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Article: Protein kinase C isoenzymes: divergence in signal transduction?

Hug, H / Sarre, T F

1993 Volume 291 Pt 2, Page(s) 329–343

MeSH term(s)	Amino Acid Sequence ; Animals ; Gene Expression ; Humans ; Isoenzymes/chemistry ; Isoenzymes/genetics ; Isoenzymes/physiology ; Molecular Sequence Data ; Protein Kinase C/chemistry ; Protein Kinase C/genetics ; Protein Kinase C/physiology ; Signal Transduction/physiology
Chemical Substances	Isoenzymes ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	1993-04-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2969-5
ISSN	1470-8728 ; 0264-6021 ; 0006-2936 ; 0306-3275
ISSN (online)	1470-8728
ISSN	0264-6021 ; 0006-2936 ; 0306-3275
DOI	10.1042/bj2910329
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Article ; Online: Opposing growth regulatory roles of protein kinase D isoforms in human keratinocytes.

Ryvkin, Vladislav / Rashel, Mohammad / Gaddapara, Trivikram / Ghazizadeh, Soosan

The Journal of biological chemistry

2015 Volume 290, Issue 17, Page(s) 11199–11208

Abstract: ... the importance and complexity of PKD signaling in human epidermis and suggest a central role for PKD3 signaling ... a divergence in the expression and function of other PKD isoforms. Contrary to mouse KCs, treatment of cultured ... PKD is a family of three serine/threonine kinases (PKD-1, -2, and -3) involved in the regulation ...

Abstract	PKD is a family of three serine/threonine kinases (PKD-1, -2, and -3) involved in the regulation of diverse biological processes including proliferation, migration, secretion, and cell survival. We have previously shown that despite expression of all three isoforms in mouse epidermis, PKD1 plays a unique and critical role in wound healing, phorbol ester-induced hyperplasia, and tumor development. In translating our findings to the human, we discovered that PKD1 is not expressed in human keratinocytes (KCs) and there is a divergence in the expression and function of other PKD isoforms. Contrary to mouse KCs, treatment of cultured human KCs with pharmacological inhibitors of PKDs resulted in growth arrest. We found that PKD2 and PKD3 are expressed differentially in proliferating and differentiating human KCs, with the former uniformly present in both compartments whereas the latter is predominantly expressed in the proliferating compartment. Knockdown of individual PKD isoforms in human KCs revealed contrasting growth regulatory roles for PKD2 and PKD3. Loss of PKD2 enhanced KC proliferative potential while loss of PKD3 resulted in a progressive proliferation defect, loss of clonogenicity and diminished tissue regenerative ability. This proliferation defect was correlated with up-regulation of CDK4/6 inhibitor p15(INK4B) and induction of a p53-independent G1 cell cycle arrest. Simultaneous silencing of PKD isoforms resulted in a more pronounced proliferation defect consistent with a predominant role for PKD3 in proliferating KCs. These data underline the importance and complexity of PKD signaling in human epidermis and suggest a central role for PKD3 signaling in maintaining human epidermal homeostasis.
MeSH term(s)	3T3 Cells ; Animals ; Cell Differentiation/physiology ; Cyclin-Dependent Kinase Inhibitor p15/biosynthesis ; Cyclin-Dependent Kinase Inhibitor p15/genetics ; Epidermal Cells ; Epidermis/enzymology ; G1 Phase Cell Cycle Checkpoints/physiology ; Humans ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Keratinocytes/cytology ; Keratinocytes/enzymology ; Mice ; Protein Kinase C/genetics ; Protein Kinase C/metabolism ; Signal Transduction/physiology ; Species Specificity ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism ; Up-Regulation/physiology ; Wound Healing/physiology
Chemical Substances	CDKN2B protein, human ; Cyclin-Dependent Kinase Inhibitor p15 ; Isoenzymes ; TP53 protein, human ; Tumor Suppressor Protein p53 ; protein kinase D (EC 2.7.10.-) ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2015-03-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M115.643742
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Article: Protein kinase C lambda/iota (PKClambda/iota): a PKC isotype essential for the development of multicellular organisms.

Suzuki, Atsushi / Akimoto, Kazunori / Ohno, Shigeo

Journal of biochemistry

2003 Volume 133, Issue 1, Page(s) 9–16

Abstract: ... regulatory domain has additional aPKC-specific structural motifs involved in various protein-protein ... terminal regulatory domain but also in the kinase domain. Although one of the most distinct features ... with PKCzeta based on its sequence divergence from conventional and novel PKCs observed not only in the N ...

