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Volumn 31, Issue 1, 2010, Pages 8-14

Protein kinase Cα: disease regulator and therapeutic target

Author keywords

[No Author keywords available]

Indexed keywords

12 (2 CYANOETHYL) 6,7,12,13 TETRAHYDRO 13 METHYL 5 OXOINDOLO[2,3 A]PYRROLO[3,4 C]CARBAZOLE; ALPHA ACTIN; ANTINEOPLASTIC AGENT; ANTISENSE OLIGONUCLEOTIDE; APOLIPOPROTEIN C3; ATRIAL NATRIURETIC FACTOR; BETA1 INTEGRIN; BRYOSTATIN; CALCINEURIN; CALPHOSTIN C; CD31 ANTIGEN; CHELERYTHRINE; ENDOTHELIAL NITRIC OXIDE SYNTHASE; ENZASTAURIN; GELATINASE A; ISIS 3521; KAI 9803; LOW DENSITY LIPOPROTEIN; OXIDIZED LOW DENSITY LIPOPROTEIN; PADGEM PROTEIN; PHOSPHOLIPASE C; PROTEIN KINASE C ALPHA; PROTEIN KINASE C INHIBITOR; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; RUBOXISTAURIN; TRANSIENT RECEPTOR POTENTIAL CHANNEL 1; TROPONIN I; UNCLASSIFIED DRUG; UNINDEXED DRUG; VASCULAR ENDOTHELIAL CADHERIN; VASCULOTROPIN;

EID: 72749088774     PISSN: 01656147     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tips.2009.10.006     Document Type: Article
Times cited : (102)

References (84)
  • 2
    • 33746909044 scopus 로고    scopus 로고
    • Protein kinase Cα but not PKCζ suppresses intestinal tumor formation in ApcMin/+ mice
    • Oster H., and Leitges M. Protein kinase Cα but not PKCζ suppresses intestinal tumor formation in ApcMin/+ mice. Cancer Res. 66 (2006) 6955-6963
    • (2006) Cancer Res. , vol.66 , pp. 6955-6963
    • Oster, H.1    Leitges, M.2
  • 3
    • 1642388834 scopus 로고    scopus 로고
    • PKCα regulates cardiac contractility and propensity toward heart failure
    • Braz J.C., et al. PKCα regulates cardiac contractility and propensity toward heart failure. Nat. Med. 10 (2004) 248-254
    • (2004) Nat. Med. , vol.10 , pp. 248-254
    • Braz, J.C.1
  • 4
    • 61749097572 scopus 로고    scopus 로고
    • PKCα regulates platelet granule secretion and thrombus formation in mice
    • Konopatskaya O., et al. PKCα regulates platelet granule secretion and thrombus formation in mice. J. Clin. Invest. 119 (2009) 399-407
    • (2009) J. Clin. Invest. , vol.119 , pp. 399-407
    • Konopatskaya, O.1
  • 5
    • 41149161288 scopus 로고    scopus 로고
    • PKC isozymes in chronic cardiac disease: possible therapeutic targets?
    • Churchill E., et al. PKC isozymes in chronic cardiac disease: possible therapeutic targets?. Annu. Rev. Pharmacol. Toxicol. 48 (2008) 569-599
    • (2008) Annu. Rev. Pharmacol. Toxicol. , vol.48 , pp. 569-599
    • Churchill, E.1
  • 6
    • 67449132316 scopus 로고    scopus 로고
    • Protein kinase C in heart failure: a therapeutic target?
    • Palaniyandi S.S., et al. Protein kinase C in heart failure: a therapeutic target?. Cardiovasc. Res. 82 (2009) 229-239
    • (2009) Cardiovasc. Res. , vol.82 , pp. 229-239
    • Palaniyandi, S.S.1
  • 7
    • 34250902930 scopus 로고    scopus 로고
    • Targeting the protein kinase C family: are we there yet?
