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Volumn 14, Issue 5, 1998, Pages 369-375

Novel membrane-to-nucleus pathways in the regulation of pancreatic acinar cell function

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; ENZYME PRECURSOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; TRANSCRIPTION FACTOR; TRANSFORMING GROWTH FACTOR BETA;

EID: 0031665453     PISSN: 02671379     EISSN: None     Source Type: Journal    
DOI: 10.1097/00001574-199809000-00003     Document Type: Review
Times cited : (1)

References (57)
  • 1
    • 0029821524 scopus 로고    scopus 로고
    • Receptors and signaling in pancreatic acinar cells
    • Miller LJ: Receptors and signaling in pancreatic acinar cells. Curr Opin Gastroenterol 1996, 12:417-422.
    • (1996) Curr Opin Gastroenterol , vol.12 , pp. 417-422
    • Miller, L.J.1
  • 3
    • 0031408388 scopus 로고    scopus 로고
    • Physiology and pathophysiology of apoptosis in epithelial cells of the liver, pancreas, and intestine
    • Jones BA, Gores GJ: Physiology and pathophysiology of apoptosis in epithelial cells of the liver, pancreas, and intestine. Amer J Physiol -Gastrointest & Liver Physiol 1997, 36:G1174-G1188.
    • (1997) Amer J Physiol -Gastrointest & Liver Physiol , vol.36
    • Jones, B.A.1    Gores, G.J.2
  • 4
    • 7344264955 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms underlying the development of pancreatic cancer
    • Edited by Bertino J. New York: Academic Press
    • Urrutia R, DiMagno EP: Cellular and molecular mechanisms underlying the development of pancreatic cancer. In Molecular Biology of Cancer, vol. II. Edited by Bertino J. New York: Academic Press; 1997:1201-1211.
    • (1997) Molecular Biology of Cancer , vol.2 , pp. 1201-1211
    • Urrutia, R.1    DiMagno, E.P.2
  • 5
    • 0030747173 scopus 로고    scopus 로고
    • Pancreatic acinar cell intracellular signaling mechanisms
    • Williams JA: Pancreatic acinar cell intracellular signaling mechanisms. Curr Opin Gastroenterol 1997, 13:369-374.
    • (1997) Curr Opin Gastroenterol , vol.13 , pp. 369-374
    • Williams, J.A.1
  • 6
    • 0030913898 scopus 로고    scopus 로고
    • Stimulus-secretion coupling of pancreatic digestive enzyme secretion
    • Williams JA, Groblewski GE, Ohnishi H, Yule DI: Stimulus-secretion coupling of pancreatic digestive enzyme secretion. Digestion 1997, 58(suppl 1):42-45.
    • (1997) Digestion , vol.58 , Issue.1 SUPPL. , pp. 42-45
    • Williams, J.A.1    Groblewski, G.E.2    Ohnishi, H.3    Yule, D.I.4
  • 7
    • 0031536705 scopus 로고    scopus 로고
    • Novel kinase signaling cascades in pancreatic acinar cells
    • Williams JA, Dabrowski A, Logsdon CD: Novel kinase signaling cascades in pancreatic acinar cells. News Phys Sci 1997, 12:117-121.
    • (1997) News Phys Sci , vol.12 , pp. 117-121
    • Williams, J.A.1    Dabrowski, A.2    Logsdon, C.D.3
  • 8
    • 0030724241 scopus 로고    scopus 로고
    • Exploring the role of homeobox and zinc finger proteins in pancreatic cell proliferation, differentiation, and apoptosis
    • Urrutia R: Exploring the role of homeobox and zinc finger proteins in pancreatic cell proliferation, differentiation, and apoptosis. Int J Pencreatol 1997, 22:1-14.
    • (1997) Int J Pencreatol , vol.22 , pp. 1-14
    • Urrutia, R.1
  • 9
    • 0030964105 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Signals, mechanisms and regulation
    • Nigg EA: Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature 1997, 386:779-787.
