메뉴 건너뛰기




Volumn 40, Issue , 2017, Pages 1-9

Protein kinase C isoforms in the normal pancreas and in pancreatic disease

Author keywords

Pancreas; Pancreatic cancer; Pancreatitis; PKC; Protein kinase C

Indexed keywords

PROTEIN KINASE C ALPHA; PROTEIN KINASE C BETA; PROTEIN KINASE C EPSILON; PROTEIN KINASE C GAMMA; PROTEIN KINASE C THETA; PROTEIN KINASE C ZETA; ISOPROTEIN; PROTEIN KINASE C;

EID: 85028001457     PISSN: 08986568     EISSN: 18733913     Source Type: Journal    
DOI: 10.1016/j.cellsig.2017.08.005     Document Type: Review
Times cited : (12)

References (102)
  • 1
    • 0028811653 scopus 로고
    • Protein kinase C: structure, function, and regulation
    • Newton, A.C., Protein kinase C: structure, function, and regulation. J. Biol. Chem. 270:48 (1995), 28495–28498.
    • (1995) J. Biol. Chem. , vol.270 , Issue.48 , pp. 28495-28498
    • Newton, A.C.1
  • 2
    • 0023555557 scopus 로고
    • Protein kinase C contains a pseudosubstrate prototope in its regulatory domain
    • House, C., Kemp, B.E., Protein kinase C contains a pseudosubstrate prototope in its regulatory domain. Science 238:4834 (1987), 1726–1728.
    • (1987) Science , vol.238 , Issue.4834 , pp. 1726-1728
    • House, C.1    Kemp, B.E.2
  • 3
    • 12344323484 scopus 로고    scopus 로고
    • Type 2 diabetes-a matter of beta-cell life and death?
    • Rhodes, C.J., Type 2 diabetes-a matter of beta-cell life and death?. Science 307:5708 (2005), 380–384.
    • (2005) Science , vol.307 , Issue.5708 , pp. 380-384
    • Rhodes, C.J.1
  • 4
    • 84883546693 scopus 로고    scopus 로고
    • Role of pancreatic beta-cell death and inflammation in diabetes
    • Quan, W., Jo, E.K., Lee, M.S., Role of pancreatic beta-cell death and inflammation in diabetes. Diabetes Obes. Metab. 15:Suppl. 3 (2013), 141–151.
    • (2013) Diabetes Obes. Metab. , vol.15 , pp. 141-151
    • Quan, W.1    Jo, E.K.2    Lee, M.S.3
  • 5
    • 84942525569 scopus 로고    scopus 로고
    • Inflammation in acute and chronic pancreatitis
    • Habtezion, A., Inflammation in acute and chronic pancreatitis. Curr. Opin. Gastroenterol. 31:5 (2015), 395–399.
    • (2015) Curr. Opin. Gastroenterol. , vol.31 , Issue.5 , pp. 395-399
    • Habtezion, A.1
  • 6
    • 85014571316 scopus 로고    scopus 로고
    • Acinar cell plasticity and development of pancreatic ductal adenocarcinoma
    • Storz, P., Acinar cell plasticity and development of pancreatic ductal adenocarcinoma. Nat. Rev. Gastroenterol. Hepatol. 14:5 (2017), 296–304.
    • (2017) Nat. Rev. Gastroenterol. Hepatol. , vol.14 , Issue.5 , pp. 296-304
    • Storz, P.1
  • 7
    • 0037362895 scopus 로고    scopus 로고
    • Expression patterns of protein kinase C isoenzymes are characteristically modulated in chronic pancreatitis and pancreatic cancer
    • Evans, J.D., Cornford, P.A., Dodson, A., Neoptolemos, J.P., Foster, C.S., Expression patterns of protein kinase C isoenzymes are characteristically modulated in chronic pancreatitis and pancreatic cancer. Am. J. Clin. Pathol. 119:3 (2003), 392–402.
    • (2003) Am. J. Clin. Pathol. , vol.119 , Issue.3 , pp. 392-402
    • Evans, J.D.1    Cornford, P.A.2    Dodson, A.3    Neoptolemos, J.P.4    Foster, C.S.5
  • 8
    • 77949268993 scopus 로고    scopus 로고
    • Enhancement of glucagon secretion in mouse and human pancreatic alpha cells by protein kinase C (PKC) involves intracellular trafficking of PKCalpha and PKCdelta
    • De Marinis, Y.Z., Zhang, E., Amisten, S., Taneera, J., Renstrom, E., Rorsman, P., Eliasson, L., Enhancement of glucagon secretion in mouse and human pancreatic alpha cells by protein kinase C (PKC) involves intracellular trafficking of PKCalpha and PKCdelta. Diabetologia 53:4 (2010), 717–729.
    • (2010) Diabetologia , vol.53 , Issue.4 , pp. 717-729
    • De Marinis, Y.Z.1    Zhang, E.2    Amisten, S.3    Taneera, J.4    Renstrom, E.5    Rorsman, P.6    Eliasson, L.7
  • 9
    • 0022541880 scopus 로고
    • Enhancement of glucagon secretion from isolated rat islets of Langerhans by phorbol 12-myristate 13-acetate
    • Hii, C.S., Stutchfield, J., Howell, S.L., Enhancement of glucagon secretion from isolated rat islets of Langerhans by phorbol 12-myristate 13-acetate. Biochem. J. 233:1 (1986), 287–289.
    • (1986) Biochem. J. , vol.233 , Issue.1 , pp. 287-289
    • Hii, C.S.1    Stutchfield, J.2    Howell, S.L.3
  • 10
    • 0029979956 scopus 로고    scopus 로고
    • Protein kinase C in beta-cells: expression of multiple isoforms and involvement in cholinergic stimulation of insulin secretion
    • Tian, Y.M., Urquidi, V., Ashcroft, S.J., Protein kinase C in beta-cells: expression of multiple isoforms and involvement in cholinergic stimulation of insulin secretion. Mol. Cell. Endocrinol. 119:2 (1996), 185–193.