    • Mackay H.J., and Twelves C.J. Targeting the protein kinase C family: are we there yet?. Nat. Rev. Cancer 7 (2007) 554-562
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 554-562
    • Mackay, H.J.1    Twelves, C.J.2
  • 8
    • 0033830338 scopus 로고    scopus 로고
    • Protein kinase C isozymes and the regulation of diverse cell responses
    • Dempsey E.C., et al. Protein kinase C isozymes and the regulation of diverse cell responses. Am. J. Physiol. Lung Cell Mol. Physiol. 279 (2000) L429-438
    • (2000) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.279
    • Dempsey, E.C.1
  • 9
    • 52449088793 scopus 로고    scopus 로고
    • The life and death of protein kinase C
    • Gould C.M., and Newton A.C. The life and death of protein kinase C. Curr. Drug Targets 9 (2008) 614-625
    • (2008) Curr. Drug Targets , vol.9 , pp. 614-625
    • Gould, C.M.1    Newton, A.C.2
  • 10
    • 0036855463 scopus 로고    scopus 로고
    • Protein kinase Cα (PKCα): regulation and biological function
    • Nakashima S. Protein kinase Cα (PKCα): regulation and biological function. J. Biochem. 132 (2002) 669-675
    • (2002) J. Biochem. , vol.132 , pp. 669-675
    • Nakashima, S.1
  • 11
    • 0036214616 scopus 로고    scopus 로고
    • Knockout of PKCα enhances insulin signaling through PI3K
    • Leitges M., et al. Knockout of PKCα enhances insulin signaling through PI3K. Mol. Endocrinol. 16 (2002) 847-858
    • (2002) Mol. Endocrinol. , vol.16 , pp. 847-858
    • Leitges, M.1
  • 12
    • 33646481323 scopus 로고    scopus 로고
    • Defective IgG2a/2b class switching in PKCα-/- mice
    • Pfeifhofer C., et al. Defective IgG2a/2b class switching in PKCα-/- mice. J. Immunol. 176 (2006) 6004-6011
    • (2006) J. Immunol. , vol.176 , pp. 6004-6011
    • Pfeifhofer, C.1
  • 13
    • 33744923428 scopus 로고    scopus 로고
    • Protein kinase C (PKC) α and PKCθ are the major PKC isotypes involved in TCR down-regulation
    • von Essen M., et al. Protein kinase C (PKC) α and PKCθ are the major PKC isotypes involved in TCR down-regulation. J. Immunol. 176 (2006) 7502-7510
    • (2006) J. Immunol. , vol.176 , pp. 7502-7510
    • von Essen, M.1
  • 14
    • 9344258622 scopus 로고    scopus 로고
    • Protein kinase Cα-induced hypertrophy of neonatal rat ventricular myocytes
    • Vijayan K., et al. Protein kinase Cα-induced hypertrophy of neonatal rat ventricular myocytes. Am. J. Physiol. Heart Circ. Physiol. 287 (2004) H2777-2789
    • (2004) Am. J. Physiol. Heart Circ. Physiol. , vol.287
    • Vijayan, K.1
  • 15
    • 0036885610 scopus 로고    scopus 로고
    • Identification of PKCα isoform-specific effects in cardiac myocytes using antisense phosphorothioate oligonucleotides
    • Kerkela R., et al. Identification of PKCα isoform-specific effects in cardiac myocytes using antisense phosphorothioate oligonucleotides. Mol. Pharmacol. 62 (2002) 1482-1491
    • (2002) Mol. Pharmacol. , vol.62 , pp. 1482-1491
    • Kerkela, R.1
  • 16
    • 0037018154 scopus 로고    scopus 로고
    • PKCα regulates the hypertrophic growth of cardiomyocytes through extracellular signal-regulated kinase1/2 (ERK1/2)
    • Braz J.C., et al. PKCα regulates the hypertrophic growth of cardiomyocytes through extracellular signal-regulated kinase1/2 (ERK1/2). J. Cell Biol. 156 (2002) 905-919
    • (2002) J. Cell Biol. , vol.156 , pp. 905-919
    • Braz, J.C.1
  • 17
    • 34547578672 scopus 로고    scopus 로고
    • Augmented protein kinase Cα-induced myofilament protein phosphorylation contributes to myofilament dysfunction in experimental congestive heart failure
    • Belin R.J., et al. Augmented protein kinase Cα-induced myofilament protein phosphorylation contributes to myofilament dysfunction in experimental congestive heart failure. Circ. Res. 101 (2007) 195-204
    • (2007) Circ. Res. , vol.101 , pp. 195-204
    • Belin, R.J.1
  • 18
    • 0041816273 scopus 로고    scopus 로고
    • Identification of a functionally critical protein kinase C phosphorylation residue of cardiac troponin T
    • Sumandea M.P., et al. Identification of a functionally critical protein kinase C phosphorylation residue of cardiac troponin T. J. Biol. Chem. 278 (2003) 35135-35144
    • (2003) J. Biol. Chem. , vol.278 , pp. 35135-35144
    • Sumandea, M.P.1
  • 19
    • 67649695506 scopus 로고    scopus 로고
    • Atherosclerotic plaque development and instability: a dual role for VEGF
    • Holm P.W., et al. Atherosclerotic plaque development and instability: a dual role for VEGF. Ann. Med. 41 (2009) 257-264
