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Article: Protein kinase C isozymes and the regulation of diverse cell responses.

Dempsey, E C / Newton, A C / Mochly-Rosen, D / Fields, A P / Reyland, M E / Insel, P A / Messing, R O

American journal of physiology. Lung cellular and molecular physiology

2000 Volume 279, Issue 3, Page(s) L429–38

Abstract: Individual protein kinase C (PKC) isozymes have been implicated in many cellular responses ... for studying PKC isozymes and their role in cell responses have been developed. Strengths and weaknesses ... binding proteins (like receptors for activated C-kinase and caveolins) is well established. Phosphorylation state ...

Abstract	Individual protein kinase C (PKC) isozymes have been implicated in many cellular responses important in lung health and disease, including permeability, contraction, migration, hypertrophy, proliferation, apoptosis, and secretion. New ideas on mechanisms that regulate PKC activity, including the identification of a novel PKC kinase, 3-phosphoinositide-dependent kinase-1 (PDK-1), that regulates phosphorylation of PKC, have been advanced. The importance of targeted translocation of PKC and isozyme-specific binding proteins (like receptors for activated C-kinase and caveolins) is well established. Phosphorylation state and localization are now thought to be key determinants of isozyme activity and specificity. New concepts on the role of individual PKC isozymes in proliferation and apoptosis are emerging. Opposing roles for selected isozymes in the same cell system have been defined. Coupling to the Wnt signaling pathway has been described. Phenotypes for PKC knockout mice have recently been reported. More specific approaches for studying PKC isozymes and their role in cell responses have been developed. Strengths and weaknesses of different experimental strategies are reviewed. Future directions for investigation are identified.
MeSH term(s)	Animals ; Apoptosis/physiology ; Cell Division/physiology ; Humans ; Ischemia/pathology ; Ischemia/physiopathology ; Isoenzymes/physiology ; Lung/cytology ; Lung/physiology ; Protein Kinase C/physiology ; Pulmonary Circulation
Chemical Substances	Isoenzymes ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2000-09
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	1013184-x
ISSN	1522-1504 ; 1040-0605
ISSN (online)	1522-1504
ISSN	1040-0605
DOI	10.1152/ajplung.2000.279.3.L429
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Zs.A 2749: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)

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Article: The protein kinase C (PKC) family of proteins in cytokine signaling in hematopoiesis.

Redig, Amanda J / Platanias, Leonidas C

Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research

2007 Volume 27, Issue 8, Page(s) 623–636

Abstract: The members of the protein kinase C (PKC) family of proteins play important roles in signaling ... responses. There is emerging evidence that these kinases also play key functional roles in the regulation ... of signals for important cellular processes and to mediate diverse and, in some cases, opposing biologic ...

Abstract	The members of the protein kinase C (PKC) family of proteins play important roles in signaling for various growth factors, cytokines, and hormones. Extensive work over the years has led to the identification of three major groups of PKC isoforms. These include the classic PKCs (PKCalpha, PKCbeta(I), PKCbeta(II), PKCgamma), the novel PKCs (PKCdelta, PKCepsilon, PKCeta, PKCmu, PKCtheta), and the atypical PKCs (PKCzeta, PKCiota/lambda). All these PKC subtypes have been shown to participate in the generation of signals for important cellular processes and to mediate diverse and, in some cases, opposing biologic responses. There is emerging evidence that these kinases also play key functional roles in the regulation of cell growth, apoptosis, and differentiation of hematopoietic cells. In this review, both the engagement of the various PKC members in cytokine and growth factor signaling and their role in the regulation of hematopoiesis are discussed.
MeSH term(s)	Animals ; Cytokines/chemistry ; Cytokines/physiology ; Hematopoiesis/physiology ; Humans ; Isoenzymes/genetics ; Isoenzymes/physiology ; Multigene Family/physiology ; Protein Kinase C/genetics ; Protein Kinase C/physiology ; Signal Transduction/physiology
Chemical Substances	Cytokines ; Isoenzymes ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2007-08
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1226675-9
ISSN	1557-7465 ; 1079-9907
ISSN (online)	1557-7465
ISSN	1079-9907
DOI	10.1089/jir.2007.0007
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Zs.A 1748: Show issues

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Article: Regulation of cardiac stress signaling by protein kinase d1.