    • (1997) Nature , vol.386 , pp. 779-787
    • Nigg, E.A.1
  • 11
    • 0031022752 scopus 로고    scopus 로고
    • RNA polymerase II transcription initiation: A structural view
    • Nikolov DB, Burley SK: RNA polymerase II transcription initiation: a structural view. Proc Natl Acad Sci USA 1997, 94:15-22.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 15-22
    • Nikolov, D.B.1    Burley, S.K.2
  • 12
    • 0031001711 scopus 로고    scopus 로고
    • Mechanisms of transcriptional activation: Differences and similarities between yeast, Drosophila, and man
    • Sauer F, Tjian R: Mechanisms of transcriptional activation: differences and similarities between yeast, Drosophila, and man. Curr Opin Genetics Dev 1997, 7:176-181.
    • (1997) Curr Opin Genetics Dev , vol.7 , pp. 176-181
    • Sauer, F.1    Tjian, R.2
  • 13
    • 0031281363 scopus 로고    scopus 로고
    • Activation and repression of RNA polymerase II transcription in yeast
    • Reece RJ, Platt A: Activation and repression of RNA polymerase II transcription in yeast. Bioessays 1997, 19:1001-1010.
    • (1997) Bioessays , vol.19 , pp. 1001-1010
    • Reece, R.J.1    Platt, A.2
  • 14
    • 0031574071 scopus 로고    scopus 로고
    • A multiplicity of mediators: Alternative forms of transcription complexes communicate with transcriptional regulators
    • Chang MP, Jaehning JA: A multiplicity of mediators: alternative forms of transcription complexes communicate with transcriptional regulators. Nucl Acids Res 1997, 25:4861-4865.
    • (1997) Nucl Acids Res , vol.25 , pp. 4861-4865
    • Chang, M.P.1    Jaehning, J.A.2
  • 15
    • 0031323575 scopus 로고    scopus 로고
    • Classification scheme of eukaryotic transcription factors
    • Wingender E: Classification scheme of eukaryotic transcription factors. Mol Biol 1997, 31:483-497.
    • (1997) Mol Biol , vol.31 , pp. 483-497
    • Wingender, E.1
  • 16
    • 0028172289 scopus 로고
    • TGF-beta 1 influences the relative development of the exocrine and endocrine pancreas in vitro
    • Sanvito F, Herrera PL, Huarte J, Nichols A, Montesano R, Orci L JD, Vassalli JD: TGF-beta 1 influences the relative development of the exocrine and endocrine pancreas in vitro. Development 1994, 120:3451-62. This study evaluated the effect of TGFβ1 on the development of embryonic pancreas cultured in three-dimensional gels of extracellular matrix proteins. The treatment with this growth factor selectively inhibited the development of acinar tissue without affecting the ducts. These results clearly demonstrated a role for TGF-beta-mediated pathways in the regulation of acinar cell proliferation and perhaps differentiation.
    • (1994) Development , vol.120 , pp. 3451-3462
    • Sanvito, F.1    Herrera, P.L.2    Huarte, J.3    Nichols, A.4    Montesano, R.5    Orci, L.J.D.6    Vassalli, J.D.7
  • 17
    • 0029017902 scopus 로고
    • Accumulation of extracellular matrix and developmental dysregulation in the pancreas by transgenic production of transforming growth factor
    • ••]. Futhermore, these experiments also reveal a role for TGFβ pathways in mediating extracellular matrix deposition; a phenomenon commonly observed in pancreatic diseases such as chronic pancreatitis and cancer.
    • (1995) Am J Pathol , vol.147 , pp. 42-52
    • Lee, M.S.1    Gu, D.2    Feng, L.3    Curriden, S.4    Arnush, M.5    Krahl, T.6
  • 18
    • 0342460497 scopus 로고    scopus 로고
    • Expression of a dominant-negative mutant TGF-beta type II receptor in transgenic mice reveals essential roles for TGF-beta in the regulation of growth and differentiation in the exocrine pancreas
    • Bottinger EP, Jakubczak JL, Roberts ISD, Mumy M, Hemmati P, Bagnall K, Merlino G, Wakefield LM: Expression of a dominant-negative mutant TGF-beta type II receptor in transgenic mice reveals essential roles for TGF-beta in the regulation of growth and differentiation in the exocrine pancreas. EMBO J 1997, 16:2621-2633. TGFβ signaling in the pancreas was inactivated in vivo by the expression of a dominant-negative mutant TGFβ receptor type II in transgenic mice. These animals displayed an increased proliferation and altered differentiation of pancreatic acinar cells. These results very elegantly demonstrate that TGFβ1 pathways are antiproliferative for acinar calls and are likely to be involved in the maintenance of a differentiated acinar phenotype.