    • (2009) Ann. Med. , vol.41 , pp. 257-264
    • Holm, P.W.1
  • 20
    • 42149116966 scopus 로고    scopus 로고
    • Differential regulation of VEGF signaling by PKCα and PKCε in endothelial cells
    • Rask-Madsen C., and King G.L. Differential regulation of VEGF signaling by PKCα and PKCε in endothelial cells. Arterioscler Thromb. Vasc. Biol. 28 (2008) 919-924
    • (2008) Arterioscler Thromb. Vasc. Biol. , vol.28 , pp. 919-924
    • Rask-Madsen, C.1    King, G.L.2
  • 21
    • 2642709170 scopus 로고    scopus 로고
    • Characterization of vascular endothelial growth factor's effect on the activation of protein kinase C, its isoforms, and endothelial cell growth
    • Xia P., et al. Characterization of vascular endothelial growth factor's effect on the activation of protein kinase C, its isoforms, and endothelial cell growth. J. Clin. Invest. 98 (1996) 2018-2026
    • (1996) J. Clin. Invest. , vol.98 , pp. 2018-2026
    • Xia, P.1
  • 22
    • 0035657643 scopus 로고    scopus 로고
    • Protein kinase C inhibitors as novel anticancer drugs
    • Goekjian P.G., and Jirousek M.R. Protein kinase C inhibitors as novel anticancer drugs. Expert Opin. Investig. Drugs 10 (2001) 2117-2140
    • (2001) Expert Opin. Investig. Drugs , vol.10 , pp. 2117-2140
    • Goekjian, P.G.1    Jirousek, M.R.2
  • 23
    • 0037155777 scopus 로고    scopus 로고
    • Inhibition of protein kinase Cα prevents endothelial cell migration and vascular tube formation in vitro and myocardial neovascularization in vivo
    • Wang A., et al. Inhibition of protein kinase Cα prevents endothelial cell migration and vascular tube formation in vitro and myocardial neovascularization in vivo. Circ. Res. 90 (2002) 609-616
    • (2002) Circ. Res. , vol.90 , pp. 609-616
    • Wang, A.1
  • 24
    • 42349108136 scopus 로고    scopus 로고
    • Protein kinase Cα promotes angiogenic activity of human endothelial cells via induction of vascular endothelial growth factor
    • Xu H., et al. Protein kinase Cα promotes angiogenic activity of human endothelial cells via induction of vascular endothelial growth factor. Cardiovasc. Res. 78 (2008) 349-355
    • (2008) Cardiovasc. Res. , vol.78 , pp. 349-355
    • Xu, H.1
  • 25
    • 0034630749 scopus 로고    scopus 로고
    • Endothelial proliferation, migration, and differentiation are blunted by conditionally expressed protein kinase C pseudosubstrate peptides
    • Harrington E.O., et al. Endothelial proliferation, migration, and differentiation are blunted by conditionally expressed protein kinase C pseudosubstrate peptides. Biochem. Biophys Res. Commun. 271 (2000) 499-508
    • (2000) Biochem. Biophys Res. Commun. , vol.271 , pp. 499-508
    • Harrington, E.O.1
  • 26
    • 33847042684 scopus 로고    scopus 로고
    • Interleukin-1beta increases expression and activity of matrix metalloproteinase-2 in cardiac microvascular endothelial cells: role of PKCalpha/beta1 and MAPKs
    • Mountain D.J., et al. Interleukin-1beta increases expression and activity of matrix metalloproteinase-2 in cardiac microvascular endothelial cells: role of PKCalpha/beta1 and MAPKs. Am. J. Physiol. Cell Physiol. 292 (2007) C867-875
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Mountain, D.J.1
  • 27
    • 49849097005 scopus 로고    scopus 로고
    • Endothelial cell junctions and the regulation of vascular permeability and leukocyte transmigration
    • Aghajanian A., et al. Endothelial cell junctions and the regulation of vascular permeability and leukocyte transmigration. J. Thromb. Haemost. 6 (2008) 1453-1460
    • (2008) J. Thromb. Haemost. , vol.6 , pp. 1453-1460
    • Aghajanian, A.1
  • 28
    • 0028121374 scopus 로고
    • Regulation of vascular endothelial barrier function
    • Lum H., and Malik A.B. Regulation of vascular endothelial barrier function. Am. J. Physiol. 267 (1994) L223-241
    • (1994) Am. J. Physiol. , vol.267
    • Lum, H.1    Malik, A.B.2
  • 29
    • 0035368773 scopus 로고    scopus 로고
    • Ca(2+) signalling and PKCα activate increased endothelial permeability by disassembly of VE-cadherin junctions
    • Sandoval R., et al. Ca(2+) signalling and PKCα activate increased endothelial permeability by disassembly of VE-cadherin junctions. J. Physiol. 533 (2001) 433-445
    • (2001) J. Physiol. , vol.533 , pp. 433-445
    • Sandoval, R.1
  • 30
    • 0042845703 scopus 로고    scopus 로고
    • Role of Ca2+ signaling in the regulation of endothelial permeability
    • Tiruppathi C., et al. Role of Ca2+ signaling in the regulation of endothelial permeability. Vascul. Pharmacol. 39 (2002) 173-185