Harrison, Brooke C / Kim, Mi-Sung / van Rooij, Eva / Plato, Craig F / Papst, Philip J / Vega, Rick B / McAnally, John A / Richardson, James A / Bassel-Duby, Rhonda / Olson, Eric N / McKinsey, Timothy A

Molecular and cellular biology

2006 Volume 26, Issue 10, Page(s) 3875–3888

Abstract: ... for protein kinase C (PKC) and its downstream effector, protein kinase D1 (PKD1), in the control of HDAC5 ... in cardiac myocytes by diverse hypertrophic agonists that signal through G protein-coupled receptors (GPCRs) and Rho ... undergoes a remodeling process that is associated with myocyte hypertrophy, myocyte death, and fibrosis ...

Abstract	In response to pathological stresses such as hypertension or myocardial infarction, the heart undergoes a remodeling process that is associated with myocyte hypertrophy, myocyte death, and fibrosis. Histone deacetylase 5 (HDAC5) is a transcriptional repressor of cardiac remodeling that is subject to phosphorylation-dependent neutralization in response to stress signaling. Recent studies have suggested a role for protein kinase C (PKC) and its downstream effector, protein kinase D1 (PKD1), in the control of HDAC5 phosphorylation. While PKCs are well-documented regulators of cardiac signaling, the function of PKD1 in heart muscle remains unclear. Here, we demonstrate that PKD1 catalytic activity is stimulated in cardiac myocytes by diverse hypertrophic agonists that signal through G protein-coupled receptors (GPCRs) and Rho GTPases. PKD1 activation in cardiomyocytes occurs through PKC-dependent and -independent mechanisms. In vivo, cardiac PKD1 is activated in multiple rodent models of pathological cardiac remodeling. PKD1 activation correlates with phosphorylation-dependent nuclear export of HDAC5, and reduction of endogenous PKD1 expression with small interfering RNA suppresses HDAC5 shuttling and associated cardiomyocyte growth. Conversely, ectopic overexpression of constitutively active PKD1 in mouse heart leads to dilated cardiomyopathy. These findings support a role for PKD1 in the control of pathological remodeling of the heart via its ability to phosphorylate and neutralize HDAC5.
MeSH term(s)	Animals ; Animals, Newborn ; COS Cells ; Cardiomyopathy, Hypertrophic/genetics ; Cardiomyopathy, Hypertrophic/metabolism ; Cardiomyopathy, Hypertrophic/pathology ; Catalytic Domain ; Cells, Cultured ; Chlorocebus aethiops ; Enzyme Activation ; Gene Expression Regulation ; Heart Ventricles/cytology ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Male ; Mice ; Mice, Transgenic ; Models, Biological ; Myocytes, Cardiac/metabolism ; Myocytes, Cardiac/pathology ; Protein Kinase C ; Protein Kinases/physiology ; RNA, Small Interfering/metabolism ; Rats ; Rats, Inbred SHR ; Rats, Inbred WF ; Rats, Sprague-Dawley ; Signal Transduction ; Stress, Physiological/metabolism
Chemical Substances	Isoenzymes ; RNA, Small Interfering ; Protein Kinases (EC 2.7.-) ; protein kinase D (EC 2.7.10.-) ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2006-04-28
Publishing country	United States
Document type	Comparative Study ; Journal Article
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.26.10.3875-3888.2006
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Zs.A 1666: Show issues

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Article: The diverse roles of protein kinase C in pancreatic beta-cell function.

Biden, Trevor J / Schmitz-Peiffer, Carsten / Burchfield, James G / Gurisik, Ebru / Cantley, James / Mitchell, Christopher J / Carpenter, Lee

Biochemical Society transactions

2008 Volume 36, Issue Pt 5, Page(s) 916–919

Abstract: Members of the serine/threonine PKC (protein kinase C) family perform diverse functions ... function, including cell proliferation, differentiation and death, as well as regulation of secretion ... of cell surface receptors, but the cPKC (conventional PKC) and nPKC (novel PKC) isoforms are also ...