    • (1997) EMBO J , vol.16 , pp. 2621-2633
    • Bottinger, E.P.1    Jakubczak, J.L.2    Roberts, I.S.D.3    Mumy, M.4    Hemmati, P.5    Bagnall, K.6    Merlino, G.7    Wakefield, L.M.8
  • 20
    • 0031438047 scopus 로고    scopus 로고
    • TGFβ signaling from cell membrane to nucleus through Smad proteins
    • Heldin CH, Miyazono K, Tendijke P: TGFβ signaling from cell membrane to nucleus through Smad proteins. Nature 1997, 390:465-471.
    • (1997) Nature , vol.390 , pp. 465-471
    • Heldin, C.H.1    Miyazono, K.2    Tendijke, P.3
  • 21
    • 0030911104 scopus 로고    scopus 로고
    • The TGFβ family mediator Smad1 is phosphorylated directly and activated by the BMP receptor kinase
    • Kretzschmar M, Liu F, Hata A, Doody J, Massague J: The TGFβ family mediator Smad1 is phosphorylated directly and activated by the BMP receptor kinase. Genes Dev 1997, 11:984-995. This reports characterizes the participation of the Smad1 protein in BPM signaling. BMP receptors activate Smad1 directly via phosphorylation. Phosphorylation of the carboxy-termmal serines of this protein is required for its association with Smad 4, nuclear translocation, and transcriptional activation. Mutation of these serine residues prevents the activation of Smad 1.
    • (1997) Genes Dev , vol.11 , pp. 984-995
    • Kretzschmar, M.1    Liu, F.2    Hata, A.3    Doody, J.4    Massague, J.5
  • 22
    • 0031939744 scopus 로고    scopus 로고
    • Smad5 and Dpc4 are key molecules in mediating BMP-2-induced osteoblastic differentiation of the pluripotent mesenchymal precursor cell fine
    • Nishimura R, Kato Y, Chen D, Harris SE, Mundy GR, Yoneda T: Smad5 and Dpc4 are key molecules in mediating BMP-2-induced osteoblastic differentiation of the pluripotent mesenchymal precursor cell fine. J Biol Chem 1998, 273:1872-1879. This article describes the identification of human Smad5, a protein highly homologous to Smad1. Smad5 associates with the BMP type Ia or Ib receptors in osteoblasts and is phosphorylated by the addition of BMP-2. Following phosphorylation, Smad5 forms a complex with Smad4 which shuttles into the nucleus. Dominant negative forms of Smad4 or Smad4 block the induction of alkaline phosphatase activity and osteocalcin production, which are markers of the BMP-2-induced osteoblasttc differentiation.
    • (1998) J Biol Chem , vol.273 , pp. 1872-1879
    • Nishimura, R.1    Kato, Y.2    Chen, D.3    Harris, S.E.4    Mundy, G.R.5    Yoneda, T.6
  • 23
    • 0030667930 scopus 로고    scopus 로고
    • SmadB mediates the signaling of the receptor serine kinase
    • Chen Y, Bhushan A, Vale W: SmadB mediates the signaling of the receptor serine kinase. Proc Natl Acad Sci USA 1997, 94:12938-12943. This article reports the isolation of the Smad8 cDNA from a rat brain library. The Smad8 protein is phosphorylated by a constitutively active activin-like receptor ALK-2 and associates with Smad4 to activate transcription. Thus, Smad8 is a good candidate to transduce signals from activin-like pathways.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12938-12943
    • Chen, Y.1    Bhushan, A.2    Vale, W.3
  • 24
    • 0030768644 scopus 로고    scopus 로고
    • TGFβ Receptor-mediated signalling through Smad2, Smad3 and Smad4
    • Nakao A, Imamura T, Souchelnytskyi S, Kawabata M, Ishisaki A, Oeda E, et al.: TGFβ Receptor-mediated signalling through Smad2, Smad3 and Smad4. EMBOJ 1997, 16:5353-5362. This article demonstrates the ability of Smad2 and Smad3 to form complexes with Smad4. These complexes translocate from the cytoplasm into the nucleus where they activate transcription.
