO synthase with No-nitro-L-arginine methyl ester (100 ,umol 1-'). 6 The relaxation of the NA contracture by 50 mmol I' sodium butyrate was abolished in arteries pretreated with the cyclic AMP antagonist Rp-cAMPS (25 ,mol I'). 7 We conclude that the butyrate-induced relaxation of the NA contracture is independent of intracellular acidification. The ability of Rp-cAMPS to abolish the butyrate relaxation indicates that stimulation of the cyclic AMP second messenger system may play an important role in mediating this effect.

show abstract

Effects of hydrogen peroxide on stimulatory guanine nucleotide-binding protein in rat heart.

Cited by 10 publications

References 27 publications

Oxygen free radicals and calcium homeostasis in the heart

Oxygen free radicals and calcium homeostasis in the heart

Antioxidant-induced Nuclear Translocation of CCAAT/Enhancer-binding Protein β

Mechanism of butyrate‐induced vasorelaxation of rat mesenteric resistance artery

Contact Info

Product

Resources

About