Abstract	Members of the serine/threonine PKC (protein kinase C) family perform diverse functions in multiple cell types. All members of the family are activated in signalling cascades triggered by occupation of cell surface receptors, but the cPKC (conventional PKC) and nPKC (novel PKC) isoforms are also responsive to fatty acid metabolites. PKC isoforms are involved in various aspects of pancreatic beta-cell function, including cell proliferation, differentiation and death, as well as regulation of secretion in response to glucose and muscarinic receptor agonists. Recently, the nPKC isoform, PKCepsilon, has also been implicated in the loss of insulin secretory responsiveness that underpins the development of Type 2 diabetes.
MeSH term(s)	Animals ; Diabetes Mellitus, Type 2/metabolism ; Diabetes Mellitus, Type 2/physiopathology ; Glucose/metabolism ; Insulin/metabolism ; Insulin-Secreting Cells/metabolism ; Isoenzymes/metabolism ; Mice ; Mice, Knockout ; Protein Kinase C/metabolism ; Signal Transduction/physiology
Chemical Substances	Insulin ; Isoenzymes ; Protein Kinase C (EC 2.7.11.13) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2008-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST0360916
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Zs.A 944: Show issues

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Article: Stress-activated protein kinase pathway functions to support protein synthesis and translational adaptation in response to environmental stress in fission yeast.

Dunand-Sauthier, Isabelle / Walker, Carol A / Narasimhan, Jana / Pearce, Amanda K / Wek, Ronald C / Humphrey, Tim C

Eukaryotic cell

2005 Volume 4, Issue 11, Page(s) 1785–1793

Abstract: ... the mitogen-activated protein kinase Spc1/Sty1, suggesting a role for these stress response factors in this translational control ... on the eIF2alpha kinases Hri2 and Gcn2. These findings suggest a role for the SAPK pathway in supporting ... The stress-activated protein kinase (SAPK) pathway plays a central role in coordinating ...

Abstract	The stress-activated protein kinase (SAPK) pathway plays a central role in coordinating gene expression in response to diverse environmental stress stimuli. We examined the role of this pathway in the translational response to stress in Schizosaccharomyces pombe. Exposing wild-type cells to osmotic stress (KCl) resulted in a rapid but transient reduction in protein synthesis. Protein synthesis was further reduced in mutants disrupting the SAPK pathway, including the mitogen-activated protein kinase Wis1 or the mitogen-activated protein kinase Spc1/Sty1, suggesting a role for these stress response factors in this translational control. Further polysome analyses revealed a role for Spc1 in supporting translation initiation during osmotic stress, and additionally in facilitating translational adaptation. Exposure to oxidative stress (H2O2) resulted in a striking reduction in translation initiation in wild-type cells, which was further reduced in spc1- cells. Reduced translation initiation correlated with phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) in wild-type cells. Disruption of Wis1 or Spc1 kinase or the downstream bZip transcription factors Atf1 and Pap1 resulted in a marked increase in eIF2alpha phosphorylation which was dependent on the eIF2alpha kinases Hri2 and Gcn2. These findings suggest a role for the SAPK pathway in supporting translation initiation and facilitating adaptation to environmental stress in part through reducing eIF2alpha phosphorylation in fission yeast.
MeSH term(s)	Cell Survival ; Eukaryotic Initiation Factor-2/metabolism ; Gene Expression Regulation, Fungal ; Isoenzymes/genetics ; Isoenzymes/metabolism ; MAP Kinase Signaling System/physiology ; Mitogen-Activated Protein Kinase 8/genetics ; Mitogen-Activated Protein Kinase 8/metabolism ; Mitogen-Activated Protein Kinase Kinases/genetics ; Mitogen-Activated Protein Kinase Kinases/metabolism ; Osmotic Pressure ; Oxidative Stress ; Pancreatitis-Associated Proteins ; Phosphorylation ; Polyribosomes/metabolism ; Protein Biosynthesis/physiology ; Schizosaccharomyces/genetics ; Schizosaccharomyces/physiology ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism ; eIF-2 Kinase/genetics ; eIF-2 Kinase/metabolism
Chemical Substances	Eukaryotic Initiation Factor-2 ; Isoenzymes ; Pancreatitis-Associated Proteins ; REG3A protein, human ; Schizosaccharomyces pombe Proteins ; eIF-2 Kinase (EC 2.7.11.1) ; Mitogen-Activated Protein Kinase 8 (EC 2.7.11.24) ; Mitogen-Activated Protein Kinase Kinases (EC 2.7.12.2) ; wis1 protein, S pombe (EC 2.7.12.2)
Language	English
Publishing date	2005-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2077635-4
ISSN	1535-9786 ; 1535-9778
ISSN (online)	1535-9786
ISSN	1535-9778
DOI	10.1128/EC.4.11.1785-1793.2005
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Zs.A 5779: Show issues