    • (1997) EMBOJ , vol.16 , pp. 5353-5362
    • Nakao, A.1    Imamura, T.2    Souchelnytskyi, S.3    Kawabata, M.4    Ishisaki, A.5    Oeda, E.6
  • 25
    • 0030690337 scopus 로고    scopus 로고
    • Dual role of the Smad4/Dpc4 tumor suppressor in TGFβ-inducible transcriptional complexes
    • Liu F, Pouponnot C, Massague J: Dual role of the Smad4/Dpc4 tumor suppressor in TGFβ-inducible transcriptional complexes. Genes Dev 1997, 11:3157-3167. This article demonstrates that Smad4 facilitates the binding of a trimeric transcription factor complex formed by Smad2, Smad4, and Fast1 to DNA. In addition, Smad4 provides a transcriptional activation function to this complex. The discovery of this dual function for Smad4 further supports a crucial role for this protein in 7-mediated transcriptional responses.
    • (1997) Genes Dev , vol.11 , pp. 3157-3167
    • Liu, F.1    Pouponnot, C.2    Massague, J.3
  • 26
    • 0030765945 scopus 로고    scopus 로고
    • Smad6 inhibits signalling by the TGFb superfamily
    • Imamura T, Takase M, Nishihara A, Oeda E, Hanai J, Kawabata M, Miyazono K: Smad6 inhibits signalling by the TGFb superfamily. Nature 1997, 389:622-626. A Smad6 encoding cDNA was isolated from a murine lung library. The Smad6 protein associates with the TGFβ receptor I and inhibits the phosphorylation of Smad1 and Smad2 that is necessary for transducing TGFβ- and BMP-mediated signals to the nucleus.
    • (1997) Nature , vol.389 , pp. 622-626
    • Imamura, T.1    Takase, M.2    Nishihara, A.3    Oeda, E.4    Hanai, J.5    Kawabata, M.6    Miyazono, K.7
  • 27
    • 0030611757 scopus 로고    scopus 로고
    • Identification of Smad7, a TGFβ-inducible antagonist of TGF-beta signalling
    • Nakao A, Afrakhte M, Moren A, Nakayama T, Christian JL, Heuchel R, et al.: Identification of Smad7, a TGFβ-inducible antagonist of TGF-beta signalling. Nature 1997, 389:631-635. Smad7 was identified as a result of a homology search of previously identified Smad family members against the expressed sequence tag database. The Smad7 protein associates with the TGFβ receptor complex and inhibits the phosphorylation of Smad2 and Smad3 that occurs upon ligand binding. Transfection of mammalian cell lines with a Smad7 cDNA interfered with TGFβ-mediated signaling, directly demonstrating the important of this protein in transducing TGFβ signals.
    • (1997) Nature , vol.389 , pp. 631-635
    • Nakao, A.1    Afrakhte, M.2    Moren, A.3    Nakayama, T.4    Christian, J.L.5    Heuchel, R.6
  • 29
    • 0029829236 scopus 로고    scopus 로고
    • Identification and characterization of a gene encoding a gut-enriched kruppel-like factor expressed during growth arrest
    • Shields JM, Christy RJ, Tang VW: Identification and characterization of a gene encoding a gut-enriched kruppel-like factor expressed during growth arrest. J Biol Chem 1996, 271:20009-20017.