Abstract	PKClambda/iota belongs to the third group of the PKC family, atypical PKC (aPKC), together with PKCzeta based on its sequence divergence from conventional and novel PKCs observed not only in the N-terminal regulatory domain but also in the kinase domain. Although one of the most distinct features of aPKC is its single, unrepeated cysteine-rich domain, recent studies have revealed that the N-terminal regulatory domain has additional aPKC-specific structural motifs involved in various protein-protein interactions, which are important for the regulation and the subcellular targeting of aPKC. The identification of aPKC-specific binding proteins has significantly facilitated our understanding of the activation mechanism as well as the physiological function of aPKC at the molecular level. In particular, the finding that the mammalian homologs of the Caenorhabditis elegans proteins, PAR-3 and PAR-6, bind aPKC unexpectedly opens a new avenue for exploring a thus far completely unrecognized critical function of aPKC, that is, as a component of an evolutionarily conserved cell polarity machinery. Together with the great progress in the genome project as well as in the genetic analysis of model organisms, these advances are leading us into the new era of aPKC study in which functional divergence between PKClambda/iota and zeta can be discussed in elaborately.
MeSH term(s)	Animals ; Biological Evolution ; Cell Polarity ; Epithelium/enzymology ; Humans ; Isoenzymes/chemistry ; Isoenzymes/metabolism ; Isoenzymes/physiology ; Mice ; Protein Kinase C/chemistry ; Protein Kinase C/metabolism ; Protein Kinase C/physiology ; Protein Structure, Tertiary ; Signal Transduction
Chemical Substances	Isoenzymes ; protein kinase C zeta (EC 2.7.11.1) ; PKC-3 protein (EC 2.7.11.13) ; Protein Kinase C (EC 2.7.11.13) ; protein kinase C lambda (EC 2.7.11.13)
Language	English
Publishing date	2003-05-16
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	218073-x
ISSN	1756-2651 ; 0021-924X
ISSN (online)	1756-2651
ISSN	0021-924X
DOI	10.1093/jb/mvg018
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Article: Activation of protein kinase C subtypes alpha, gamma, delta, epsilon, zeta, and eta by tumor-promoting and nontumor-promoting agents.

Geiges, D / Meyer, T / Marte, B / Vanek, M / Weissgerber, G / Stabel, S / Pfeilschifter, J / Fabbro, D / Huwiler, A

Biochemical pharmacology

1997 Volume 53, Issue 6, Page(s) 865–875

Abstract: Protein kinase C (PKC) subtypes alpha, gamma, delta, epsilon, zeta, and eta have been expressed ... a divergence of individual PKC subtypes in signal transduction. ... promoting agents, as well as their inhibition of kinase activity by staurosporine and two related compounds ...

Abstract	Protein kinase C (PKC) subtypes alpha, gamma, delta, epsilon, zeta, and eta have been expressed using the baculovirus expression system. The partially purified PKC subtypes have been studied for their substrate specificities and phospholipid-independent activation by various chemically different nontumor- and tumor-promoting agents, as well as their inhibition of kinase activity by staurosporine and two related compounds. An endogenous PKC-like kinase activity of Sf9 cells was detected and analyzed for cofactor requirements and inhibition. Protamine sulfate was most efficiently phosphorylated by all of the PKC subtypes tested, although this phosphorylation was independent of phosphatidylserine (PS) and diacylglycerol (DAG) or 12-O-tetradecanoylphorbol 13-acetate (TPA). Except for PKC-zeta, all subtypes tested phosphorylated myelin basic protein (MBP), histone, or a peptide derived from the pseudosubstrate region of PKC-alpha in a PS/DAG-dependent manner but to varying extents. Among the various agents tested, TPA most efficiently stimulated the kinase activities of the PKC subtypes in a phospholipid-dependent manner. Phorbol 12,13-dibutyrate (PDBu) was less effective than TPA but displayed no major difference among the subtypes. Activation of PKC-alpha by bryostatin-1 reached only half of the TPA response whereas the other subtypes were activated more effectively. The weak tumor promoter resiniferonol 9,13,14-orthophenyl acetate (ROPA) mainly stimulated PKC-alpha and PKC-gamma at 1 microM concentration, whereas PKC-epsilon and PKC-eta were much less activated. Sapintoxin D, mezerein, indolactam V, and resiniferatoxin at concentrations of 1-100 nM preferentially activated PKC-alpha in a DAG-like manner, whereas at 1 microM other subtypes were activated as well. Preferential activation of PKC-alpha was also noted for tinyatoxin and thapsigargin, but their mode of activation is unclear because these two compounds did not compete for the phorbol ester binding of the PKC subtypes as the other agents did. Of the three PKC inhibitors tested, staurosporine most efficiently inhibited kinase activity of the PKC subtypes, whereas K252a and CGP 41251 were at least 10 times less effective. However, K252a showed certain specificity for inhibition of PKC-alpha, and CGP 41251 failed to inhibit PKC-epsilon and PKC-zeta. Given the different substrate specificities and modes of activation by various tumor-promoting and nontumor-promoting agents, as well as the different sensitivities towards different inhibitors, our results indicate a divergence of individual PKC subtypes in signal transduction.
MeSH term(s)	Animals ; Carcinogens/pharmacology ; Enzyme Activation ; Isoenzymes/drug effects ; Phosphorylation ; Protein Kinase C/antagonists & inhibitors ; Protein Kinase C/drug effects ; Protein Kinase C/metabolism ; Spodoptera ; Staurosporine/pharmacology ; Substrate Specificity
Chemical Substances	Carcinogens ; Isoenzymes ; Protein Kinase C (EC 2.7.11.13) ; Staurosporine (H88EPA0A3N)
Language	English
Publishing date	1997-03-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	208787-x
ISSN	1873-2968 ; 0006-2952
ISSN (online)	1873-2968
ISSN	0006-2952
DOI	10.1016/s0006-2952(96)00885-4
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Article: Divergence in the anti-apoptotic signalling pathways used by nerve growth factor and basic fibroblast growth factor (bFGF) in PC12 cells: rescue by bFGF involves protein kinase C delta.

