Characterization of phorbol esters activity on individual mammalian protein kinase C isoforms, using the yeast phenotypic assay

We have isolated and characterized a new human cDNA, coding for a protein kinase, related to the protein kinase C (PKC) gene family. Although this protein kinase shares some homologous sequences and structural features with the four members of the PKC family initially isolated (alpha, beta I, beta II, and gamma), it shows more homology with the recently described PKC-related subfamily, encoded by the cDNAs delta, epsilon, and zeta. The transcript for this gene product, termed PKC-L, is most abundant in lung tissue, less expressed in heart and skin tissue, and exhibited very low expression in brain tissue. Thus, its tissue distribution is different from that described for other mammalian members of the PKC gene family, their expression being enriched in brain tissues. PKC-L is also expressed in several human cell lines, including the human epidermoid carcinoma line A431. The ability of phorbol esters to bind to and stimulate the kinase activity of PKC-L was revealed by introducing the cDNA into COS cells.

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Characterization of the yeast BMH1 gene encoding a putative protein homologous to mammalian protein kinase II activators and protein kinase C inhibitors

FEBS Letters ◽

10.1016/0014-5793(92)80426-h ◽

1992 ◽

Vol 302 (2) ◽

pp. 145-150 ◽

Cited By ~ 86

Author(s):

G.Paul H. van Heusden ◽

Thibaut J. Wenzel ◽

Ellen L. Lagendijk ◽

H.Y. de Steensma ◽

Johan A. van den Berg

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Gene Encoding ◽

Protein Kinase C Inhibitors ◽

Putative Protein ◽

Kinase C ◽

Protein Kinase Ii ◽

Mammalian Protein

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Characterization of protein kinase C isoforms in primary cultured cerebellar granule cells

Brain Research ◽

10.1016/j.brainres.2006.01.110 ◽

2006 ◽

Vol 1083 (1) ◽

pp. 70-84 ◽

Cited By ~ 9

Author(s):

R. Lisa Popp ◽

Oscar Velasquez ◽

Jason Bland ◽

Peter Hughes

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Granule Cells ◽

Cerebellar Granule Cells ◽

Cerebellar Granule ◽

Kinase C ◽

Protein Kinase C Isoforms

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A growth factor-repressible gene associated with protein kinase C-mediated inhibition of adipocyte differentiation.

The Journal of Cell Biology ◽

10.1083/jcb.107.1.279 ◽

1988 ◽

Vol 107 (1) ◽

pp. 279-286 ◽

Cited By ~ 40

Author(s):

M Navre ◽

G M Ringold

Keyword(s):

Protein Kinase C ◽

Growth Factor ◽

Protein Kinase ◽

Fibroblast Growth Factor ◽

Basic Fibroblast Growth Factor ◽

Phorbol Esters ◽

Adipocyte Differentiation ◽

Fibroblast Growth ◽

Kinase C

The conversion of determined adipoblasts to fully differentiated adipocytes requires appropriate environmental conditions. A strict dependence on cell confluence and a facilitation by glucocorticoid hormones have previously been described. We have found that agents that are capable of activating protein kinase C, such as basic fibroblast growth factor and phorbol esters, inhibit the differentiation of the adipogenic cell line TA1 without stimulating cell growth. Here we describe the sequence and characterization of a cDNA (clone 5) that detects an RNA, the expression of which is enhanced by glucocorticoids and increasing cell density. In contrast, activators of protein kinase C including basic fibroblast growth factor, phorbol esters, and synthetic diacylglycerols inhibit clone 5 gene expression. It appears that clone 5 expression is closely linked to environmental and hormonal factors that promote the differentiation of adipogenic cells.

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Stimulation of human B lymphocytes by phorbol esters reported to be selective in the protein kinase C isoforms they activate

Molecular Immunology ◽

10.1016/0161-5890(94)90176-7 ◽

1994 ◽

Vol 31 (9) ◽

pp. 671-674 ◽

Cited By ~ 8

Author(s):

Ian MacDonald ◽

Kirstine A. Knox ◽

John Gordon

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

B Lymphocytes ◽

Phorbol Esters ◽

Kinase C ◽

Protein Kinase C Isoforms ◽

Stimulation Of

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Expression of mammalian protein kinase C in Schizosaccharomyces pombe: isotype-specific induction of growth arrest, vesicle formation, and endocytosis.

Molecular Biology of the Cell ◽

10.1091/mbc.5.8.907 ◽

1994 ◽

Vol 5 (8) ◽

pp. 907-920 ◽

Cited By ~ 20

Author(s):

N T Goode ◽

M A Hajibagheri ◽

G Warren ◽

P J Parker

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Growth Inhibition ◽

Schizosaccharomyces Pombe ◽

Phorbol Ester ◽

Phorbol Esters ◽

Vesicle Formation ◽

Vesicular Traffic ◽

Kinase C ◽

Mammalian Protein

Mammalian protein kinase C (PKC) isotypes elicit a number of effects on expression in Schizosaccharomyces pombe. A small decrease in growth rate results from PKC-gamma expression, and treatment of these cells with phorbol esters leads to marked growth inhibition and vesicle formation. PKC-delta and -eta expression causes growth inhibition and vesiculation, and the magnitude of both of these effects is increased by phorbol esters. In contrast, PKC-epsilon expression produces growth inhibition but no vesicle accumulation, and this effect is not responsive to phorbol ester. Finally, PKC-zeta has no observable effect. Thus, isotype-specific biological effects are observed. The accumulation of vesicles correlates with phorbol ester-dependent growth inhibition and occurs only with expression of those isotypes that down-regulate in response to phorbol esters in these cells. Antibodies against mammalian clathrin light chain 1a identified clathrin-coated vesicles and up-regulation of clathrin expression in those cells where vesicles accumulate; the increased vesicular traffic includes an element of endocytosis. Thus expression of specific mammalian PKC isotypes up-regulates endocytosis in S. pombe, providing a likely explanation for PKC-mediated receptor internalization in higher eukaryotes.

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