    • (1996) J Biol Chem , vol.271 , pp. 20009-20017
    • Shields, J.M.1    Christy, R.J.2    Tang, V.W.3
  • 30
    • 0030610532 scopus 로고    scopus 로고
    • Overexpression of the TGF-beta-regulated zinc finger encoding gene, TIEG, induces apoptosis in pancreatic epithelial cells
    • Tachibana I, Imoto M, Adjei PN, Gores GJ, Subramaniam M, Spelsberg TC, Urrutia R: Overexpression of the TGF-beta-regulated zinc finger encoding gene, TIEG, induces apoptosis in pancreatic epithelial cells. J Clin Invest 1997, 99:2365-2374. This article describes the isolation of a cDNA encoding the TGFβ-inducible zinc finger transcription factor TIEG from a pancreatic library. TIEG constitutes the first member of the SP1-like family of proteins shown to be expressed in the exocrine pancreas. The overexpression of a TIEG cDNA in a human pancreatic cell line inhibits cell growth and induces apoptosis.
    • (1997) J Clin Invest , vol.99 , pp. 2365-2374
    • Tachibana, I.1    Imoto, M.2    Adjei, P.N.3    Gores, G.J.4    Subramaniam, M.5    Spelsberg, T.C.6    Urrutia, R.7
  • 31
    • 0031298187 scopus 로고    scopus 로고
    • A nuclear factor other than Sp1 binds the GC-rich promoter of the gene encoding rate poly(DP-ribose) polymerase in vitro
    • Laniel MA, Bergeron MJ, Poirier GG, Guerin SL: A nuclear factor other than Sp1 binds the GC-rich promoter of the gene encoding rate poly(DP-ribose) polymerase in vitro. Biochem Cell Biol 1997, 75:427-434.
    • (1997) Biochem Cell Biol , vol.75 , pp. 427-434
    • Laniel, M.A.1    Bergeron, M.J.2    Poirier, G.G.3    Guerin, S.L.4
  • 32
    • 0031906550 scopus 로고    scopus 로고
    • Signal transduction through NF-kappa-B
    • May MJ, Ghosh S: Signal transduction through NF-kappa-B. Immunol Today 1998, 19:80-88.
    • (1998) Immunol Today , vol.19 , pp. 80-88
    • May, M.J.1    Ghosh, S.2
  • 33
    • 0031126702 scopus 로고    scopus 로고
    • Rel/NF-kappa-B and I-kappa-B proteins: An overview
    • May MJ, Ghosgh S: Rel/NF-kappa-B and I-kappa-B proteins: an overview. Sem Cancer Biol 1997, 8:63-73.
    • (1997) Sem Cancer Biol , vol.8 , pp. 63-73
    • May, M.J.1    Ghosgh, S.2
  • 34
    • 0030923560 scopus 로고    scopus 로고
    • Pancreatic acinar cells produce, release, and respond to tumor necrosis factor-alpha: Role in regulating cell death and pancreatitis
    • Gukovskaya AS, Gukovsky I, Zaninovic V, Song M, Sandoval D, Gukovsky S, Pandol SJ: Pancreatic acinar cells produce, release, and respond to tumor necrosis factor-alpha: role in regulating cell death and pancreatitis. J Clin Invest 1997, 100:1853-1862. This study constitutes the first report of a membrane-to-nucleus apoptotic signal-ing pathway involving TNFα and NFκB in pancreatic acinar cells. Biochemical, molecular, and immunological assays demonstrate that pancreatic acinar cells produce, release, and respond to TNFα. In isolated pancreatic acini, TNFα elicits an apoptotic response that is accompanied by the translocation of NFκB into the nucleus. The in vivo neutralization of TNFα greatly inhibited apoptosis during cerulein-induced pancreatitis, providing compelling evidence for the usefulness of this approach to potentially interfere with the development of pancreatic injury in vivo.
    • (1997) J Clin Invest , vol.100 , pp. 1853-1862
    • Gukovskaya, A.S.1    Gukovsky, I.2    Zaninovic, V.3    Song, M.4    Sandoval, D.5    Gukovsky, S.6    Pandol, S.J.7
  • 35
    • 0030830283 scopus 로고    scopus 로고
    • Gene targeting demonstrates additive detrimental effects of interleukin 1 and tumor necrosis factor during pancreatitis
    • Denham W, Yang J, Fink G, Denham D, Carter G, Ward K, Norman J: Gene targeting demonstrates additive detrimental effects of interleukin 1 and tumor necrosis factor during pancreatitis. Gastroenterology 1997, 113:1741-1746.