Wert, M M / Palfrey, H C

The Biochemical journal

2000 Volume 352 Pt 1, Page(s) 175–182

Abstract: ... protein kinase C (PKC) inhibitors such as bisindoylmaleimide-I and Gö 6983 suggested that PKC delta is a likely ... strongly activated mitogen-activated protein (MAP) kinases, but blockade of signalling through this pathway ... signal was not mediated by the MAP kinase cascade, as bFGF activation of this pathway was not affected ...

Abstract	The mechanisms whereby nerve growth factor (NGF) and basic fibroblast growth factor (bFGF) block apoptosis in serum-deprived PC12 cells were investigated. NGF, but not bFGF, strongly activated Akt/protein kinase B, a downstream effector of phosphoinositide (phosphatidylinositol) 3-kinase (PI 3-kinase). In addition, inhibition of PI 3-kinase by LY294002 partially blocked inhibition of apoptosis by NGF, but not that by bFGF, suggesting divergence in NGF and bFGF anti-apoptotic signalling pathways. Both growth factors strongly activated mitogen-activated protein (MAP) kinases, but blockade of signalling through this pathway, either by the expression of dominant-negative Ras or by treatment with the MAP kinase/ERK kinase (MEK) inhibitor U0126, partially inhibited only bFGF, but not NGF, anti-apoptotic signalling. Use of isoform-specific protein kinase C (PKC) inhibitors such as bisindoylmaleimide-I and Gö 6983 suggested that PKC delta is a likely component of bFGF trophic signalling. A role for PKC delta was confirmed in PC12 cells expressing a dominant-negative PKCdelta fragment, in which reversal of apoptosis by bFGF was partially blocked. The PKC delta signal was not mediated by the MAP kinase cascade, as bFGF activation of this pathway was not affected in cells expressing the dominant-negative PKC delta fragment. Full inhibition of bFGF anti-apoptotic signalling occurred when both the PKCdelta and Ras/MAP kinase pathways were inhibited. Together, these data demonstrate that inhibition of apoptosis by bFGF in PC12 cells operates differently from that mediated by NGF, requiring the addition of signals from both the Ras/MAP kinase and PKC signalling pathways.
MeSH term(s)	Acetophenones/pharmacology ; Animals ; Apoptosis ; Benzopyrans/pharmacology ; Butadienes/pharmacology ; Cell Nucleus/metabolism ; Cell Survival/drug effects ; Chromones/pharmacology ; Culture Media, Serum-Free/metabolism ; Dose-Response Relationship, Drug ; Down-Regulation ; Enzyme Inhibitors/pharmacology ; Fibroblast Growth Factor 2/metabolism ; Genes, Dominant ; Immunoblotting ; Indoles/pharmacology ; Isoenzymes/chemistry ; Isoenzymes/genetics ; Isoenzymes/metabolism ; MAP Kinase Signaling System ; Maleimides/pharmacology ; Mitogen-Activated Protein Kinases/metabolism ; Morpholines/pharmacology ; Nerve Growth Factor/metabolism ; Nitriles/pharmacology ; PC12 Cells ; Phosphatidylinositol 3-Kinases/metabolism ; Protein Isoforms ; Protein Kinase C/chemistry ; Protein Kinase C/genetics ; Protein Kinase C/metabolism ; Protein Kinase C-delta ; Protein-Serine-Threonine Kinases ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; Rats ; Signal Transduction ; Time Factors ; ras Proteins/metabolism
Chemical Substances	Acetophenones ; Benzopyrans ; Butadienes ; Chromones ; Culture Media, Serum-Free ; Enzyme Inhibitors ; Indoles ; Isoenzymes ; Maleimides ; Morpholines ; Nitriles ; Protein Isoforms ; Proto-Oncogene Proteins ; U 0126 ; Fibroblast Growth Factor 2 (103107-01-3) ; 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (31M2U1DVID) ; Nerve Growth Factor (9061-61-4) ; rottlerin (E29LP3ZMUH) ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Prkcd protein, rat (EC 2.7.1.-) ; Akt1 protein, rat (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Protein Kinase C (EC 2.7.11.13) ; Protein Kinase C-delta (EC 2.7.11.13) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; ras Proteins (EC 3.6.5.2)
Language	English
Publishing date	2000-11-15
Publishing country	England
Document type	Journal Article
ZDB-ID	2969-5
ISSN	1470-8728 ; 0264-6021 ; 0006-2936 ; 0306-3275
ISSN (online)	1470-8728
ISSN	0264-6021 ; 0006-2936 ; 0306-3275
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Article ; Online: PHLPP1 splice variants differentially regulate AKT and PKCα signaling in hippocampal neurons: characterization of PHLPP proteins in the adult hippocampus.