    • (1996) Mol. Cell. Endocrinol. , vol.119 , Issue.2 , pp. 185-193
    • Tian, Y.M.1    Urquidi, V.2    Ashcroft, S.J.3
  • 11
    • 0030599453 scopus 로고    scopus 로고
    • Atypical isoforms of pKc and insulin secretion from pancreatic beta-cells: evidence using Go 6976 and Ro 31-8220 as Pkc inhibitors
    • Harris, T.E., Persaud, S.J., Jones, P.M., Atypical isoforms of pKc and insulin secretion from pancreatic beta-cells: evidence using Go 6976 and Ro 31-8220 as Pkc inhibitors. Biochem. Biophys. Res. Commun. 227:3 (1996), 672–676.
    • (1996) Biochem. Biophys. Res. Commun. , vol.227 , Issue.3 , pp. 672-676
    • Harris, T.E.1    Persaud, S.J.2    Jones, P.M.3
  • 12
    • 0036868797 scopus 로고    scopus 로고
    • Glucose-stimulated signaling pathways in biphasic insulin secretion
    • Straub, S.G., Sharp, G.W., Glucose-stimulated signaling pathways in biphasic insulin secretion. Diabetes Metab. Res. Rev. 18:6 (2002), 451–463.
    • (2002) Diabetes Metab. Res. Rev. , vol.18 , Issue.6 , pp. 451-463
    • Straub, S.G.1    Sharp, G.W.2
  • 13
    • 0037400679 scopus 로고    scopus 로고
    • Protein kinase A- and C-induced insulin release from Ca2 + -insensitive pools
    • Lee, I.S., Hur, E.M., Suh, B.C., Kim, M.H., Koh, D.S., Rhee, I.J., Ha, H., Kim, K.T., Protein kinase A- and C-induced insulin release from Ca2 + -insensitive pools. Cell. Signal. 15:5 (2003), 529–537.
    • (2003) Cell. Signal. , vol.15 , Issue.5 , pp. 529-537
    • Lee, I.S.1    Hur, E.M.2    Suh, B.C.3    Kim, M.H.4    Koh, D.S.5    Rhee, I.J.6    Ha, H.7    Kim, K.T.8
  • 15
    • 85004147176 scopus 로고    scopus 로고
    • EX4 stabilizes and activates Nrf2 via PKCdelta, contributing to the prevention of oxidative stress-induced pancreatic beta cell damage
    • Kim, M.H., Kim, E.H., Jung, H.S., Yang, D., Park, E.Y., Jun, H.S., EX4 stabilizes and activates Nrf2 via PKCdelta, contributing to the prevention of oxidative stress-induced pancreatic beta cell damage. Toxicol. Appl. Pharmacol. 315 (2017), 60–69.
    • (2017) Toxicol. Appl. Pharmacol. , vol.315 , pp. 60-69
    • Kim, M.H.1    Kim, E.H.2    Jung, H.S.3    Yang, D.4    Park, E.Y.5    Jun, H.S.6
  • 17
    • 0027960617 scopus 로고
    • Effects of cholecystokinin (CCK) and other secretagogues on isoforms of protein kinase C (PKC) in pancreatic acini
    • Pollo, D.A., Baldassare, J.J., Honda, T., Henderson, P.A., Talkad, V.D., Gardner, J.D., Effects of cholecystokinin (CCK) and other secretagogues on isoforms of protein kinase C (PKC) in pancreatic acini. Biochim. Biophys. Acta 1224:1 (1994), 127–138.
    • (1994) Biochim. Biophys. Acta , vol.1224 , Issue.1 , pp. 127-138
    • Pollo, D.A.1    Baldassare, J.J.2    Honda, T.3    Henderson, P.A.4    Talkad, V.D.5    Gardner, J.D.6
  • 18
    • 0028889361 scopus 로고
    • Cellular distribution of isoforms of protein kinase C (PKC) in pancreatic acini
    • Bastani, B., Yang, L., Baldassare, J.J., Pollo, D.A., Gardner, J.D., Cellular distribution of isoforms of protein kinase C (PKC) in pancreatic acini. Biochim. Biophys. Acta 1269:3 (1995), 307–315.
    • (1995) Biochim. Biophys. Acta , vol.1269 , Issue.3 , pp. 307-315
    • Bastani, B.1    Yang, L.2    Baldassare, J.J.3    Pollo, D.A.4    Gardner, J.D.5
  • 19
    • 4644292587 scopus 로고    scopus 로고
    • Regulation of CCK-induced amylase release by PKC-delta in rat pancreatic acinar cells
    • Li, C., Chen, X., Williams, J.A., Regulation of CCK-induced amylase release by PKC-delta in rat pancreatic acinar cells. Am. J. Physiol. Gastrointest. Liver Physiol. 287:4 (2004), G764–71.
    • (2004) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.287 , Issue.4 , pp. G764-71
    • Li, C.1    Chen, X.2    Williams, J.A.3
  • 21
    • 0028113896 scopus 로고
    • Multiple affinity states of different cholecystokinin receptors
    • Huang, S.C., Fortune, K.P., Wank, S.A., Kopin, A.S., Gardner, J.D., Multiple affinity states of different cholecystokinin receptors. J. Biol. Chem. 269:42 (1994), 26121–26126.
    • (1994) J. Biol. Chem. , vol.269 , Issue.42 , pp. 26121-26126
    • Huang, S.C.1    Fortune, K.P.2    Wank, S.A.3    Kopin, A.S.4    Gardner, J.D.5
  • 22
    • 0028143113 scopus 로고
    • Characterization of the three different states of the cholecystokinin (CCK) receptor in pancreatic acini
    • Talkad, V.D., Patto, R.J., Metz, D.C., Turner, R.J., Fortune, K.P., Bhat, S.T., Gardner, J.D., Characterization of the three different states of the cholecystokinin (CCK) receptor in pancreatic acini. Biochim. Biophys. Acta 1224:1 (1994), 103–116.
    • (1994) Biochim. Biophys. Acta , vol.1224 , Issue.1 , pp. 103-116
    • Talkad, V.D.1    Patto, R.J.2    Metz, D.C.3    Turner, R.J.4    Fortune, K.P.5    Bhat, S.T.6    Gardner, J.D.7
  • 23
    • 0037121531 scopus 로고    scopus 로고
    • Cholecystokinin-stimulated tyrosine phosphorylation of PKC-delta in pancreatic acinar cells is regulated bidirectionally by PKC activation
    • Tapia, J.A., Bragado, M.J., Garcia-Marin, L.J., Jensen, R.T., Cholecystokinin-stimulated tyrosine phosphorylation of PKC-delta in pancreatic acinar cells is regulated bidirectionally by PKC activation. Biochim. Biophys. Acta 1593:1 (2002), 99–113.