    • (1997) Gastroenterology , vol.113 , pp. 1741-1746
    • Denham, W.1    Yang, J.2    Fink, G.3    Denham, D.4    Carter, G.5    Ward, K.6    Norman, J.7
  • 36
    • 0030999560 scopus 로고    scopus 로고
    • Early events in TNFa signaling: A story of association and dissociation
    • Darnay BG, Aggarwal BB: Early events in TNFa signaling: a story of association and dissociation. J Leuk Biol 1997, 61:559-566.
    • (1997) J Leuk Biol , vol.61 , pp. 559-566
    • Darnay, B.G.1    Aggarwal, B.B.2
  • 37
    • 0030730967 scopus 로고    scopus 로고
    • Therapeutic modification of nuclear factor kappa-b binding activity and tumor necrosis factor-alpha gene expression during acute biliary pancreatitis
    • Dunn JA, Li CF, Ha TH, Kao RL, Browder W: Therapeutic modification of nuclear factor kappa-b binding activity and tumor necrosis factor-alpha gene expression during acute biliary pancreatitis. Am Surg 1997, 63:1036-1043. This study assessed the effects of inhibiting NFκB binding activity and tumor necrosis factor TNFα gene expression in the treatment of experimental biliary acute pancreatitis. The induction of biliary pancreatitis was accompanied by an concomitant upregulation in NFκB binding activity and in the levels of TNFα mRNA. The administration of amobarbital blocked the activation of NFκB and the overexpression of TNFα, and resulted in a decrease severity of the pancreatitis.
    • (1997) Am Surg , vol.63 , pp. 1036-1043
    • Dunn, J.A.1    Li, C.F.2    Ha, T.H.3    Kao, R.L.4    Browder, W.5
  • 39
    • 0031126554 scopus 로고    scopus 로고
    • Rel/NF-kappa-B transcription factors and the control of apoptosis
    • Sonenshein GE: Rel/NF-kappa-B transcription factors and the control of apoptosis. Semin Cancer Biol 1997, 8:113-119.
    • (1997) Semin Cancer Biol , vol.8 , pp. 113-119
    • Sonenshein, G.E.1
  • 40
    • 0032477945 scopus 로고    scopus 로고
    • Alterations in NF-kappa-B function in transgenic epithelial tissue demonstrate a growth inhibitor role for NF-kappa-B
    • Seitz CS, Lin Q, Deng H, Khavari PA: Alterations in NF-kappa-B function in transgenic epithelial tissue demonstrate a growth inhibitor role for NF-kappa-B. Proc Natl Acad Sci USA 1998, 95:2307-2312.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2307-2312
    • Seitz, C.S.1    Lin, Q.2    Deng, H.3    Khavari, P.A.4
  • 41
    • 0031990814 scopus 로고    scopus 로고
    • Modulation of transcription factor NF-kappa-B by enantiomers of the nonsteroidal drug ibuprofen
    • Schuren N, Bang H, Munster T, Brune K, Pahl A: Modulation of transcription factor NF-kappa-B by enantiomers of the nonsteroidal drug ibuprofen. Br J Pharmacol 1998, 123:645-652.
    • (1998) Br J Pharmacol , vol.123 , pp. 645-652
    • Schuren, N.1    Bang, H.2    Munster, T.3    Brune, K.4    Pahl, A.5
  • 42
    • 0031982964 scopus 로고    scopus 로고
    • Activation of P38 mitogen-activated protein kinase by sodium salicylate leads to inhibition of tumor necrosis factor-induced I-kappa-B-alpha phosphorylation and degradation
    • Schwenger P, Alpert D, Skolnik EY, Vilcek J: Activation of P38 mitogen-activated protein kinase by sodium salicylate leads to inhibition of tumor necrosis factor-induced I-kappa-B-alpha phosphorylation and degradation. Mol Cell Biol 1998, 18:78-84.
