Retention of specific protein kinase C isozymes following chronic phorbol ester treatment in BC3H-1 myocytes

Cooper, Denise R.; Watson, James; Acevedo‐Duncan, Mildred; Pollet, Robert J.; Standaert, Mary L.; Farese, Robert V.

doi:10.1016/0006-291x(89)91600-8

Cited by 56 publications

(22 citation statements)

References 25 publications

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“…This is consistent with the observations that TPA potentiates the action of NGF in PC12 cells (Burstein et al, 1982) but appears inconsistent with the reports that NGF (and bFGF) can elicit neurite outgrowth in PC12 cells in which PKC has been down-regulated by prolonged treatment with TPA (Reinhold and Neet, 1989;Damon et al, 1990;Sigmund et al, 1990). However, down-regulating PKC in this manner may not be a totally effective means of eliminating all PKC isozymes (Cooper et al, 1989 (Curran and Morgan, 1985;Milbrandt, 1986). The fos antibodies used in the present study have been found to immunoprecipitate c-fos and possibly the fos-related antigen, fra-1 (Riabowol et al, 1988b;Vosatka et al, 1989;Riabowol, unpublished observations).…”

Section: Effect Of Fos Antibodies On Numbers Of Round Cells and Cell mentioning

confidence: 59%

Testing the in vivo role of protein kinase C and c-fos in neurite outgrowth by microinjection of antibodies into PC12 cells.

Altin

Wetts

Riabowol

et al. 1992

MBoC

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To define the molecular bases of growth factor-induced signal transduction pathways, antibodies known to block the activity of either protein kinase C (PKC) or the fos protein were introduced into PC12 cells by microinjection. The antibody against PKC significantly inhibited neurite outgrowth when scored 24 h after microinjection and exposure to nerve growth factor (NGF). Microinjection of antibodies to fos significantly increased the percentage of neurite-bearing cells after exposure to either NGF or basic fibroblast growth factor (bFGF) but inhibited the stimulation of DNA synthesis by serum, suggesting that in PC12 cells, fos is involved in cellular proliferation. Thus, activation of PKC is involved in the induction of neurite outgrowth by NGF, but expression of the fos protein, which is induced by both NGF and bFGF, is not necessary and inhibits neurite outgrowth.

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Section: Effect Of Fos Antibodies On Numbers Of Round Cells and Cell mentioning

confidence: 59%

Testing the in vivo role of protein kinase C and c-fos in neurite outgrowth by microinjection of antibodies into PC12 cells.

Altin

Wetts

Riabowol

et al. 1992

MBoC

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“…An explanation for this discrep¬ ancy may lie in the recent findings that multiple forms of PKC exist (for review see Huang, Huang, Nakabayashi & Yoshida, 1989) and that these forms may have different functions in cellular signalling and be regulated by different mechanisms. Only a portion of PKC isoforms is 'down-regulated' by TPA treatment (Cooper, Watson, Acevedo-Duncan et al 1989;Fournier, Hardy, Clark & Murray, 1989). Clearly, these down-regulated forms seem not to be required for c-fos induction by GH in mouse osteoblasts.…”

Section: Gh Induces Formation Of Diacylglycerol In Mouse Osteoblastsmentioning

confidence: 98%

Growth hormone induces expression of c-jun and jun B oncogenes and employs a protein kinase C signal transduction pathway for the induction of c-fos oncogene expression

Slootweg

Groot²,

Herrmann‐Erlee³

et al. 1991

Journal of Molecular Endocrinology

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Although the structure of several members of the GH receptor family has been defined, signal transduction following GH binding to its receptor has not been elucidated. Mouse osteoblasts were used to study the effect of GH on immediate early gene expression and, subsequently, the cellular signal(s) mediating this expression were analysed. GH rapidly and transiently induced the expression of c-jun and jun B in concert with the already reported expression of c-fos. The GH-induced expression of c-fos was completely blocked by the protein kinase inhibitors staurosporine and H7, indicating that the action of GH is mediated by one or several protein kinases. We next analysed the identity of the putative protein kinases in more detail by using a more specific protein kinase inhibitor, namely the ether-lipid 1-O-alkyl-2-O-methylglycerol, understood to be an inhibitor of protein kinase C (PKC). Data obtained from these studies revealed that GH-induced expression of c-fos is mediated by PKC. In addition, we observed a profound increase in formation of the PKC activator diacyglycerol upon addition of GH, a natural activator of PKC. In conclusion, upon binding of GH to mouse osteoblasts, the receptor-mediated cellular signal involves diacyglycerol formation and activation of PKC, leading to the induction of oncogene expression. Finally, the expression of c-fos, c-jun and jun B results in an increased binding of protein complexes to AP-1 binding sites.

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“…It is now apparent that pretreatment with phorbol esters results in selective isozyme depletion, and even partial retention of PKC activity is sufficient to evoke an agonist effect in other systems (32,33). A similar situation may occur in anterior pituitaries.…”

Section: Discussionmentioning

confidence: 83%

Calcium mobilization is a prerequisite for the expression of phorbol ester-stimulated luteinizing hormone secretion from pituitaries of male and acutely ovariectomized rats

Das

Fahmy²,

Bourne³

1994

European Journal of Endocrinology

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Ionomycin, which mobilizes Ca2+, and phorbol 12-myristate 13-acetate (PMA), which activates protein kinase C (PKC), were used to compare the effects/interactions of Ca2+ and PKC on luteinizing hormone (LH) secretion from pituitaries of intact male and acutely ovariectomized (72 h) rats. Quartered pituitaries from donor animals were perifused at 0.25 ml/min and sequential effluent fractions were collected every 10 min. Continuous administration (4 h) of 1 nmol of gonadotropin-releasing hormone (GnRH) resulted in an increase in LH secretion. Cycloheximide (5 mumol) dissociated the GnRH-stimulated LH responses into protein synthesis-independent and -dependent components. While ionomycin (10 mumol) stimulated LH secretion from pituitaries of both sexes by protein synthesis-independent mechanisms, PMA (1 mumol) and the inactive phorbol ester, 4 alpha-phorbol 12,13-didecanoate (PDD), were ineffective secretagogues. However, PMA (but not PDD) interacted synergistically with ionomycin and GnRH to augment LH secretion by protein synthesis-dependent mechanisms. These results suggest a similarity in the effects/interactions of Ca2+ and PKC in gonadotropes from male and ovariectomized rats. If the effects of PMA can be attributed to PKC activation, then it also appears that Ca2+ mobilization is necessary for the manifestation of PKC as a mediator of LH secretion from these gonadotropes. While PKC activity can be divorced from the protein synthesis-independent component of LH release (this component appears to be mediated by Ca2+ mobilization), the enzyme might be involved in amplifying the response to Ca2+ mobilization through synergistic protein synthesis-dependent mechanisms.

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Retention of specific protein kinase C isozymes following chronic phorbol ester treatment in BC3H-1 myocytes

Cited by 56 publications

References 25 publications

Testing the in vivo role of protein kinase C and c-fos in neurite outgrowth by microinjection of antibodies into PC12 cells.

Testing the in vivo role of protein kinase C and c-fos in neurite outgrowth by microinjection of antibodies into PC12 cells.

Growth hormone induces expression of c-jun and jun B oncogenes and employs a protein kinase C signal transduction pathway for the induction of c-fos oncogene expression

Calcium mobilization is a prerequisite for the expression of phorbol ester-stimulated luteinizing hormone secretion from pituitaries of male and acutely ovariectomized rats

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