    • (2002) Biochim. Biophys. Acta , vol.1593 , Issue.1 , pp. 99-113
    • Tapia, J.A.1    Bragado, M.J.2    Garcia-Marin, L.J.3    Jensen, R.T.4
  • 24
    • 33947305951 scopus 로고    scopus 로고
    • CCK causes PKD1 activation in pancreatic acini by signaling through PKC-delta and PKC-independent pathways
    • Berna, M.J., Hoffmann, K.M., Tapia, J.A., Thill, M., Pace, A., Mantey, S.A., Jensen, R.T., CCK causes PKD1 activation in pancreatic acini by signaling through PKC-delta and PKC-independent pathways. Biochim. Biophys. Acta 1773:4 (2007), 483–501.
    • (2007) Biochim. Biophys. Acta , vol.1773 , Issue.4 , pp. 483-501
    • Berna, M.J.1    Hoffmann, K.M.2    Tapia, J.A.3    Thill, M.4    Pace, A.5    Mantey, S.A.6    Jensen, R.T.7
  • 25
    • 0035851112 scopus 로고    scopus 로고
    • Rottlerin is a mitochondrial uncoupler that decreases cellular ATP levels and indirectly blocks protein kinase Cdelta tyrosine phosphorylation
    • Soltoff, S.P., Rottlerin is a mitochondrial uncoupler that decreases cellular ATP levels and indirectly blocks protein kinase Cdelta tyrosine phosphorylation. J. Biol. Chem. 276:41 (2001), 37986–37992.
    • (2001) J. Biol. Chem. , vol.276 , Issue.41 , pp. 37986-37992
    • Soltoff, S.P.1
  • 26
    • 32144454027 scopus 로고    scopus 로고
    • Rottlerin inhibits stimulated enzymatic secretion and several intracellular signaling transduction pathways in pancreatic acinar cells by a non-PKC-delta-dependent mechanism
    • Tapia, J.A., Jensen, R.T., Garcia-Marin, L.J., Rottlerin inhibits stimulated enzymatic secretion and several intracellular signaling transduction pathways in pancreatic acinar cells by a non-PKC-delta-dependent mechanism. Biochim. Biophys. Acta 1763:1 (2006), 25–38.
    • (2006) Biochim. Biophys. Acta , vol.1763 , Issue.1 , pp. 25-38
    • Tapia, J.A.1    Jensen, R.T.2    Garcia-Marin, L.J.3
  • 27
    • 84979520528 scopus 로고    scopus 로고
    • Involvement of myristoylated alanine-rich C kinase substrate phosphorylation and translocation in cholecystokinin-induced amylase release in rat pancreatic acini
    • Satoh, K., Narita, T., Katsumata-Kato, O., Sugiya, H., Seo, Y., Involvement of myristoylated alanine-rich C kinase substrate phosphorylation and translocation in cholecystokinin-induced amylase release in rat pancreatic acini. Am. J. Physiol. Gastrointest. Liver Physiol. 310:6 (2016), G399–409.
    • (2016) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.310 , Issue.6 , pp. G399-409
    • Satoh, K.1    Narita, T.2    Katsumata-Kato, O.3    Sugiya, H.4    Seo, Y.5
  • 28
    • 0037731790 scopus 로고
    • Molecular cloning, characterization, and expression of a cDNA encoding the “80- to 87-kDa” myristoylated alanine-rich C kinase substrate: a major cellular substrate for protein kinase C
    • Stumpo, D.J., Graff, J.M., Albert, K.A., Greengard, P., Blackshear, P.J., Molecular cloning, characterization, and expression of a cDNA encoding the “80- to 87-kDa” myristoylated alanine-rich C kinase substrate: a major cellular substrate for protein kinase C. Proc. Natl. Acad. Sci. U. S. A. 86:11 (1989), 4012–4016.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , Issue.11 , pp. 4012-4016
    • Stumpo, D.J.1    Graff, J.M.2    Albert, K.A.3    Greengard, P.4    Blackshear, P.J.5
  • 30
    • 82555167074 scopus 로고    scopus 로고
    • PKCtheta activation in pancreatic acinar cells by gastrointestinal hormones/neurotransmitters and growth factors is needed for stimulation of numerous important cellular signaling cascades
    • Sancho, V., Berna, M.J., Thill, M., Jensen, R.T., PKCtheta activation in pancreatic acinar cells by gastrointestinal hormones/neurotransmitters and growth factors is needed for stimulation of numerous important cellular signaling cascades. Biochim. Biophys. Acta 1813:12 (2011), 2145–2156.
    • (2011) Biochim. Biophys. Acta , vol.1813 , Issue.12 , pp. 2145-2156
    • Sancho, V.1    Berna, M.J.2    Thill, M.3    Jensen, R.T.4
  • 32
    • 0026752739 scopus 로고
    • Structure, function, and regulation of cellular tight junctions
    • Schneeberger, E.E., Lynch, R.D., Structure, function, and regulation of cellular tight junctions. Am. J. Phys. 262:6 Pt 1 (1992), L647–61.
    • (1992) Am. J. Phys. , vol.262 , Issue.6 , pp. L647-61
    • Schneeberger, E.E.1    Lynch, R.D.2
  • 33
    • 77957255799 scopus 로고    scopus 로고
    • Transcriptional control of tight junction proteins via a protein kinase C signal pathway in human telomerase reverse transcriptase-transfected human pancreatic duct epithelial cells
    • Yamaguchi, H., Kojima, T., Ito, T., Kimura, Y., Imamura, M., Son, S., Koizumi, J., Murata, M., Nagayama, M., Nobuoka, T., Tanaka, S., Hirata, K., Sawada, N., Transcriptional control of tight junction proteins via a protein kinase C signal pathway in human telomerase reverse transcriptase-transfected human pancreatic duct epithelial cells. Am. J. Pathol. 177:2 (2010), 698–712.