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Article ; Online: The WD40 repeat protein WDR-23 functions with the CUL4/DDB1 ubiquitin ligase to regulate nuclear abundance and activity of SKN-1 in Caenorhabditis elegans.

Choe, Keith P / Przybysz, Aaron J / Strange, Kevin

Molecular and cellular biology

2009 Volume 29, Issue 10, Page(s) 2704–2715

Abstract: ... but the mechanisms of regulation and signal integration are unknown. We screened the C. elegans genome for regulators ... SKN-1 is regulated by diverse signals that control metabolism, development, and stress responses ... of cytoprotective gene expression and identified a new SKN-1 regulatory pathway. SKN-1 protein levels, nuclear ...

Abstract	The transcription factor SKN-1 protects Caenorhabditis elegans from stress and promotes longevity. SKN-1 is regulated by diverse signals that control metabolism, development, and stress responses, but the mechanisms of regulation and signal integration are unknown. We screened the C. elegans genome for regulators of cytoprotective gene expression and identified a new SKN-1 regulatory pathway. SKN-1 protein levels, nuclear accumulation, and activity are repressed by the WD40 repeat protein WDR-23, which interacts with the CUL-4/DDB-1 ubiquitin ligase to presumably target the transcription factor for proteasomal degradation. WDR-23 regulates SKN-1 target genes downstream from p38 mitogen-activated protein kinase, glycogen synthase kinase 3, and insulin-like receptor pathways, suggesting that phosphorylation of SKN-1 may function to modify its interaction with WDR-23 and/or CUL-4/DDB-1. These findings define the mechanism of SKN-1 accumulation in the cell nucleus and provide a new mechanistic framework for understanding how phosphorylation signals are integrated to regulate stress resistance and longevity.
MeSH term(s)	Amino Acid Sequence ; Animals ; Caenorhabditis elegans/cytology ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/classification ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cell Nucleus/metabolism ; Cullin Proteins/genetics ; Cullin Proteins/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Forkhead Transcription Factors ; Gene Expression Regulation ; Glutathione Transferase/genetics ; Glutathione Transferase/metabolism ; Humans ; Isoenzymes/genetics ; Isoenzymes/metabolism ; MAP Kinase Kinase 4/genetics ; MAP Kinase Kinase 4/metabolism ; Molecular Sequence Data ; Phylogeny ; Proteasome Endopeptidase Complex/metabolism ; Receptor, Insulin/genetics ; Receptor, Insulin/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Repetitive Sequences, Amino Acid ; Repressor Proteins/classification ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Sequence Alignment ; Signal Transduction/physiology ; Stress, Physiological ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Two-Hybrid System Techniques
Chemical Substances	Caenorhabditis elegans Proteins ; Cullin Proteins ; DDB-1 protein, C elegans ; DNA-Binding Proteins ; Forkhead Transcription Factors ; Isoenzymes ; Recombinant Fusion Proteins ; Repressor Proteins ; Transcription Factors ; WDR-23 protein, C elegans ; daf-16 protein, C elegans ; skn-1 protein, C elegans (148733-36-2) ; Glutathione Transferase (EC 2.5.1.18) ; DAF-2 protein, C elegans (EC 2.7.10.1) ; Receptor, Insulin (EC 2.7.10.1) ; MAP Kinase Kinase 4 (EC 2.7.12.2) ; sek-1 protein, C elegans (EC 2.7.12.2) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2009-03-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.01811-08
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Zs.A 1666: Show issues

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Article: Protein kinase C targeting in antineoplastic treatment strategies.

