Induction of the c-jun proto-oncogene by a protein kinase c-dependent mechanism during exposure of human epidermal keratinocytes to ethanol

Kharbanda, Surender; Nakamura, Takashi; Küfe, Donald

doi:10.1016/0006-2952(93)90142-j

Cited by 38 publications

(24 citation statements)

References 28 publications

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“…These data suggest an isozyme-specific role for PKC in producing ethanol's longterm cardioprotective effect against ischemia-reperfusion injury. This observation is consistent with recent studies in other cell types demonstrating ethanol-induced activation of PKC (40)(41)(42)(43)(44).…”

Section: Discussionsupporting

confidence: 93%

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Activation of ɛ protein kinase C correlates with a cardioprotective effect of regular ethanol consumption

Miyamae

Rodriguez

Camacho

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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Section: Discussionsupporting

confidence: 93%

“…Such sustained translocation was proposed to occur by Downey and coworkers (59). Ethanol-induced activation of PKC has been observed in other cell types (40)(41)(42)(43)(44). For example, in neural crest-derived PC12 cells, ethanol-induced activation of PKC enhances nerve growth factor-induced signaling and neurite outgrowth (40).…”

Section: Discussionmentioning

confidence: 99%

Activation of ɛ protein kinase C correlates with a cardioprotective effect of regular ethanol consumption

Miyamae

Rodriguez

Camacho

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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“…PKC activity is also increased in human platelets (10), lymphocytes (11), and epidermal keratinocytes (12) after acute ethanol exposure. Moreover, ethanol causes translocation of PKC activity from cytosolic to membrane fractions in astroglial cells (13), human lymphocytes (11), and epidermal keratinocytes (12).…”

mentioning

confidence: 99%

Ethanol Alters the Subcellular Localization of δ- and ε Protein Kinase C in NG108–15 Cells

Gordon

Yao

et al. 1997

Mol Pharmacol

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SUMMARYProtein kinase C (PKC) has been shown to regulate the ethanol sensitivity of membrane-bound receptors and transporters, but little is known about the molecular mechanisms underlying this regulation. PKC is a family of isozymes that translocate to new intracellular sites on activation. Here we present immunochemical data showing that ethanol causes translocation of ␦-and ⑀-PKC to new intracellular sites. Ethanol causes translocation of ␦-PKC from the Golgi to the perinucleus; this translocation is similar to that induced by activation of PKC with phorbol esters.In contrast, ⑀-PKC translocation caused by ethanol is different from that induced by phorbol esters; ethanol causes translocation of ⑀-PKC from the perinucleus to the cytoplasm, whereas phorbol ester activation causes translocation of ⑀-PKC to the nucleus. Because the substrate specificity of these kinases is determined by their site of localization, ethanol-induced translocation of ␦-and ⑀-PKC to new intracellular sites may explain some of the pleiotropic effects of ethanol on cellular functions.PKC, a family of isozymes that mediates multiple cellular functions, has been shown to regulate the effects of ethanol on receptors (1-6) and membrane-bound transporters (7), but the mechanism underlying this regulation is unknown. Ethanol alters the amount, activity, and subcellular distribution of PKC. Increased amounts of ␣-, ␦-, and ⑀-PKC in NG108 -15 cells (8) and of ␦-and ⑀-PKC in PC12 cells (9) are found after chronic ethanol exposure, and there is increased activity of PKC in NG108 -15 and PC12 cells (9). PKC activity is also increased in human platelets (10), lymphocytes (11), and epidermal keratinocytes (12) after acute ethanol exposure. Moreover, ethanol causes translocation of PKC activity from cytosolic to membrane fractions in astroglial cells (13), human lymphocytes (11), and epidermal keratinocytes (12).On activation, each PKC isozyme translocates from a specific intracellular site to another (14). Recent evidence suggests that the specificity of substrate phosphorylation of each isozyme is determined by its localization (14). Ethanol-induced activation and translocation of specific PKC isozymes to new intracellular sites could therefore account for many of the pleiotropic effects of ethanol on cell functions. To test this hypothesis, we carried out studies on the localization of ␦-and ⑀-PKC in NG108 -15 neuroblastoma ϫ glioma hybrid cells. We report here that ethanol causes translocation of ␦-and ⑀-PKC to new intracellular sites in these cells. Materials and MethodsCell culture. NG108-15 neuroblastoma ϫ glioma hybrid cells were seeded in single-chamber slides in defined media consisting of Dulbecco's modified Eagle's medium/Ham's F-12 medium (3:1); 0.1 mM hypoxanthine; 1.0 M aminopterin; 12 mM thymidine; 25 mM HEPES, pH 7.4; trace elements (0.5 nM MnCl 2 , 0.5 nM [NH 4 ] 6 Mo 7 O 24 , 0.25 nM SnCl 4 , 25 nM Na 3 VO 4 , 5 nM CdSO 4 , 0.25 nM NiSO 4 , 15 nM H 2 SeO 3 , 25 nM Na 2 SiO 3 ); bovine insulin (5 g/ml); human transferrin (50 g/ml);...

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“…Alcohol may initiate and promote oncogenes (44). Acetaldehyde, a product of a1cohol metabolism, may impair the repair ofDNA, increasing the chance that mutations will lead to cancer (45).…”

Section: Ii) Cancer Ascertainment In Cohort Studiesmentioning

confidence: 99%

Malignancy in Systemic Lupus Erythematosus

Egiziano

Clarke

Ramsey‐Goldman

et al. 2016

Curr Treat Options in Rheum

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Induction of the c-jun proto-oncogene by a protein kinase c-dependent mechanism during exposure of human epidermal keratinocytes to ethanol

Cited by 38 publications

References 28 publications

Activation of ɛ protein kinase C correlates with a cardioprotective effect of regular ethanol consumption

Activation of ɛ protein kinase C correlates with a cardioprotective effect of regular ethanol consumption

Ethanol Alters the Subcellular Localization of δ- and ε Protein Kinase C in NG108–15 Cells

Malignancy in Systemic Lupus Erythematosus

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