    • (2010) Am. J. Pathol. , vol.177 , Issue.2 , pp. 698-712
    • Yamaguchi, H.1    Kojima, T.2    Ito, T.3    Kimura, Y.4    Imamura, M.5    Son, S.6    Koizumi, J.7    Murata, M.8    Nagayama, M.9    Nobuoka, T.10    Tanaka, S.11    Hirata, K.12    Sawada, N.13
  • 34
    • 80051519812 scopus 로고    scopus 로고
    • Transcriptional regulation of claudin-18 via specific protein kinase C signaling pathways and modification of DNA methylation in human pancreatic cancer cells
    • Ito, T., Kojima, T., Yamaguchi, H., Kyuno, D., Kimura, Y., Imamura, M., Takasawa, A., Murata, M., Tanaka, S., Hirata, K., Sawada, N., Transcriptional regulation of claudin-18 via specific protein kinase C signaling pathways and modification of DNA methylation in human pancreatic cancer cells. J. Cell. Biochem. 112:7 (2011), 1761–1772.
    • (2011) J. Cell. Biochem. , vol.112 , Issue.7 , pp. 1761-1772
    • Ito, T.1    Kojima, T.2    Yamaguchi, H.3    Kyuno, D.4    Kimura, Y.5    Imamura, M.6    Takasawa, A.7    Murata, M.8    Tanaka, S.9    Hirata, K.10    Sawada, N.11
  • 35
    • 0029907455 scopus 로고    scopus 로고
    • Interactions between secretin and acetylcholine in the regulation of fluid secretion by isolated rat pancreatic ducts
    • Evans, R.L., Ashton, N., Elliott, A.C., Green, R., Argent, B.E., Interactions between secretin and acetylcholine in the regulation of fluid secretion by isolated rat pancreatic ducts. J. Physiol. 496:Pt 1 (1996), 265–273.
    • (1996) J. Physiol. , vol.496 , pp. 265-273
    • Evans, R.L.1    Ashton, N.2    Elliott, A.C.3    Green, R.4    Argent, B.E.5
  • 37
    • 23044434059 scopus 로고    scopus 로고
    • Metabolon disruption: a mechanism that regulates bicarbonate transport
    • Alvarez, B.V., Vilas, G.L., Casey, J.R., Metabolon disruption: a mechanism that regulates bicarbonate transport. EMBO J. 24:14 (2005), 2499–2511.
    • (2005) EMBO J. , vol.24 , Issue.14 , pp. 2499-2511
    • Alvarez, B.V.1    Vilas, G.L.2    Casey, J.R.3
  • 40
    • 84934343239 scopus 로고    scopus 로고
    • Mechanisms linking inflammation to insulin resistance
    • Chen, L., Chen, R., Wang, H., Liang, F., Mechanisms linking inflammation to insulin resistance. Int. J. Endocrinol., 2015, 2015, 508409.
    • (2015) Int. J. Endocrinol. , vol.2015 , pp. 508409
    • Chen, L.1    Chen, R.2    Wang, H.3    Liang, F.4
  • 41
    • 80355133234 scopus 로고    scopus 로고
    • Macrophagse-mediated inflammation in metabolic disease
    • Chawla, A., Nguyen, K.D., Goh, Y.P., Macrophagse-mediated inflammation in metabolic disease. Nat. Rev. Immunol. 11:11 (2011), 738–749.
    • (2011) Nat. Rev. Immunol. , vol.11 , Issue.11 , pp. 738-749
    • Chawla, A.1    Nguyen, K.D.2    Goh, Y.P.3
  • 44
    • 65549130128 scopus 로고    scopus 로고
    • mTORC1 activation regulates beta-cell mass and proliferation by modulation of cyclin D2 synthesis and stability
    • Balcazar, N., Sathyamurthy, A., Elghazi, L., Gould, A., Weiss, A., Shiojima, I., Walsh, K., Bernal-Mizrachi, E., mTORC1 activation regulates beta-cell mass and proliferation by modulation of cyclin D2 synthesis and stability. J. Biol. Chem. 284:12 (2009), 7832–7842.
    • (2009) J. Biol. Chem. , vol.284 , Issue.12 , pp. 7832-7842
    • Balcazar, N.1    Sathyamurthy, A.2    Elghazi, L.3    Gould, A.4    Weiss, A.5    Shiojima, I.6    Walsh, K.7    Bernal-Mizrachi, E.8
  • 45
    • 78951485569 scopus 로고    scopus 로고
    • Deletion of protein kinase Cdelta in mice modulates stability of inflammatory genes and protects against cytokine-stimulated beta cell death in vitro and in vivo
    • Cantley, J., Boslem, E., Laybutt, D.R., Cordery, D.V., Pearson, G., Carpenter, L., Leitges, M., Biden, T.J., Deletion of protein kinase Cdelta in mice modulates stability of inflammatory genes and protects against cytokine-stimulated beta cell death in vitro and in vivo. Diabetologia 54:2 (2011), 380–389.
    • (2011) Diabetologia , vol.54 , Issue.2 , pp. 380-389
    • Cantley, J.1    Boslem, E.2    Laybutt, D.R.3    Cordery, D.V.4    Pearson, G.5    Carpenter, L.6    Leitges, M.7    Biden, T.J.8
  • 46
    • 34548036686 scopus 로고    scopus 로고
    • Toll-like receptor 2 senses beta-cell death and contributes to the initiation of autoimmune diabetes
    • Kim, H.S., Han, M.S., Chung, K.W., Kim, S., Kim, E., Kim, M.J., Jang, E., Lee, H.A., Youn, J., Akira, S., Lee, M.S., Toll-like receptor 2 senses beta-cell death and contributes to the initiation of autoimmune diabetes. Immunity 27:2 (2007), 321–333.
    • (2007) Immunity , vol.27 , Issue.2 , pp. 321-333
    • Kim, H.S.1    Han, M.S.2    Chung, K.W.3    Kim, S.4    Kim, E.5    Kim, M.J.6    Jang, E.7    Lee, H.A.8    Youn, J.9    Akira, S.10    Lee, M.S.11
  • 48
    • 0035895998 scopus 로고    scopus 로고
    • Protein kinase Cdelta activation by interleukin-1beta stabilizes inducible nitric-oxide synthase mRNA in pancreatic beta-cells
    • Carpenter, L., Cordery, D., Biden, T.J., Protein kinase Cdelta activation by interleukin-1beta stabilizes inducible nitric-oxide synthase mRNA in pancreatic beta-cells. J. Biol. Chem. 276:7 (2001), 5368–5374.