Jarvis, W D / Grant, S

Investigational new drugs

1999 Volume 17, Issue 3, Page(s) 227–240

Abstract: ... Noteworthy among several anti-apoptotic signaling elements is the protein kinase C (PKC) isoenzyme family ... which mediates a central cytoprotective effect in the regulation of cell survival. Activation of PKC, and ... been associated with loss of the mitogen-activated protein kinase (MAPK) response. Accordingly, recent ...

Abstract	Neoplastic cell survival is governed by a balance between pro-apoptotic and anti-apoptotic signals. Noteworthy among several anti-apoptotic signaling elements is the protein kinase C (PKC) isoenzyme family, which mediates a central cytoprotective effect in the regulation of cell survival. Activation of PKC, and subsequent recruitment of numerous downstream elements such as the mitogen-activated protein kinase (MAPK) cascade, opposes initiation of the apoptotic cell death program by diverse cytotoxic stimuli. The understanding that the lethal actions of numerous antineoplastic agents are, in many instances, antagonized by cytoprotective signaling systems has been an important stimulus for the development of novel antineoplastic strategies. In this regard, inhibition of PKC, which has been shown to initiate apoptosis in a variety of malignant cell types, has recently been the focus of intense interest. Furthermore, there is accumulating evidence that selective targeting of PKC may prove useful in improving the therapeutic efficacy of established antineoplastic agents. Such chemosensitizing strategies can involve either (a) direct inhibition of PKC (e.g., following acute treatment with relatively specific inhibitors such as the synthetic sphingoid base analog safingol, or the novel staurosporine derivatives UCN-01 and CGP-41251) or (b) down-regulation (e.g., following chronic treatment with the non-tumor-promoting PKC activator bryostatin 1). In preclinical model systems, suppression of the cytoprotective function(s) of PKC potentiates the activity of cytotoxic agents (e.g., cytarabine) as well as ionizing radiation, and efforts to translate these findings into the clinical arena in humans are currently underway. Although the PKC-driven cytoprotective signaling systems affected by these treatments have not been definitively characterized, interference with PKC activity has been associated with loss of the mitogen-activated protein kinase (MAPK) response. Accordingly, recent pre-clinical studies have demonstrated that pharmacological disruption of the primary MEK-ERK module can mimic the chemopotentiating and radiopotentiating actions of PKC inhibition and/or down-regulation.
MeSH term(s)	Animals ; Antineoplastic Agents/pharmacology ; Bryostatins ; Cell Survival ; Cytoprotection ; Enzyme Inhibitors/pharmacology ; Humans ; Lactones/pharmacology ; Macrolides ; Mitogen-Activated Protein Kinase Kinases/physiology ; Naphthalenes/pharmacology ; Protein Kinase C/antagonists & inhibitors ; Protein Kinase C/physiology ; Sphingosine/analogs & derivatives ; Sphingosine/pharmacology ; Staurosporine/pharmacology
Chemical Substances	Antineoplastic Agents ; Bryostatins ; Enzyme Inhibitors ; Lactones ; Macrolides ; Naphthalenes ; bryostatin 1 (37O2X55Y9E) ; Protein Kinase C (EC 2.7.11.13) ; Mitogen-Activated Protein Kinase Kinases (EC 2.7.12.2) ; Staurosporine (H88EPA0A3N) ; calphostin C (I271P23G24) ; Sphingosine (NGZ37HRE42) ; safingol (OWA98U788S)
Language	English
Publishing date	1999
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	604895-x
ISSN	1573-0646 ; 0167-6997
ISSN (online)	1573-0646
ISSN	0167-6997
DOI	10.1023/a:1006328303451
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Article: Protein interactions with nitric oxide synthases: controlling the right time, the right place, and the right amount of nitric oxide.