    • (1998) Mol Cell Biol , vol.18 , pp. 78-84
    • Schwenger, P.1    Alpert, D.2    Skolnik, E.Y.3    Vilcek, J.4
  • 43
    • 0031915368 scopus 로고    scopus 로고
    • Sesquiterpene lactones specifically inhibit activation of NF-kappa-B by preventing the degradation of I-kappa-B-alpha and I-kappa-B-beta
    • Hehner SP, Heinrich M, Bork PM, Vogt M, Ratter F, Lehmann V, et al.: Sesquiterpene lactones specifically inhibit activation of NF-kappa-B by preventing the degradation of I-kappa-B-alpha and I-kappa-B-beta. J Biol Chem 1998, 273:1288-1297.
    • (1998) J Biol Chem , vol.273 , pp. 1288-1297
    • Hehner, S.P.1    Heinrich, M.2    Bork, P.M.3    Vogt, M.4    Ratter, F.5    Lehmann, V.6
  • 44
    • 0032032469 scopus 로고    scopus 로고
    • Surfasalazine: A potent and specific inhibitor of nuclear factor kappa B
    • Wahl C, Liptay S, Adler G, Schmid RM: Surfasalazine: a potent and specific inhibitor of nuclear factor kappa B. J Clin Invest 1998, 101:1163-1174.
    • (1998) J Clin Invest , vol.101 , pp. 1163-1174
    • Wahl, C.1    Liptay, S.2    Adler, G.3    Schmid, R.M.4
  • 45
    • 0030972807 scopus 로고    scopus 로고
    • Transcriptional regulation by cyclic AMP
    • Montiminy M: Transcriptional regulation by cyclic AMP. Ann Rev Biochem 1997, 66:807-822.
    • (1997) Ann Rev Biochem , vol.66 , pp. 807-822
    • Montiminy, M.1
  • 48
    • 0031739577 scopus 로고    scopus 로고
    • Analysis of molecular mechanisms controlling neuroendocrine cell specific transcription of the chromogranin a gene
    • Canaff L, Bevan S, Wheller DG, Mouland AJ, Rehfuss RP, White JH, Hendy GN: Analysis of molecular mechanisms controlling neuroendocrine cell specific transcription of the chromogranin A gene. Endocrinology 1998, 139:1184-1196.
    • (1998) Endocrinology , vol.139 , pp. 1184-1196
    • Canaff, L.1    Bevan, S.2    Wheller, D.G.3    Mouland, A.J.4    Rehfuss, R.P.5    White, J.H.6    Hendy, G.N.7
  • 49
    • 0030726539 scopus 로고    scopus 로고
    • Dominant-negative Creb inhibits tumor growth and metastasis of human melanoma cells
    • Xie SH, Price JE, Luca M, Jean D, Ronai Z, Bareli M: Dominant-negative Creb inhibits tumor growth and metastasis of human melanoma cells. Oncogene 1997, 15:2069-2075.
    • (1997) Oncogene , vol.15 , pp. 2069-2075
    • Xie, S.H.1    Price, J.E.2    Luca, M.3    Jean, D.4    Ronai, Z.5    Bareli, M.6
  • 50
    • 0032478276 scopus 로고    scopus 로고
    • Creb-binding protein cooperates with transcription factor Gata-1 and is required for erythroid differentiation
    • Blobel GA, Nakajima T, Eckner R, Montminy M, Orkin SH: Creb-binding protein cooperates with transcription factor Gata-1 and is required for erythroid differentiation. Proc Natl Acad Sci USA 1998, 95:2061-2066.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2061-2066
    • Blobel, G.A.1    Nakajima, T.2    Eckner, R.3    Montminy, M.4    Orkin, S.H.5
  • 52
    • 0030973579 scopus 로고    scopus 로고
    • Transcription factors of the NFAT family: Regulation and function
    • Rao A, Luo C, Hogan PG: Transcription factors of the NFAT family: regulation and function. Ann Rev Imm 1997, 15:707-747.