    • (2002) Vascul. Pharmacol. , vol.39 , pp. 173-185
    • Tiruppathi, C.1
  • 31
    • 2442685287 scopus 로고    scopus 로고
    • Protein kinase Cα phosphorylates the TRPC1 channel and regulates store-operated Ca2+ entry in endothelial cells
    • Ahmmed G.U., et al. Protein kinase Cα phosphorylates the TRPC1 channel and regulates store-operated Ca2+ entry in endothelial cells. J. Biol. Chem. 279 (2004) 20941-20949
    • (2004) J. Biol. Chem. , vol.279 , pp. 20941-20949
    • Ahmmed, G.U.1
  • 32
    • 0035933870 scopus 로고    scopus 로고
    • Protein kinase C-alpha signals rho-guanine nucleotide dissociation inhibitor phosphorylation and rho activation and regulates the endothelial cell barrier function
    • Mehta D., et al. Protein kinase C-alpha signals rho-guanine nucleotide dissociation inhibitor phosphorylation and rho activation and regulates the endothelial cell barrier function. J. Biol. Chem. 276 (2001) 22614-22620
    • (2001) J. Biol. Chem. , vol.276 , pp. 22614-22620
    • Mehta, D.1
  • 33
    • 33646823302 scopus 로고    scopus 로고
    • Protein kinase Calpha-RhoA cross-talk in CCL2-induced alterations in brain endothelial permeability
    • Stamatovic S.M., et al. Protein kinase Calpha-RhoA cross-talk in CCL2-induced alterations in brain endothelial permeability. J. Biol. Chem. 281 (2006) 8379-8388
    • (2006) J. Biol. Chem. , vol.281 , pp. 8379-8388
    • Stamatovic, S.M.1
  • 34
    • 0033949332 scopus 로고    scopus 로고
    • Protein kinase C-alpha mediates endothelial barrier dysfunction induced by TNF-alpha
    • Ferro T., et al. Protein kinase C-alpha mediates endothelial barrier dysfunction induced by TNF-alpha. Am. J. Physiol. Lung Cell Mol. Physiol. 278 (2000) L1107-1117
    • (2000) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.278
    • Ferro, T.1
  • 35
    • 0034822445 scopus 로고    scopus 로고
    • Protein phosphatase 2B inhibitor potentiates endothelial PKC activity and barrier dysfunction
    • Lum H., et al. Protein phosphatase 2B inhibitor potentiates endothelial PKC activity and barrier dysfunction. Am. J. Physiol. Lung Cell Mol. Physiol. 281 (2001) L546-555
    • (2001) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.281
    • Lum, H.1
  • 36
    • 0030743466 scopus 로고    scopus 로고
    • High glucose concentrations increase endothelial cell permeability via activation of protein kinase C alpha
    • Hempel A., et al. High glucose concentrations increase endothelial cell permeability via activation of protein kinase C alpha. Circ. Res. 81 (1997) 363-371
    • (1997) Circ. Res. , vol.81 , pp. 363-371
    • Hempel, A.1
  • 37
    • 0026333959 scopus 로고
    • Role of oxidized low density lipoprotein in atherogenesis
    • Witztum J.L., and Steinberg D. Role of oxidized low density lipoprotein in atherogenesis. J. Clin. Invest. 88 (1991) 1785-1792
    • (1991) J. Clin. Invest. , vol.88 , pp. 1785-1792
    • Witztum, J.L.1    Steinberg, D.2
  • 38
    • 13844255039 scopus 로고    scopus 로고
    • Oxidized low-density lipoprotein increases superoxide production by endothelial nitric oxide synthase by inhibiting PKCalpha
    • Fleming I., et al. Oxidized low-density lipoprotein increases superoxide production by endothelial nitric oxide synthase by inhibiting PKCalpha. Cardiovasc. Res. 65 (2005) 897-906
    • (2005) Cardiovasc. Res. , vol.65 , pp. 897-906
    • Fleming, I.1
  • 39
    • 33750439866 scopus 로고    scopus 로고
    • SDF-1-induced adhesion of monocytes to vascular endothelium is modulated by azelnidipine via protein kinase C inhibition
    • Takahashi K., et al. SDF-1-induced adhesion of monocytes to vascular endothelium is modulated by azelnidipine via protein kinase C inhibition. Eur. J. Pharmacol. 552 (2006) 162-169
    • (2006) Eur. J. Pharmacol. , vol.552 , pp. 162-169
    • Takahashi, K.1
  • 40
    • 33847013084 scopus 로고    scopus 로고
    • Apolipoprotein CIII-induced THP-1 cell adhesion to endothelial cells involves pertussis toxin-sensitive G protein- and protein kinase C alpha-mediated nuclear factor-kappaB activation
    • Kawakami A., et al. Apolipoprotein CIII-induced THP-1 cell adhesion to endothelial cells involves pertussis toxin-sensitive G protein- and protein kinase C alpha-mediated nuclear factor-kappaB activation. Arterioscler Thromb. Vasc. Biol. 27 (2007) 219-225
    • (2007) Arterioscler Thromb. Vasc. Biol. , vol.27 , pp. 219-225
    • Kawakami, A.1
  • 41
    • 2342523261 scopus 로고    scopus 로고