Jackson, Travis C / Verrier, Jonathan D / Semple-Rowland, Susan / Kumar, Ashok / Foster, Thomas C

Journal of neurochemistry

2010 Volume 115, Issue 4, Page(s) 941–955

Abstract: ... limited. In this study, we characterized PHLPP protein expression and target kinases in the adult ... of potent protein kinase B (AKT) inhibitors that have been intensely investigated in relation to AKT ... development, constituting the most abundant PHLPP protein in adult neurons. Further, while all PHLPP proteins ...

Abstract	Pleckstrin homology and leucine rich repeat protein phosphatases (PHLPPs) are a novel class of potent protein kinase B (AKT) inhibitors that have been intensely investigated in relation to AKT activity in cancer. Currently, our understanding of the role of PHLPP1α in the central nervous system is limited. In this study, we characterized PHLPP protein expression and target kinases in the adult hippocampus. We directly verify PHLPP1α inhibits AKT in hippocampal neurons and demonstrate a novel role for PHLPP1β/SCOP, to promote AKT activation. PHLPP1α expression changes dramatically in the hippocampus during development, constituting the most abundant PHLPP protein in adult neurons. Further, while all PHLPP proteins could be observed in the cytosolic fraction, only PHLPP1α could be localized to the nucleus. The results provide unique evidence for a divergence in the function of PHLPP1α and PHLPP1β/SCOP, and suggest that PHLPP1α plays a major role in regulating AKT signaling in neurons.
MeSH term(s)	Aging/genetics ; Aging/physiology ; Animals ; Cell Line ; Cells, Cultured ; Female ; Hippocampus/embryology ; Hippocampus/enzymology ; Hippocampus/physiology ; Humans ; Isoenzymes/genetics ; Isoenzymes/physiology ; Male ; Neurons/enzymology ; Neurons/metabolism ; Neurons/physiology ; Nuclear Proteins/genetics ; Nuclear Proteins/physiology ; Phosphoprotein Phosphatases/genetics ; Phosphoprotein Phosphatases/physiology ; Protein Kinase C-alpha/metabolism ; Protein Kinase C-alpha/physiology ; Proto-Oncogene Proteins c-akt/antagonists & inhibitors ; Proto-Oncogene Proteins c-akt/metabolism ; Proto-Oncogene Proteins c-akt/physiology ; RNA Splicing/physiology ; Rats ; Rats, Inbred BN ; Rats, Inbred F344 ; Signal Transduction/genetics
Chemical Substances	Isoenzymes ; Nuclear Proteins ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Protein Kinase C-alpha (EC 2.7.11.13) ; PHLPP1 protein, rat (EC 3.1.3.16) ; Phosphoprotein Phosphatases (EC 3.1.3.16)
Language	English
Publishing date	2010-09-28
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80158-6
ISSN	1471-4159 ; 0022-3042 ; 1474-1644
ISSN (online)	1471-4159
ISSN	0022-3042 ; 1474-1644
DOI	10.1111/j.1471-4159.2010.06984.x
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Article: Protein kinase C isoenzymes: divergence in signal transduction?

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Article ; Online: Opposing growth regulatory roles of protein kinase D isoforms in human keratinocytes.

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Article: Protein kinase C lambda/iota (PKClambda/iota): a PKC isotype essential for the development of multicellular organisms.

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Article: Activation of protein kinase C subtypes alpha, gamma, delta, epsilon, zeta, and eta by tumor-promoting and nontumor-promoting agents.

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Article: Divergence in the anti-apoptotic signalling pathways used by nerve growth factor and basic fibroblast growth factor (bFGF) in PC12 cells: rescue by bFGF involves protein kinase C delta.

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Article ; Online: PHLPP1 splice variants differentially regulate AKT and PKCα signaling in hippocampal neurons: characterization of PHLPP proteins in the adult hippocampus.

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