    • (2001) J. Biol. Chem. , vol.276 , Issue.7 , pp. 5368-5374
    • Carpenter, L.1    Cordery, D.2    Biden, T.J.3
  • 49
    • 0030005411 scopus 로고    scopus 로고
    • The harmony of the spheres: inducible nitric oxide synthase and related genes in pancreatic beta cells
    • Eizirik, D.L., Flodstrom, M., Karlsen, A.E., Welsh, N., The harmony of the spheres: inducible nitric oxide synthase and related genes in pancreatic beta cells. Diabetologia 39:8 (1996), 875–890.
    • (1996) Diabetologia , vol.39 , Issue.8 , pp. 875-890
    • Eizirik, D.L.1    Flodstrom, M.2    Karlsen, A.E.3    Welsh, N.4
  • 51
    • 0028268936 scopus 로고
    • Long-term exposure of rat pancreatic islets to fatty acids inhibits glucose-induced insulin secretion and biosynthesis through a glucose fatty acid cycle
    • Zhou, Y.P., Grill, V.E., Long-term exposure of rat pancreatic islets to fatty acids inhibits glucose-induced insulin secretion and biosynthesis through a glucose fatty acid cycle. J. Clin. Invest. 93:2 (1994), 870–876.
    • (1994) J. Clin. Invest. , vol.93 , Issue.2 , pp. 870-876
    • Zhou, Y.P.1    Grill, V.E.2
  • 53
    • 0031767880 scopus 로고    scopus 로고
    • Zymogen proteolysis within the pancreatic acinar cell is associated with cellular injury
    • Grady, T., Mah'Moud, M., Otani, T., Rhee, S., Lerch, M.M., Gorelick, F.S., Zymogen proteolysis within the pancreatic acinar cell is associated with cellular injury. Am. J. Phys. 275:5 Pt 1 (1998), G1010–7.
    • (1998) Am. J. Phys. , vol.275 , Issue.5 , pp. G1010-7
    • Grady, T.1    Mah'Moud, M.2    Otani, T.3    Rhee, S.4    Lerch, M.M.5    Gorelick, F.S.6
  • 54
    • 12344302086 scopus 로고    scopus 로고
    • Effects of increased intracellular cAMP on carbachol-stimulated zymogen activation, secretion, and injury in the pancreatic acinar cell
    • Chaudhuri, A., Kolodecik, T.R., Gorelick, F.S., Effects of increased intracellular cAMP on carbachol-stimulated zymogen activation, secretion, and injury in the pancreatic acinar cell. Am. J. Physiol. Gastrointest. Liver Physiol. 288:2 (2005), G235–43.
    • (2005) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.288 , Issue.2 , pp. G235-43
    • Chaudhuri, A.1    Kolodecik, T.R.2    Gorelick, F.S.3
  • 55
    • 81855228093 scopus 로고    scopus 로고
    • Intra-acinar trypsinogen activation mediates early stages of pancreatic injury but not inflammation in mice with acute pancreatitis
    • (e2)
    • Dawra, R., Sah, R.P., Dudeja, V., Rishi, L., Talukdar, R., Garg, P., Saluja, A.K., Intra-acinar trypsinogen activation mediates early stages of pancreatic injury but not inflammation in mice with acute pancreatitis. Gastroenterology 141:6 (2011), 2210–2217 (e2).
    • (2011) Gastroenterology , vol.141 , Issue.6 , pp. 2210-2217
    • Dawra, R.1    Sah, R.P.2    Dudeja, V.3    Rishi, L.4    Talukdar, R.5    Garg, P.6    Saluja, A.K.7
  • 57
    • 0023080603 scopus 로고
    • Exocytosis occurs at the lateral plasma membrane of the pancreatic acinar cell during supramaximal secretagogue stimulation
    • Scheele, G., Adler, G., Kern, H., Exocytosis occurs at the lateral plasma membrane of the pancreatic acinar cell during supramaximal secretagogue stimulation. Gastroenterology 92:2 (1987), 345–353.
    • (1987) Gastroenterology , vol.92 , Issue.2 , pp. 345-353
    • Scheele, G.1    Adler, G.2    Kern, H.3
  • 58
    • 0035206785 scopus 로고    scopus 로고
    • Supramaximal cholecystokinin displaces Munc18c from the pancreatic acinar basal surface, redirecting apical exocytosis to the basal membrane
    • Gaisano, H.Y., Lutz, M.P., Leser, J., Sheu, L., Lynch, G., Tang, L., Tamori, Y., Trimble, W.S., Salapatek, A.M., Supramaximal cholecystokinin displaces Munc18c from the pancreatic acinar basal surface, redirecting apical exocytosis to the basal membrane. J. Clin. Invest. 108:11 (2001), 1597–1611.
    • (2001) J. Clin. Invest. , vol.108 , Issue.11 , pp. 1597-1611
    • Gaisano, H.Y.1    Lutz, M.P.2    Leser, J.3    Sheu, L.4    Lynch, G.5    Tang, L.6    Tamori, Y.7    Trimble, W.S.8    Salapatek, A.M.9
  • 59
    • 34247265426 scopus 로고    scopus 로고
    • Alcohol-induced protein kinase Calpha phosphorylation of Munc18c in carbachol-stimulated acini causes basolateral exocytosis
    • Cosen-Binker, L.I., Lam, P.P., Binker, M.G., Gaisano, H.Y., Alcohol-induced protein kinase Calpha phosphorylation of Munc18c in carbachol-stimulated acini causes basolateral exocytosis. Gastroenterology 132:4 (2007), 1527–1545.
    • (2007) Gastroenterology , vol.132 , Issue.4 , pp. 1527-1545
    • Cosen-Binker, L.I.1    Lam, P.P.2    Binker, M.G.3    Gaisano, H.Y.4
  • 60
    • 34250368480 scopus 로고    scopus 로고
    • Alcohol/cholecystokinin-evoked pancreatic acinar basolateral exocytosis is mediated by protein kinase C alpha phosphorylation of Munc18c
    • Cosen-Binker, L.I., Lam, P.P., Binker, M.G., Reeve, J., Pandol, S., Gaisano, H.Y., Alcohol/cholecystokinin-evoked pancreatic acinar basolateral exocytosis is mediated by protein kinase C alpha phosphorylation of Munc18c. J. Biol. Chem. 282:17 (2007), 13047–13058.