    • Lactosylceramide recruits PKCalpha/epsilon and phospholipase A2 to stimulate PECAM-1 expression in human monocytes and adhesion to endothelial cells
    • Gong N., et al. Lactosylceramide recruits PKCalpha/epsilon and phospholipase A2 to stimulate PECAM-1 expression in human monocytes and adhesion to endothelial cells. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 6490-6495
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 6490-6495
    • Gong, N.1
  • 42
    • 13544273188 scopus 로고    scopus 로고
    • Protease-activated receptor-1 activation of endothelial cells induces protein kinase Calpha-dependent phosphorylation of syntaxin 4 and Munc18c: role in signaling p-selectin expression
    • Fu J., et al. Protease-activated receptor-1 activation of endothelial cells induces protein kinase Calpha-dependent phosphorylation of syntaxin 4 and Munc18c: role in signaling p-selectin expression. J. Biol. Chem. 280 (2005) 3178-3184
    • (2005) J. Biol. Chem. , vol.280 , pp. 3178-3184
    • Fu, J.1
  • 43
    • 34248371253 scopus 로고    scopus 로고
    • Clinical aspects of platelet inhibitors and thrombus formation
    • Meadows T.A., and Bhatt D.L. Clinical aspects of platelet inhibitors and thrombus formation. Circ. Res. 100 (2007) 1261-1275
    • (2007) Circ. Res. , vol.100 , pp. 1261-1275
    • Meadows, T.A.1    Bhatt, D.L.2
  • 44
    • 36749062608 scopus 로고    scopus 로고
    • Isoform-specific functions of protein kinase C: the platelet paradigm
    • Harper M.T., and Poole A.W. Isoform-specific functions of protein kinase C: the platelet paradigm. Biochem. Soc. Trans. 35 (2007) 1005-1008
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1005-1008
    • Harper, M.T.1    Poole, A.W.2
  • 45
    • 0035914445 scopus 로고    scopus 로고
    • Identification of protein kinase Calpha as an essential, but not sufficient, cytosolic factor for Ca2+-induced alpha- and dense-core granule secretion in platelets
    • Yoshioka A., et al. Identification of protein kinase Calpha as an essential, but not sufficient, cytosolic factor for Ca2+-induced alpha- and dense-core granule secretion in platelets. J. Biol. Chem. 276 (2001) 39379-39385
    • (2001) J. Biol. Chem. , vol.276 , pp. 39379-39385
    • Yoshioka, A.1
  • 46
    • 0038712739 scopus 로고    scopus 로고
    • Direct demonstration of involvement of protein kinase Calpha in the Ca2+-induced platelet aggregation
    • Tabuchi A., et al. Direct demonstration of involvement of protein kinase Calpha in the Ca2+-induced platelet aggregation. J. Biol. Chem. 278 (2003) 26374-26379
    • (2003) J. Biol. Chem. , vol.278 , pp. 26374-26379
    • Tabuchi, A.1
  • 47
    • 14844302394 scopus 로고    scopus 로고
    • Functional interaction of protein kinase Calpha with the tyrosine kinases Syk and Src in human platelets
    • Pula G., et al. Functional interaction of protein kinase Calpha with the tyrosine kinases Syk and Src in human platelets. J. Biol. Chem. 280 (2005) 7194-7205
    • (2005) J. Biol. Chem. , vol.280 , pp. 7194-7205
    • Pula, G.1
  • 48
    • 33748454742 scopus 로고    scopus 로고
    • Reconstructing and deconstructing agonist-induced activation of integrin alphaIIbbeta3
    • Han J., et al. Reconstructing and deconstructing agonist-induced activation of integrin alphaIIbbeta3. Curr. Biol. 16 (2006) 1796-1806
    • (2006) Curr. Biol. , vol.16 , pp. 1796-1806
    • Han, J.1
  • 49
    • 51349135500 scopus 로고    scopus 로고
    • Protein kinase C isozymes as therapeutic targets for treatment of human cancers
    • Fields A.P., and Murray N.R. Protein kinase C isozymes as therapeutic targets for treatment of human cancers. Adv. Enzyme Regul. 48 (2008) 166-178
    • (2008) Adv. Enzyme Regul. , vol.48 , pp. 166-178
    • Fields, A.P.1    Murray, N.R.2
  • 50
    • 4143112597 scopus 로고    scopus 로고
    • Protein kinase C alpha/beta inhibitor Go6976 promotes formation of cell junctions and inhibits invasion of urinary bladder carcinoma cells
    • Koivunen J., et al. Protein kinase C alpha/beta inhibitor Go6976 promotes formation of cell junctions and inhibits invasion of urinary bladder carcinoma cells. Cancer Res. 64 (2004) 5693-5701
    • (2004) Cancer Res. , vol.64 , pp. 5693-5701
    • Koivunen, J.1
  • 51
    • 0035150233 scopus 로고    scopus 로고
    • High PKC alpha and low E-cadherin expression contribute to high migratory activity of colon carcinoma cells
    • Masur K., et al. High PKC alpha and low E-cadherin expression contribute to high migratory activity of colon carcinoma cells. Mol. Biol. Cell 12 (2001) 1973-1982