Kone, Bruce C / Kuncewicz, Teresa / Zhang, Wenzheng / Yu, Zhi-Yuan

American journal of physiology. Renal physiology

2003 Volume 285, Issue 2, Page(s) F178–90

Abstract: ... caveolins, anchoring proteins, G protein-coupled receptors, kinases, and molecular chaperones, modulate ... with the inhibitory molecules kalirin and NOS-associated protein 110 kDa, as well as activator proteins, the Rac ... Because of its high biological reactivity and diffusibility, multiple tiers of regulation, ranging ...

Abstract	Nitric oxide (NO) is a potent cell-signaling, effector, and vasodilator molecule that plays important roles in diverse biological effects in the kidney, vasculature, and many other tissues. Because of its high biological reactivity and diffusibility, multiple tiers of regulation, ranging from transcriptional to posttranslational controls, tightly control NO biosynthesis. Interactions of each of the major NO synthase (NOS) isoforms with heterologous proteins have emerged as a mechanism by which the activity, spatial distribution, and proximity of the NOS isoforms to regulatory proteins and intended targets are governed. Dimerization of the NOS isozymes, required for their activity, exhibits distinguishing features among these proteins and may serve as a regulated process and target for therapeutic intervention. An increasingly wide array of proteins, ranging from scaffolding proteins to membrane receptors, has been shown to function as NOS-binding partners. Neuronal NOS interacts via its PDZ domain with several PDZ-domain proteins. Several resident and recruited proteins of plasmalemmal caveolae, including caveolins, anchoring proteins, G protein-coupled receptors, kinases, and molecular chaperones, modulate the activity and trafficking of endothelial NOS in the endothelium. Inducible NOS (iNOS) interacts with the inhibitory molecules kalirin and NOS-associated protein 110 kDa, as well as activator proteins, the Rac GTPases. In addition, protein-protein interactions of proteins governing iNOS transcription function to specify activation or suppression of iNOS induction by cytokines. The calpain and ubiquitin-proteasome pathways are the major proteolytic systems responsible for the regulated degradation of NOS isozymes. The experimental basis for these protein-protein interactions, their functional importance, and potential implication for renal and vascular physiology and pathophysiology is reviewed.
MeSH term(s)	Animals ; Calmodulin/metabolism ; HSP90 Heat-Shock Proteins/metabolism ; Humans ; Nitric Oxide/metabolism ; Nitric Oxide Synthase/metabolism ; rac GTP-Binding Proteins/metabolism
Chemical Substances	Calmodulin ; HSP90 Heat-Shock Proteins ; Nitric Oxide (31C4KY9ESH) ; Nitric Oxide Synthase (EC 1.14.13.39) ; rac GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2003-08
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	603837-2
ISSN	1522-1466 ; 1931-857X ; 0363-6127
ISSN (online)	1522-1466
ISSN	1931-857X ; 0363-6127
DOI	10.1152/ajprenal.00048.2003
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Article: Identification of WNK1 as a substrate of Akt/protein kinase B and a negative regulator of insulin-stimulated mitogenesis in 3T3-L1 cells.

Jiang, Zhen Y / Zhou, Qiong L / Holik, John / Patel, Shraddha / Leszyk, John / Coleman, Kerri / Chouinard, My / Czech, Michael P

The Journal of biological chemistry

2005 Volume 280, Issue 22, Page(s) 21622–21628

Abstract: ... WNK1 phosphorylation, but depletion of protein kinase C lambda did not. Whereas small interfering RNA ... of the phosphatidylinositol 3-kinase (PI3K) pathway, regulates diverse cellular functions including metabolic pathways ... protein were identified as the protein kinase WNK1 (with no lysine) by matrix-assisted laser desorption ...