    • (2007) J. Biol. Chem. , vol.282 , Issue.17 , pp. 13047-13058
    • Cosen-Binker, L.I.1    Lam, P.P.2    Binker, M.G.3    Reeve, J.4    Pandol, S.5    Gaisano, H.Y.6
  • 61
    • 0036007501 scopus 로고    scopus 로고
    • NF-kappaB activation in pancreas induces pancreatic and systemic inflammatory response
    • Chen, X., Ji, B., Han, B., Ernst, S.A., Simeone, D., Logsdon, C.D., NF-kappaB activation in pancreas induces pancreatic and systemic inflammatory response. Gastroenterology 122:2 (2002), 448–457.
    • (2002) Gastroenterology , vol.122 , Issue.2 , pp. 448-457
    • Chen, X.1    Ji, B.2    Han, B.3    Ernst, S.A.4    Simeone, D.5    Logsdon, C.D.6
  • 63
    • 78149414074 scopus 로고    scopus 로고
    • PKC delta mediates pro-inflammatory responses in a mouse model of caerulein-induced acute pancreatitis
    • (Berl)
    • Ramnath, R.D., Sun, J., Bhatia, M., PKC delta mediates pro-inflammatory responses in a mouse model of caerulein-induced acute pancreatitis. J. Mol. Med. 88:10 (2010), 1055–1063 (Berl).
    • (2010) J. Mol. Med. , vol.88 , Issue.10 , pp. 1055-1063
    • Ramnath, R.D.1    Sun, J.2    Bhatia, M.3
  • 65
    • 0036327373 scopus 로고    scopus 로고
    • Enhancement of anchorage-independent growth of human pancreatic carcinoma MIA PaCa-2 cells by signaling from protein kinase C to mitogen-activated protein kinase
    • Ishino, K., Fukazawa, H., Shikano, M., Ohba, M., Kuroki, T., Uehara, Y., Enhancement of anchorage-independent growth of human pancreatic carcinoma MIA PaCa-2 cells by signaling from protein kinase C to mitogen-activated protein kinase. Mol. Carcinog. 34:4 (2002), 180–186.
    • (2002) Mol. Carcinog. , vol.34 , Issue.4 , pp. 180-186
    • Ishino, K.1    Fukazawa, H.2    Shikano, M.3    Ohba, M.4    Kuroki, T.5    Uehara, Y.6
  • 66
    • 77950250455 scopus 로고    scopus 로고
    • Protein kinase Ciota is required for pancreatic cancer cell transformed growth and tumorigenesis
    • Scotti, M.L., Bamlet, W.R., Smyrk, T.C., Fields, A.P., Murray, N.R., Protein kinase Ciota is required for pancreatic cancer cell transformed growth and tumorigenesis. Cancer Res. 70:5 (2010), 2064–2074.
    • (2010) Cancer Res. , vol.70 , Issue.5 , pp. 2064-2074
    • Scotti, M.L.1    Bamlet, W.R.2    Smyrk, T.C.3    Fields, A.P.4    Murray, N.R.5
  • 67
    • 0033828604 scopus 로고    scopus 로고
    • Activation of protein kinase Calpha inhibits growth of pancreatic cancer cells via p21(cip)-mediated G(1) arrest
    • Detjen, K.M., Brembeck, F.H., Welzel, M., Kaiser, A., Haller, H., Wiedenmann, B., Rosewicz, S., Activation of protein kinase Calpha inhibits growth of pancreatic cancer cells via p21(cip)-mediated G(1) arrest. J. Cell Sci. 113:Pt 17 (2000), 3025–3035.
    • (2000) J. Cell Sci. , vol.113 , pp. 3025-3035
    • Detjen, K.M.1    Brembeck, F.H.2    Welzel, M.3    Kaiser, A.4    Haller, H.5    Wiedenmann, B.6    Rosewicz, S.7
  • 68
    • 0038308404 scopus 로고    scopus 로고
    • Activation of conventional PKC isoforms increases expression of the pro-apoptotic protein bad and TRAIL receptors
    • Farrow, B., Thomas, R.P., Wang, X.F., Evers, B.M., Activation of conventional PKC isoforms increases expression of the pro-apoptotic protein bad and TRAIL receptors. Int. J. Gastrointest. Cancer 32:2–3 (2002), 63–72.
    • (2002) Int. J. Gastrointest. Cancer , vol.32 , Issue.2-3 , pp. 63-72
    • Farrow, B.1    Thomas, R.P.2    Wang, X.F.3    Evers, B.M.4
  • 71
    • 84906938439 scopus 로고    scopus 로고
    • Oncogenic KRAS signalling in pancreatic cancer
    • Eser, S., Schnieke, A., Schneider, G., Saur, D., Oncogenic KRAS signalling in pancreatic cancer. Br. J. Cancer 111:5 (2014), 817–822.
    • (2014) Br. J. Cancer , vol.111 , Issue.5 , pp. 817-822
    • Eser, S.1    Schnieke, A.2    Schneider, G.3    Saur, D.4
  • 73
    • 37649023286 scopus 로고    scopus 로고
    • Matrix metalloproteinase 7 controls pancreatic acinar cell transdifferentiation by activating the Notch signaling pathway
    • Sawey, E.T., Johnson, J.A., Crawford, H.C., Matrix metalloproteinase 7 controls pancreatic acinar cell transdifferentiation by activating the Notch signaling pathway. Proc. Natl. Acad. Sci. U. S. A. 104:49 (2007), 19327–19332.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , Issue.49 , pp. 19327-19332
    • Sawey, E.T.1    Johnson, J.A.2    Crawford, H.C.3
  • 75
    • 84947713840 scopus 로고    scopus 로고
    • K-Ras promotes Tumorigenicity through suppression of non-canonical Wnt signaling
    • Wang, M.T., Holderfield, M., Galeas, J., Delrosario, R., M.D. To, Balmain, A., McCormick, F., K-Ras promotes Tumorigenicity through suppression of non-canonical Wnt signaling. Cell 163:5 (2015), 1237–1251.