    • (1997) Ann Rev Imm , vol.15 , pp. 707-747
    • Rao, A.1    Luo, C.2    Hogan, P.G.3
  • 53
    • 0029983229 scopus 로고    scopus 로고
    • Induction of NFAT-mediated transcription by G(q)-coupled receptors in lymphoid and non-lymphoid cells
    • Talpade DJ, Murphy TJ: Induction of NFAT-mediated transcription by G(q)-coupled receptors in lymphoid and non-lymphoid cells. J Biol Chem 1996, 271:10429-10432.
    • (1996) J Biol Chem , vol.271 , pp. 10429-10432
    • Talpade, D.J.1    Murphy, T.J.2
  • 54
    • 0029053852 scopus 로고
    • Isolation of two new members of the NF-AT gene family and functional characterization of the NF-AT proteins
    • Hoey T, Sun YL, Williamson K, Xu X: Isolation of two new members of the NF-AT gene family and functional characterization of the NF-AT proteins. Immunity 1995, 2:461-72.
    • (1995) Immunity , vol.2 , pp. 461-472
    • Hoey, T.1    Sun, Y.L.2    Williamson, K.3    Xu, X.4
  • 55
    • 0024411240 scopus 로고
    • Identification of a cell-specific DNA-binding activity that interacts with a transcriptional activator of genes expressed in the acinar pancreas
    • Cockell M, Stevenson BJ, Strubin M, Hagenbuchle O, Wellauer PK: Identification of a cell-specific DNA-binding activity that interacts with a transcriptional activator of genes expressed in the acinar pancreas. Mol Cell Biol 1989, 9:2464-2476.
    • (1989) Mol Cell Biol , vol.9 , pp. 2464-2476
    • Cockell, M.1    Stevenson, B.J.2    Strubin, M.3    Hagenbuchle, O.4    Wellauer, P.K.5
  • 56
    • 0029737816 scopus 로고    scopus 로고
    • The P48 DNA-binding subunit of transcription factor PTF1 is a new exocrine pancreas-specific basic helix-loop-helix protein
    • Krapp A, Knofler M, Fruitiger S, Hughes GJ, Hagenbuchle O, Wellauer PK: The P48 DNA-binding subunit of transcription factor PTF1 is a new exocrine pancreas-specific basic helix-loop-helix protein. EMBO J 1996, 15:4317-4329. This study reports the isolation of cDNA encoding the p48 subunit of the transcription factor PTF1. Sequence analysis demonstrates that p48 is a novel member of the helix-loop-helix family of the developmental regulators. In situ hybridization experiments reveal that p48 is specifically expressed in the embryonic and adult exocrine pancreas. A reduction in the levels of the p48 mRNA in AR42J cells using antisense technology results in a decreased expression of several pancreatic digestive enzymes. Thus, together these studies demonstrate that distinct tissue-specific transcription factors can regulate the production of secretory products in acinar cells. A role for this factor in determining and maintaining the differentiation of acinar cells is also proposed.
    • (1996) EMBO J , vol.15 , pp. 4317-4329
    • Krapp, A.1    Knofler, M.2    Fruitiger, S.3    Hughes, G.J.4    Hagenbuchle, O.5    Wellauer, P.K.6
  • 57
    • 0029831032 scopus 로고    scopus 로고
    • Constitutive expression of the gene for the cell-specific P48 DNA-bindings subunit of pancreas transcription factor 1 in cultured cells is under control of binding sites for transcription factors Sp1 and alpha-Cbf
    • Knofler M, Krapp A, Hagenbuchle P, Wellauer PK: Constitutive expression of the gene for the cell-specific P48 DNA-bindings subunit of pancreas transcription factor 1 in cultured cells is under control of binding sites for transcription factors Sp1 and alpha-Cbf. J Biol Chem 1996, 271:21993-22002.
    • (1996) J Biol Chem , vol.271 , pp. 21993-22002
    • Knofler, M.1    Krapp, A.2    Hagenbuchle, P.3    Wellauer, P.K.4


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