Abstract	Insulin signaling through protein kinase Akt/protein kinase B (PKB), a downstream element of the phosphatidylinositol 3-kinase (PI3K) pathway, regulates diverse cellular functions including metabolic pathways, apoptosis, mitogenesis, and membrane trafficking. To identify Akt/PKB substrates that mediate these effects, we used antibodies that recognize phosphopeptide sites containing the Akt/PKB substrate motif (RXRXX(p)S/T) to immunoprecipitate proteins from insulin-stimulated adipocytes. Tryptic peptides from a 250-kDa immunoprecipitated protein were identified as the protein kinase WNK1 (with no lysine) by matrix-assisted laser desorption ionization time-of-flight mass spectrometry, consistent with a recent report that WNK1 is phosphorylated on Thr60 in response to insulin-like growth factor I. Insulin treatment of 3T3-L1 adipocytes stimulated WNK1 phosphorylation, as detected by immunoprecipitation with antibody against WNK1 followed by immunoblotting with the anti-phosphoAkt substrate antibody. WNK1 phosphorylation induced by insulin was unaffected by rapamycin, an inhibitor of p70 S6 kinase pathway but abolished by the PI3K inhibitor wortmannin. RNA interference-directed depletion of Akt1/PKB alpha and Akt2/PKB beta attenuated insulin-stimulated WNK1 phosphorylation, but depletion of protein kinase C lambda did not. Whereas small interfering RNA-induced loss of WNK1 protein did not significantly affect insulin-stimulated glucose transport in 3T3-L1 adipocytes, it significantly enhanced insulin-stimulated thymidine incorporation by about 2-fold. Furthermore, depletion of WNK1 promoted serum-stimulated cell proliferation of 3T3-L1 preadipocytes, as evidenced by a 36% increase in cell number after 48 h in culture. These data suggest that WNK1 is a physiologically relevant target of insulin signaling through PI3K and Akt/PKB and functions as a negative regulator of insulin-stimulated mitogenesis.
MeSH term(s)	3T3-L1 Cells ; Adipocytes/metabolism ; Androstadienes/pharmacology ; Animals ; Apoptosis ; Binding Sites ; Biological Transport ; Cell Membrane/metabolism ; Cell Proliferation ; Dose-Response Relationship, Drug ; Electrophoresis, Polyacrylamide Gel ; Gene Expression Regulation ; Gene Expression Regulation, Enzymologic ; Glucose/metabolism ; Humans ; Immunoblotting ; Immunoprecipitation ; Insulin/metabolism ; Intracellular Signaling Peptides and Proteins ; Isoenzymes/metabolism ; Mass Spectrometry ; Mice ; Minor Histocompatibility Antigens ; Peptides/chemistry ; Phosphoinositide-3 Kinase Inhibitors ; Phosphorylation ; Protein Kinase C/metabolism ; Protein Structure, Tertiary ; Protein Transport ; Protein-Serine-Threonine Kinases/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; RNA Interference ; RNA, Small Interfering/metabolism ; Receptor, Insulin/metabolism ; Ribosomal Protein S6 Kinases, 70-kDa/metabolism ; Signal Transduction ; Sirolimus/pharmacology ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Thymidine/metabolism ; Time Factors ; Transfection ; Trypsin/pharmacology ; WNK Lysine-Deficient Protein Kinase 1 ; Wortmannin
Chemical Substances	Androstadienes ; Insulin ; Intracellular Signaling Peptides and Proteins ; Isoenzymes ; Minor Histocompatibility Antigens ; Peptides ; Phosphoinositide-3 Kinase Inhibitors ; Proto-Oncogene Proteins ; RNA, Small Interfering ; Receptor, Insulin (EC 2.7.10.1) ; AKT1 protein, human (EC 2.7.11.1) ; AKT2 protein, human (EC 2.7.11.1) ; Akt2 protein, mouse (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Ribosomal Protein S6 Kinases, 70-kDa (EC 2.7.11.1) ; WNK Lysine-Deficient Protein Kinase 1 (EC 2.7.11.1) ; WNK1 protein, human (EC 2.7.11.1) ; Wnk1 protein, mouse (EC 2.7.11.1) ; Protein Kinase C (EC 2.7.11.13) ; protein kinase C lambda (EC 2.7.11.13) ; Trypsin (EC 3.4.21.4) ; Glucose (IY9XDZ35W2) ; Thymidine (VC2W18DGKR) ; Sirolimus (W36ZG6FT64) ; Wortmannin (XVA4O219QW)
Language	English
Publishing date	2005-03-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M414464200
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: A p53-independent G1 cell cycle checkpoint induced by the suppression of protein kinase C alpha and theta isoforms.