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1973-1982
    • Masur, K.1
  • 52
    • 0034980135 scopus 로고    scopus 로고
    • Protein kinase C alpha expression is inversely related to ER status in endometrial carcinoma: possible role in AP-1-mediated proliferation of ER-negative endometrial cancer
    • Fournier D.B., et al. Protein kinase C alpha expression is inversely related to ER status in endometrial carcinoma: possible role in AP-1-mediated proliferation of ER-negative endometrial cancer. Gynecol. Oncol. 81 (2001) 366-372
    • (2001) Gynecol. Oncol. , vol.81 , pp. 366-372
    • Fournier, D.B.1
  • 53
    • 3242809148 scopus 로고    scopus 로고
    • Expression of protein kinase C isoenzymes in benign hyperplasia and carcinoma of prostate
    • Koren R., et al. Expression of protein kinase C isoenzymes in benign hyperplasia and carcinoma of prostate. Oncol. Rep. 11 (2004) 321-326
    • (2004) Oncol. Rep. , vol.11 , pp. 321-326
    • Koren, R.1
  • 54
    • 0034848941 scopus 로고    scopus 로고
    • Patterns of protein kinase C isoenzyme expression in transitional cell carcinoma of bladder. Relation to degree of malignancy
    • Langzam L., et al. Patterns of protein kinase C isoenzyme expression in transitional cell carcinoma of bladder. Relation to degree of malignancy. Am. J. Clin. Pathol. 116 (2001) 377-385
    • (2001) Am. J. Clin. Pathol. , vol.116 , pp. 377-385
    • Langzam, L.1
  • 55
    • 4444275128 scopus 로고    scopus 로고
    • Tumor grade-dependent alterations in the protein kinase C isoform pattern in urinary bladder carcinomas
    • Varga A., et al. Tumor grade-dependent alterations in the protein kinase C isoform pattern in urinary bladder carcinomas. Eur. Urol. 46 (2004) 462-465
    • (2004) Eur. Urol. , vol.46 , pp. 462-465
    • Varga, A.1
  • 56
    • 31144449363 scopus 로고    scopus 로고
    • The role of protein kinase C-alpha in hematologic malignancies
    • Lahn M., et al. The role of protein kinase C-alpha in hematologic malignancies. Acta Haematol. 115 (2006) 1-8
    • (2006) Acta Haematol. , vol.115 , pp. 1-8
    • Lahn, M.1
  • 57
    • 0043136680 scopus 로고    scopus 로고
    • Loss of protein kinase Calpha expression may enhance the tumorigenic potential of Gli1 in basal cell carcinoma
    • Neill G.W., et al. Loss of protein kinase Calpha expression may enhance the tumorigenic potential of Gli1 in basal cell carcinoma. Cancer Res. 63 (2003) 4692-4697
    • (2003) Cancer Res. , vol.63 , pp. 4692-4697
    • Neill, G.W.1
  • 58
    • 5644271449 scopus 로고    scopus 로고
    • Protein kinase C alpha expression in breast and ovarian cancer
    • Lahn M., et al. Protein kinase C alpha expression in breast and ovarian cancer. Oncology 67 (2004) 1-10
    • (2004) Oncology , vol.67 , pp. 1-10
    • Lahn, M.1
  • 59
    • 33744936606 scopus 로고    scopus 로고
    • Upregulation and activation of PKC alpha by ErbB2 through Src promotes breast cancer cell invasion that can be blocked by combined treatment with PKC alpha and Src inhibitors
    • Tan M., et al. Upregulation and activation of PKC alpha by ErbB2 through Src promotes breast cancer cell invasion that can be blocked by combined treatment with PKC alpha and Src inhibitors. Oncogene 25 (2006) 3286-3295
    • (2006) Oncogene , vol.25 , pp. 3286-3295
    • Tan, M.1
  • 60
    • 1242273836 scopus 로고    scopus 로고
    • Immunohistochemical analysis of advanced human breast carcinomas reveals downregulation of protein kinase C alpha
    • Kerfoot C., et al. Immunohistochemical analysis of advanced human breast carcinomas reveals downregulation of protein kinase C alpha. J. Histochem. Cytochem. 52 (2004) 419-422
    • (2004) J. Histochem. Cytochem. , vol.52 , pp. 419-422
    • Kerfoot, C.1
  • 61
    • 2442543262 scopus 로고    scopus 로고
    • The role of protein kinase C-alpha (PKC-alpha) in cancer and its modulation by the novel PKC-alpha-specific inhibitor aprinocarsen
    • Hanauske A.R., et al. The role of protein kinase C-alpha (PKC-alpha) in cancer and its modulation by the novel PKC-alpha-specific inhibitor aprinocarsen. Curr. Pharm. Des. 10 (2004) 1923-1936
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 1923-1936
    • Hanauske, A.R.1
  • 62
    • 0034781901 scopus 로고    scopus 로고
    • ISIS-3521. Isis Pharmaceuticals
    • Li K., and Zhang J. ISIS-3521. Isis Pharmaceuticals. Curr. Opin. Investig. Drugs 2 (2001) 1454-1461
    • (2001) Curr. Opin. Investig. Drugs , vol.2 , pp. 1454-1461
    • Li, K.1    Zhang, J.2