    • (2015) Cell , vol.163 , Issue.5 , pp. 1237-1251
    • Wang, M.T.1    Holderfield, M.2    Galeas, J.3    Delrosario, R.4    To, M.D.5    Balmain, A.6    McCormick, F.7
  • 76
    • 84867580010 scopus 로고    scopus 로고
    • Activation of protein kinase Cdelta leads to increased pancreatic acinar cell dedifferentiation in the absence of MIST1
    • Johnson, C.L., Peat, J.M., Volante, S.N., Wang, R., McLean, C.A., Pin, C.L., Activation of protein kinase Cdelta leads to increased pancreatic acinar cell dedifferentiation in the absence of MIST1. J. Pathol. 228:3 (2012), 351–365.
    • (2012) J. Pathol. , vol.228 , Issue.3 , pp. 351-365
    • Johnson, C.L.1    Peat, J.M.2    Volante, S.N.3    Wang, R.4    McLean, C.A.5    Pin, C.L.6
  • 78
    • 0031455541 scopus 로고    scopus 로고
    • Protein kinase C-epsilon associates with the Raf-1 kinase and induces the production of growth factors that stimulate Raf-1 activity
    • Ueffing, M., Lovric, J., Philipp, A., Mischak, H., Kolch, W., Protein kinase C-epsilon associates with the Raf-1 kinase and induces the production of growth factors that stimulate Raf-1 activity. Oncogene 15:24 (1997), 2921–2927.
    • (1997) Oncogene , vol.15 , Issue.24 , pp. 2921-2927
    • Ueffing, M.1    Lovric, J.2    Philipp, A.3    Mischak, H.4    Kolch, W.5
  • 79
    • 0037631323 scopus 로고    scopus 로고
    • Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein
    • Corbit, K.C., Trakul, N., Eves, E.M., Diaz, B., Marshall, M., Rosner, M.R., Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein. J. Biol. Chem. 278:15 (2003), 13061–13068.
    • (2003) J. Biol. Chem. , vol.278 , Issue.15 , pp. 13061-13068
    • Corbit, K.C.1    Trakul, N.2    Eves, E.M.3    Diaz, B.4    Marshall, M.5    Rosner, M.R.6
  • 80
    • 0038520185 scopus 로고    scopus 로고
    • Neurotensin stimulates protein kinase C-dependent mitogenic signaling in human pancreatic carcinoma cell line PANC-1
    • Guha, S., Lunn, J.A., Santiskulvong, C., Rozengurt, E., Neurotensin stimulates protein kinase C-dependent mitogenic signaling in human pancreatic carcinoma cell line PANC-1. Cancer Res. 63:10 (2003), 2379–2387.
    • (2003) Cancer Res. , vol.63 , Issue.10 , pp. 2379-2387
    • Guha, S.1    Lunn, J.A.2    Santiskulvong, C.3    Rozengurt, E.4
  • 81
    • 33746577861 scopus 로고    scopus 로고
    • Possible role of duration of PKC-induced ERK activation in the effects of agonists and phorbol esters on DNA synthesis in Panc-1 cells
    • Racz, G.Z., Szucs, A., Szlavik, V., Vag, J., Burghardt, B., Elliott, A.C., Varga, G., Possible role of duration of PKC-induced ERK activation in the effects of agonists and phorbol esters on DNA synthesis in Panc-1 cells. J. Cell. Biochem. 98:6 (2006), 1667–1680.
    • (2006) J. Cell. Biochem. , vol.98 , Issue.6 , pp. 1667-1680
    • Racz, G.Z.1    Szucs, A.2    Szlavik, V.3    Vag, J.4    Burghardt, B.5    Elliott, A.C.6    Varga, G.7
  • 82
    • 84920414826 scopus 로고    scopus 로고
    • Dying tumor cells stimulate proliferation of living tumor cells via caspase-dependent protein kinase Cdelta activation in pancreatic ductal adenocarcinoma
    • Cheng, J., Tian, L., Ma, J., Gong, Y., Zhang, Z., Chen, Z., Xu, B., Xiong, H., Li, C., Huang, Q., Dying tumor cells stimulate proliferation of living tumor cells via caspase-dependent protein kinase Cdelta activation in pancreatic ductal adenocarcinoma. Mol. Oncol. 9:1 (2015), 105–114.
    • (2015) Mol. Oncol. , vol.9 , Issue.1 , pp. 105-114
    • Cheng, J.1    Tian, L.2    Ma, J.3    Gong, Y.4    Zhang, Z.5    Chen, Z.6    Xu, B.7    Xiong, H.8    Li, C.9    Huang, Q.10
  • 83
    • 84883178112 scopus 로고    scopus 로고
    • Protein kinase C zeta regulates human pancreatic cancer cell transformed growth and invasion through a STAT3-dependent mechanism
    • Butler, A.M., Scotti Buzhardt, M.L., Li, S., Smith, K.E., Fields, A.P., Murray, N.R., Protein kinase C zeta regulates human pancreatic cancer cell transformed growth and invasion through a STAT3-dependent mechanism. PLoS One, 8(8), 2013, e72061.
    • (2013) PLoS One , vol.8 , Issue.8
    • Butler, A.M.1    Scotti Buzhardt, M.L.2    Li, S.3    Smith, K.E.4    Fields, A.P.5    Murray, N.R.6
  • 86
    • 0027212503 scopus 로고
    • Nonpromoting 12-deoxyphorbol 13-esters inhibit phorbol 12-myristate 13-acetate induced tumor promotion in CD-1 mouse skin
    • Szallasi, Z., Krsmanovic, L., Blumberg, P.M., Nonpromoting 12-deoxyphorbol 13-esters inhibit phorbol 12-myristate 13-acetate induced tumor promotion in CD-1 mouse skin. Cancer Res. 53:11 (1993), 2507–2512.
    • (1993) Cancer Res. , vol.53 , Issue.11 , pp. 2507-2512
    • Szallasi, Z.1    Krsmanovic, L.2    Blumberg, P.M.3
  • 87
    • 77955191504 scopus 로고    scopus 로고
    • PKCalpha-induced drug resistance in pancreatic cancer cells is associated with transforming growth factor-beta1
    • Chen, Y., Yu, G., Yu, D., Zhu, M., PKCalpha-induced drug resistance in pancreatic cancer cells is associated with transforming growth factor-beta1. J. Exp. Clin. Cancer Res., 29, 2010, 104.