Deeds, Linda / Teodorescu, Sanda / Chu, Michelle / Yu, Qiang / Chen, Chang-Yan

The Journal of biological chemistry

2003 Volume 278, Issue 41, Page(s) 39782–39793

Abstract: The protein kinase C (PKC) family consists of multiple isoforms that are involved in the regulation ... isoforms is crucial for the induction of G1 cell cycle arrest and that this negative cell cycle regulation ... of diverse cellular responses. Suppression of PKC induces growth arrest in various types of cells ...

Abstract	The protein kinase C (PKC) family consists of multiple isoforms that are involved in the regulation of diverse cellular responses. Suppression of PKC induces growth arrest in various types of cells. However, the underlying molecular mechanisms have not been thoroughly investigated. In this report, we demonstrated that the concurrent inhibition, rather than separate inhibition, of phorbol ester-dependent PKC alpha and theta isoforms is crucial for the induction of G1 cell cycle arrest and that this negative cell cycle regulation is via p53-independent mechanisms. PKC suppression-mediated growth arrest is associated with the induction of cell cycle inhibitor p21WAF1/CIP1 and the occurrence of hypophosphorylated Rb. The G1 checkpoint induced by the suppression of PKC occurs not only in murine Swiss3T3 but also in p53-deficient cells and human lung cancer cells containing mutated p53. Luciferase and nuclear run-off assays demonstrated that p21WAF1/CIP1 is, in part, transcriptionally regulated in response to the suppression of PKC alpha and theta. However, the stability of p21 mRNA is also augmented after the addition of PKC alpha and theta antisense oligonucleotides, indicating the involvement of post-transcriptional mechanisms in p21WAF1/CIP1 expression. These data suggest the existence of a cell cycle checkpoint pathway regulated by PKC alpha and theta isoforms. Furthermore, our findings support the notion that G1 checkpoint control can be restored in tumor cells containing abnormal p53, by targeting the PKC-regulated p21WAF1/CIP1 induction.
MeSH term(s)	3T3 Cells ; Animals ; Base Sequence ; Cyclin D ; Cyclin-Dependent Kinase 4 ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclin-Dependent Kinases/metabolism ; Cyclins/genetics ; Cyclins/metabolism ; Enzyme Inhibitors/pharmacology ; G1 Phase/drug effects ; G1 Phase/genetics ; G1 Phase/physiology ; Gene Deletion ; Genes, p53 ; Humans ; Isoenzymes/antagonists & inhibitors ; Isoenzymes/genetics ; Mice ; Oligodeoxyribonucleotides, Antisense/genetics ; Oligodeoxyribonucleotides, Antisense/pharmacology ; Protein Kinase C/antagonists & inhibitors ; Protein Kinase C/genetics ; Protein Kinase C-alpha ; Protein Kinase C-theta ; Proto-Oncogene Proteins ; Retinoblastoma Protein/metabolism ; Transcription, Genetic ; Tumor Suppressor Protein p53/metabolism
Chemical Substances	CDKN1A protein, human ; Cdkn1a protein, mouse ; Cyclin D ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclins ; Enzyme Inhibitors ; Isoenzymes ; Oligodeoxyribonucleotides, Antisense ; Proto-Oncogene Proteins ; Retinoblastoma Protein ; Tumor Suppressor Protein p53 ; PRKCA protein, human (EC 2.7.11.13) ; PRKCQ protein, human (EC 2.7.11.13) ; Prkca protein, mouse (EC 2.7.11.13) ; Prkcq protein, mouse (EC 2.7.11.13) ; Protein Kinase C (EC 2.7.11.13) ; Protein Kinase C-alpha (EC 2.7.11.13) ; Protein Kinase C-theta (EC 2.7.11.13) ; CDK4 protein, human (EC 2.7.11.22) ; Cdk4 protein, mouse (EC 2.7.11.22) ; Cyclin-Dependent Kinase 4 (EC 2.7.11.22) ; Cyclin-Dependent Kinases (EC 2.7.11.22)
Language	English
Publishing date	2003-08-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M306854200
Database	MEDical Literature Analysis and Retrieval System OnLINE

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