  • 63
    • 4644262519 scopus 로고    scopus 로고
    • A phase I/II study of LY900003, an antisense inhibitor of protein kinase C-alpha, in combination with cisplatin and gemcitabine in patients with advanced non-small cell lung cancer
    • Villalona-Calero M.A., et al. A phase I/II study of LY900003, an antisense inhibitor of protein kinase C-alpha, in combination with cisplatin and gemcitabine in patients with advanced non-small cell lung cancer. Clin. Cancer Res. 10 (2004) 6086-6093
    • (2004) Clin. Cancer Res. , vol.10 , pp. 6086-6093
    • Villalona-Calero, M.A.1
  • 64
    • 19944422076 scopus 로고    scopus 로고
    • A phase II trial of ISIS 3521 in patients with metastatic colorectal cancer
    • Marshall J.L., et al. A phase II trial of ISIS 3521 in patients with metastatic colorectal cancer. Clin. Colorectal. Cancer 4 (2004) 268-274
    • (2004) Clin. Colorectal. Cancer , vol.4 , pp. 268-274
    • Marshall, J.L.1
  • 65
    • 9144226837 scopus 로고    scopus 로고
    • A Phase II trial of aprinocarsen, an antisense oligonucleotide inhibitor of protein kinase C alpha, administered as a 21-day infusion to patients with advanced ovarian carcinoma
    • Advani R., et al. A Phase II trial of aprinocarsen, an antisense oligonucleotide inhibitor of protein kinase C alpha, administered as a 21-day infusion to patients with advanced ovarian carcinoma. Cancer 100 (2004) 321-326
    • (2004) Cancer , vol.100 , pp. 321-326
    • Advani, R.1
  • 66
    • 0037397817 scopus 로고    scopus 로고
    • Antisense therapy directed to protein kinase C-alpha (Affinitak, LY900003/ISIS 3521): potential role in breast cancer
    • Roychowdhury D., and Lahn M. Antisense therapy directed to protein kinase C-alpha (Affinitak, LY900003/ISIS 3521): potential role in breast cancer. Semin Oncol. 30 (2003) 30-33
    • (2003) Semin Oncol. , vol.30 , pp. 30-33
    • Roychowdhury, D.1    Lahn, M.2
  • 67
    • 0036023413 scopus 로고    scopus 로고
    • A randomized phase II and pharmacokinetic study of the antisense oligonucleotides ISIS 3521 and ISIS 5132 in patients with hormone-refractory prostate cancer
    • Tolcher A.W., et al. A randomized phase II and pharmacokinetic study of the antisense oligonucleotides ISIS 3521 and ISIS 5132 in patients with hormone-refractory prostate cancer. Clin. Cancer Res. 8 (2002) 2530-2535
    • (2002) Clin. Cancer Res. , vol.8 , pp. 2530-2535
    • Tolcher, A.W.1
  • 68
    • 4644305430 scopus 로고    scopus 로고
    • Phase II study of ISIS 3521, an antisense oligodeoxynucleotide to protein kinase C alpha, in patients with previously treated low-grade non-Hodgkin's lymphoma
    • Rao S., et al. Phase II study of ISIS 3521, an antisense oligodeoxynucleotide to protein kinase C alpha, in patients with previously treated low-grade non-Hodgkin's lymphoma. Ann. Oncol. 15 (2004) 1413-1418
    • (2004) Ann. Oncol. , vol.15 , pp. 1413-1418
    • Rao, S.1
  • 69
    • 33645453677 scopus 로고    scopus 로고
    • Phase III study of gemcitabine and cisplatin with or without aprinocarsen, a protein kinase C-alpha antisense oligonucleotide, in patients with advanced-stage non-small-cell lung cancer
    • Paz-Ares L., et al. Phase III study of gemcitabine and cisplatin with or without aprinocarsen, a protein kinase C-alpha antisense oligonucleotide, in patients with advanced-stage non-small-cell lung cancer. J. Clin. Oncol. 24 (2006) 1428-1434
    • (2006) J. Clin. Oncol. , vol.24 , pp. 1428-1434
    • Paz-Ares, L.1
  • 70
    • 64149103614 scopus 로고    scopus 로고
    • Protein kinase C intervention: the state of play
    • Roffey J., et al. Protein kinase C intervention: the state of play. Curr. Opin. Cell Biol. 21 (2009) 268-279
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 268-279
    • Roffey, J.1
  • 71
    • 53549089928 scopus 로고    scopus 로고
    • Identification, characterization and initial hit-to-lead optimization of a series of 4-arylamino-3-pyridinecarbonitrile as protein kinase C theta (PKCtheta) inhibitors
    • Cole D.C., et al. Identification, characterization and initial hit-to-lead optimization of a series of 4-arylamino-3-pyridinecarbonitrile as protein kinase C theta (PKCtheta) inhibitors. J. Med. Chem. 51 (2008) 5958-5963
    • (2008) J. Med. Chem. , vol.51 , pp. 5958-5963
    • Cole, D.C.1
  • 72
    • 68049086486 scopus 로고    scopus 로고
    • Protein Kinase C{alpha}, but Not PKC{beta} or PKC{gamma}, Regulates Contractility and Heart Failure Susceptibility. Implications for Ruboxistaurin As a Novel Therapeutic Approach