    • (2010) J. Exp. Clin. Cancer Res. , vol.29 , pp. 104
    • Chen, Y.1    Yu, G.2    Yu, D.3    Zhu, M.4
  • 88
    • 84878997835 scopus 로고    scopus 로고
    • Protein kinase Calpha inhibitor protects against downregulation of claudin-1 during epithelial-mesenchymal transition of pancreatic cancer
    • Kyuno, D., Kojima, T., Yamaguchi, H., Ito, T., Kimura, Y., Imamura, M., Takasawa, A., Murata, M., Tanaka, S., Hirata, K., Sawada, N., Protein kinase Calpha inhibitor protects against downregulation of claudin-1 during epithelial-mesenchymal transition of pancreatic cancer. Carcinogenesis 34:6 (2013), 1232–1243.
    • (2013) Carcinogenesis , vol.34 , Issue.6 , pp. 1232-1243
    • Kyuno, D.1    Kojima, T.2    Yamaguchi, H.3    Ito, T.4    Kimura, Y.5    Imamura, M.6    Takasawa, A.7    Murata, M.8    Tanaka, S.9    Hirata, K.10    Sawada, N.11
  • 89
    • 42049109067 scopus 로고    scopus 로고
    • TGF-beta mediates PTEN suppression and cell motility through calcium-dependent PKC-alpha activation in pancreatic cancer cells
    • Chow, J.Y., Dong, H., Quach, K.T., Van Nguyen, P.N., Chen, K., Carethers, J.M., TGF-beta mediates PTEN suppression and cell motility through calcium-dependent PKC-alpha activation in pancreatic cancer cells. Am. J. Physiol. Gastrointest. Liver Physiol. 294:4 (2008), G899–905.
    • (2008) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.294 , Issue.4 , pp. G899-905
    • Chow, J.Y.1    Dong, H.2    Quach, K.T.3    Van Nguyen, P.N.4    Chen, K.5    Carethers, J.M.6
  • 91
    • 36749090072 scopus 로고    scopus 로고
    • Inhibition of protein kinase Cbeta by enzastaurin enhances radiation cytotoxicity in pancreatic cancer
    • Spalding, A.C., Watson, R., Davis, M.E., Kim, A.C., Lawrence, T.S., Ben-Josef, E., Inhibition of protein kinase Cbeta by enzastaurin enhances radiation cytotoxicity in pancreatic cancer. Clin. Cancer Res. 13:22 Pt 1 (2007), 6827–6833.
    • (2007) Clin. Cancer Res. , vol.13 , Issue.22 , pp. 6827-6833
    • Spalding, A.C.1    Watson, R.2    Davis, M.E.3    Kim, A.C.4    Lawrence, T.S.5    Ben-Josef, E.6
  • 93
    • 0026808555 scopus 로고
    • Differential regulation of glycogen synthase kinase-3 beta by protein kinase C isotypes
    • Goode, N., Hughes, K., Woodgett, J.R., Parker, P.J., Differential regulation of glycogen synthase kinase-3 beta by protein kinase C isotypes. J. Biol. Chem. 267:24 (1992), 16878–16882.
    • (1992) J. Biol. Chem. , vol.267 , Issue.24 , pp. 16878-16882
    • Goode, N.1    Hughes, K.2    Woodgett, J.R.3    Parker, P.J.4
  • 96
    • 0032727468 scopus 로고    scopus 로고
    • Proteolytic activation of protein kinase C delta and epsilon by caspase-3 in U937 cells during chemotherapeutic agent-induced apoptosis
    • Koriyama, H., Kouchi, Z., Umeda, T., Saido, T.C., Momoi, T., Ishiura, S., Suzuki, K., Proteolytic activation of protein kinase C delta and epsilon by caspase-3 in U937 cells during chemotherapeutic agent-induced apoptosis. Cell. Signal. 11:11 (1999), 831–838.
    • (1999) Cell. Signal. , vol.11 , Issue.11 , pp. 831-838
    • Koriyama, H.1    Kouchi, Z.2    Umeda, T.3    Saido, T.C.4    Momoi, T.5    Ishiura, S.6    Suzuki, K.7
  • 98
    • 84925669194 scopus 로고    scopus 로고
    • Targeting protein kinase C subtypes in pancreatic cancer
    • Storz, P., Targeting protein kinase C subtypes in pancreatic cancer. Expert. Rev. Anticancer. Ther. 15:4 (2015), 433–438.
    • (2015) Expert. Rev. Anticancer. Ther. , vol.15 , Issue.4 , pp. 433-438
    • Storz, P.1
  • 99
    • 0032721005 scopus 로고    scopus 로고
    • Pharmacology and clinical experience with bryostatin 1: a novel anticancer drug
    • Philip, P.A., Zonder, J.A., Pharmacology and clinical experience with bryostatin 1: a novel anticancer drug. Expert Opin. Investig. Drugs 8:12 (1999), 2189–2199.
    • (1999) Expert Opin. Investig. Drugs , vol.8 , Issue.12 , pp. 2189-2199
    • Philip, P.A.1    Zonder, J.A.2
  • 100
    • 42549158923 scopus 로고    scopus 로고
    • Protein kinase C: a target for therapy in pancreatic cancer
    • El-Rayes, B.F., Ali, S., Philip, P.A., Sarkar, F.H., Protein kinase C: a target for therapy in pancreatic cancer. Pancreas 36:4 (2008), 346–352.
    • (2008) Pancreas , vol.36 , Issue.4 , pp. 346-352
    • El-Rayes, B.F.1    Ali, S.2    Philip, P.A.3    Sarkar, F.H.4
  • 102
    • 0031827507 scopus 로고    scopus 로고
    • Directed antisense therapy confirms the role of protein kinase C-alpha in the tumorigenicity of pancreatic cancer
    • (discussion 223–4)
    • Denham, D.W., Franz, M.G., Denham, W., Zervos, E.E., Gower, W.R. Jr., Rosemurgy, A.S., Norman, J., Directed antisense therapy confirms the role of protein kinase C-alpha in the tumorigenicity of pancreatic cancer. Surgery 124:2 (1998), 218–223 (discussion 223–4).
    • (1998) Surgery , vol.124 , Issue.2 , pp. 218-223
    • Denham, D.W.1    Franz, M.G.2    Denham, W.3    Zervos, E.E.4    Gower, W.R.5    Rosemurgy, A.S.6    Norman, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.