Selective Involvement Of Protein Kinase C Isozymes In Differentiation And Neoplastic Transformation

Goodnight, J; Mischak, Harald; Mushinski, J F

doi:10.1016/s0065-230x(08)60838-6

Cited by 97 publications

(82 citation statements)

References 295 publications

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“…BIOCHEMISTRYond MOLECULAR BIOLOGY INTERNATIONAL Both PKC and MAP kinase are known to affect growth and proliferation of several cell types (1)(2)(3)7,17). We, therefore, determined whether the potentiation of MAP kinase activation by the overexpression of PKC isoforms is related to the growth characteristics of cells such as maximum cell density and proliferation.…”

Section: Vol 45 No 6 1998mentioning

confidence: 99%

“…PKC comprises a large family with 11 known isoforms, each of which exhibits unique characteristics (7)(8)(9). Individual PKC isoforms are activated in different ways, are variably dependent on Ca 2 + and various membrane lipid mediators, and play distinct roles in the control of physiological functions.…”

Section: Introductionmentioning

confidence: 99%

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confidence: 99%

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Modulation of map kinase signaling and growth characteristics by the overexpression of protein kinase C in NIH3T3 cells

et al. 1998

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Summary : This study was performed to examine effects of the overexpression of protein kinase C (PKC) isoforms (i.e., 13I, [3II,7, 6,11, and ~)on mitogen-activated protein (MAP) kinase (Erk-1 and -2) signaling and growth characteristics of NIH3T3 cells. Phorbol ester (PMA) activated endogenous and ectopically expressed PKCo~, 131, 131I, 7, 6, e, and 11. Overexpression of the examined PKC isoforms enhanced PMA-induced MAP kinase activation. Potentiation of MAP kinase activation was also observed upon stimulation of cells with platelet-derived growth factor (PDGF) although there was no indication for the activation PKC isoforms by PDGF. Inhibition of PKC blocked PMA-but not PDGF-induced MAP kinase activation. Thus, potentiation of PDGF-induced MAP kinase activation appears to be independent to PKC activity, while PMA-induced MAP kinase activation requires PKC activity. The ability of PKC isoforms to potentiate MAP kinase activation is not related to the growth characteristics of cells because individual PKC isoforms differentially regulated maximum density and proliferation of cells.

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Section: Vol 45 No 6 1998mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Modulation of map kinase signaling and growth characteristics by the overexpression of protein kinase C in NIH3T3 cells

et al. 1998

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“…Protein kinase C (PKC) is a family of phospholipiddependent serine-threonine protein kinases consisting of 12 members that play important roles in signal transduction pathways that regulate growth and di erentiation, in a variety of cell types (for review see Borner and Fabbro, 1992;Goodnight et al, 1994;Jaken, 1996). Individual PKC isoforms show di erent substrate speci®cities, sub-cellular localization, cofactor requirements, and sensitivity to agonist induced down-regulation Jaken, 1996).…”

Section: Introductionmentioning

confidence: 99%

The α isoform of protein kinase C mediates phorbol ester-induced growth inhibition and p21cip1 induction in HC11 mammary epithelial cells

et al. 1999

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“…Building Abbreviations: DAG, diacylglycerol; DDRT-PCR, differential display, reverse transcription polymerase chain reaction; GAPDH, glyceraldehyde phosphate dehydrogenase; PKC, protein kinase C; TPA, 12-0-tetradecanoylphorbol-13-acetate; TRE, TPA-responsive element; SRE, serum-responsive element. differentiation, gene expression, membrane transport as well as secretion of hormones and neurotransmitters (see [1][2][3] for reviews). Initially, PKC was described as a Ca 2+-and phospholipid-dependent serine/threonine kinase [4,5], and later it was shown to be the major intracellular receptor for the tumorpromoting phorbol esters [6,7].…”

Section: Introductionmentioning

confidence: 99%

Identification of the primary growth response gene, ST2/T1, as a gene whose expression is differentially regulated by different protein kinase C isozymes

Kieser¹,

Goodnight²,

Kölch³

et al. 1995

FEBS Letters

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kbstract Individual protein kinase C isozymes have been shown Io play different roles in mediating proliferation, differentiation and transformation, but it is not known to what extent these effects involve induction of expression of particular genes. To explore the differential gene expression that might be induced by activation of different PKC isozymes, we stably transfected NIH 3T3 cells with expression vectors that encode the isozymes PKC-~, -Eli, -V, -~i, -c, -~ and -~l. Using differential display-reverse transcription-polymerase chain reaction we isolated a small eDNA that encodes a portion of the primary response gene, ST2 (also referred to as T1 or DER4), and we confirmed by RNA blot studies that ST2fYI expression is differentially regulated by PKC isozymes. ST2/TI mRNA is undetectable in the unstimulated parental NIH 3T3 cells that express only the a isozyme of PKC, but it can be induced by phorbol ester treatment. Clones that overexpress PKC-a, -5 or -e similarly do not express ST2/TI until they are stimulated with phorbol esters, which induces expression of ST2/TI with kinetics similar to wild-type NIH 3T3 but to different extents. In contrast, ST2/TI mRNA is already present in unstimulated cells that overexpress PKC-~III, -V, -~ and -~l, but phorbol ester greatly enhances ST2frl expression in these cells. These results suggest a differential role for PKC isozymes in mediating the ST2ffl expression that is induced by growth stimuli.

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Selective Involvement Of Protein Kinase C Isozymes In Differentiation And Neoplastic Transformation

Cited by 97 publications

References 295 publications

Modulation of map kinase signaling and growth characteristics by the overexpression of protein kinase C in NIH3T3 cells

Modulation of map kinase signaling and growth characteristics by the overexpression of protein kinase C in NIH3T3 cells

The α isoform of protein kinase C mediates phorbol ester-induced growth inhibition and p21cip1 induction in HC11 mammary epithelial cells

Identification of the primary growth response gene, ST2/T1, as a gene whose expression is differentially regulated by different protein kinase C isozymes

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