    • Liu Q., et al. Protein Kinase C{alpha}, but Not PKC{beta} or PKC{gamma}, Regulates Contractility and Heart Failure Susceptibility. Implications for Ruboxistaurin As a Novel Therapeutic Approach. Circ. Res. 105 (2009) 194-200
    • (2009) Circ. Res. , vol.105 , pp. 194-200
    • Liu, Q.1
  • 74
    • 34250702110 scopus 로고    scopus 로고
    • The role of protein kinase C activation and the vascular complications of diabetes
    • Das Evcimen N., and King G.L. The role of protein kinase C activation and the vascular complications of diabetes. Pharmacol. Res. 55 (2007) 498-510
    • (2007) Pharmacol. Res. , vol.55 , pp. 498-510
    • Das Evcimen, N.1    King, G.L.2
  • 75
    • 34547687425 scopus 로고    scopus 로고
    • Phase I pharmacokinetic and pharmacodynamic study of the oral protein kinase C beta-inhibitor enzastaurin in combination with gemcitabine and cisplatin in patients with advanced cancer
    • Rademaker-Lakhai J.M., et al. Phase I pharmacokinetic and pharmacodynamic study of the oral protein kinase C beta-inhibitor enzastaurin in combination with gemcitabine and cisplatin in patients with advanced cancer. Clin. Cancer Res. 13 (2007) 4474-4481
    • (2007) Clin. Cancer Res. , vol.13 , pp. 4474-4481
    • Rademaker-Lakhai, J.M.1
  • 76
    • 0025258567 scopus 로고
    • Chelerythrine is a potent and specific inhibitor of protein kinase C
    • Herbert J.M., et al. Chelerythrine is a potent and specific inhibitor of protein kinase C. Biochem. Biophys Res. Commun. 172 (1990) 993-999
    • (1990) Biochem. Biophys Res. Commun. , vol.172 , pp. 993-999
    • Herbert, J.M.1
  • 77
    • 0028055160 scopus 로고
    • Differential regulation of protein kinase C isozymes by bryostatin 1 and phorbol 12-myristate 13-acetate in NIH 3T3 fibroblasts
    • Szallasi Z., et al. Differential regulation of protein kinase C isozymes by bryostatin 1 and phorbol 12-myristate 13-acetate in NIH 3T3 fibroblasts. J. Biol. Chem. 269 (1994) 2118-2124
    • (1994) J. Biol. Chem. , vol.269 , pp. 2118-2124
    • Szallasi, Z.1
  • 78
    • 38949138457 scopus 로고    scopus 로고
    • Function-oriented synthesis, step economy, and drug design
    • Wender P.A., et al. Function-oriented synthesis, step economy, and drug design. Acc. Chem. Res. 41 (2008) 40-49
    • (2008) Acc. Chem. Res. , vol.41 , pp. 40-49
    • Wender, P.A.1
  • 79
    • 0025784927 scopus 로고
    • Inhibition of protein kinase C by calphostin C is light-dependent
    • Bruns R.F., et al. Inhibition of protein kinase C by calphostin C is light-dependent. Biochem. Biophys Res. Commun. 176 (1991) 288-293
    • (1991) Biochem. Biophys Res. Commun. , vol.176 , pp. 288-293
    • Bruns, R.F.1
  • 80
    • 4544323559 scopus 로고    scopus 로고
    • PKC-interacting proteins: from function to pharmacology
    • Poole A.W., et al. PKC-interacting proteins: from function to pharmacology. Trends Pharmacol. Sci. 25 (2004) 528-535
    • (2004) Trends Pharmacol. Sci. , vol.25 , pp. 528-535
    • Poole, A.W.1
  • 81
    • 58149175775 scopus 로고    scopus 로고
    • Rationally designed peptide regulators of protein kinase C
    • Churchill E.N., et al. Rationally designed peptide regulators of protein kinase C. Trends Endocrinol. Metab. 20 (2009) 25-33
    • (2009) Trends Endocrinol. Metab. , vol.20 , pp. 25-33
    • Churchill, E.N.1
  • 82
    • 39449092458 scopus 로고    scopus 로고
    • Intracoronary KAI-9803 as an adjunct to primary percutaneous coronary intervention for acute ST-segment elevation myocardial infarction
    • Bates E., et al. Intracoronary KAI-9803 as an adjunct to primary percutaneous coronary intervention for acute ST-segment elevation myocardial infarction. Circulation 117 (2008) 886-896
    • (2008) Circulation , vol.117 , pp. 886-896
    • Bates, E.1
  • 83
    • 0035986315 scopus 로고    scopus 로고
    • Molecular characterization of protein kinase C-alpha binding to lamin A
    • Martelli A.M., et al. Molecular characterization of protein kinase C-alpha binding to lamin A. J. Cell Biochem. 86 (2002) 320-330
    • (2002) J. Cell Biochem. , vol.86 , pp. 320-330
    • Martelli, A.M.1
  • 84
    • 0035996587 scopus 로고    scopus 로고
    • Binding of elements of protein kinase C-alpha regulatory domain to lamin B1
    • Tabellini G., et al. Binding of elements of protein kinase C-alpha regulatory domain to lamin B1. Cell Signal. 14 (2002) 819-827
    • (2002) Cell Signal. , vol.14 , pp. 819-827
    • Tabellini, G.1


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