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Volumn 49, Issue 10, 2004, Pages 1664-1671

Taurodeoxycholate stimulates intestinal cell proliferation and protects against apoptotic cell death through activation of NF-κB

Author keywords

apoptosis; bile salts; enterocyte; NF B; proliferation

Indexed keywords

BILE SALT; I KAPPA B; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; TAURODEOXYCHOLIC ACID; TUMOR NECROSIS FACTOR ALPHA;

EID: 4944267762     PISSN: 01632116     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:DDAS.0000043383.96077.99     Document Type: Article
Times cited : (34)

References (43)
  • 1
    • 0028174061 scopus 로고
    • Function and activation of NF-κB in the immune system
    • Baeuerle PA, Henkle P: Function and activation of NF-κB in the immune system. Annu Rev Immunol 12:141-179, 1994
    • (1994) Annu Rev Immunol , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkle, P.2
  • 2
    • 0030615201 scopus 로고    scopus 로고
    • Nuclear factor-κB, a pivotal transcription factor in chronic inflammatory diseases
    • Barnes PJ, Karin M: Nuclear factor-κB, a pivotal transcription factor in chronic inflammatory diseases. N Engl J Med 336:1066-1071, 1997
    • (1997) N Engl J Med , vol.336 , pp. 1066-1071
    • Barnes, P.J.1    Karin, M.2
  • 3
    • 17544365995 scopus 로고    scopus 로고
    • The IκB/NF-κB system: A key determinant of mucosal inflammation and protection
    • Jobin C, Sartor RB: The IκB/NF-κB system: A key determinant of mucosal inflammation and protection. Cell Physiol 278:451-462, 2000
    • (2000) Cell Physiol , vol.278 , pp. 451-462
    • Jobin, C.1    Sartor, R.B.2
  • 4
    • 0028986075 scopus 로고
    • Control of IκBα proteolysis by site-specific, signal-induced phosphrylation
    • Brown KS, Gerstberger L, Carlson G, et al.: Control of IκBα proteolysis by site-specific, signal-induced phosphrylation. Science 267:1485-1488, 1995
    • (1995) Science , vol.267 , pp. 1485-1488
    • Brown, K.S.1    Gerstberger, L.2    Carlson, G.3
  • 5
    • 0027207242 scopus 로고
    • Tumor necrosis factor and interleukin-1 lead to phosphorylation and loss of IκBα: A mechanism for NF-κB activation
    • Beg AA, Finco TS, Nantermet PV, et al.: Tumor necrosis factor and interleukin-1 lead to phosphorylation and loss of IκBα: A mechanism for NF-κB activation. Mol Cell Biol 13:3301-3310, 1993
    • (1993) Mol Cell Biol , vol.13 , pp. 3301-3310
    • Beg, A.A.1    Finco, T.S.2    Nantermet, P.V.3
  • 6
    • 0031285250 scopus 로고    scopus 로고
    • Activation of the IκBα kinase complex by MEKK1, a kinase of the JNK pathway
    • Lee FS, Hagler J, Chen ZJ, et al.: Activation of the IκBα kinase complex by MEKK1, a kinase of the JNK pathway. Cell 88:213-222, 1997
    • (1997) Cell , vol.88 , pp. 213-222
    • Lee, F.S.1    Hagler, J.2    Chen, Z.J.3
  • 7
    • 0030685825 scopus 로고    scopus 로고
    • IKK-1 and IKK-2: Cytokine-activated IκB kinases essential for NF-κB activation
    • Mercurio FH, Zhu BW, Murray A, et al.; IKK-1 and IKK-2: Cytokine-activated IκB kinases essential for NF-κB activation. Science 278:860-866, 1997
    • (1997) Science , vol.278 , pp. 860-866
    • Mercurio, F.H.1    Zhu, B.W.2    Murray, A.3
  • 8
    • 0028986194 scopus 로고
    • IκBβ regulates the persistent response in a biphasic activation of NF-κB
    • Thompson JE, Phillips RJ, Erdjument-Bromage H, et al.: IκBβ regulates the persistent response in a biphasic activation of NF-κB. Cell 80:573-582, 1995
    • (1995) Cell , vol.80 , pp. 573-582
    • Thompson, J.E.1    Phillips, R.J.2    Erdjument-Bromage, H.3
  • 9
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-κB in preventing TNF-α-induced cell death
    • Beg AA, Baltimore D: An essential role for NF-κB in preventing TNF-α-induced cell death. Science 274:782-784, 1996
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 10
    • 0032577979 scopus 로고    scopus 로고
    • Supperssion of steady-state, but not stimulus induced, NF-κB activity inhibits alphavirus-induced apoptosis
    • Lin K-I, DiDonato JA, Hoffman A, Hardwick JM, Ratan RR: Supperssion of steady-state, but not stimulus induced, NF-κB activity inhibits alphavirus-induced apoptosis. J Cell Biol 141:1479-1487, 1998
    • (1998) J Cell Biol , vol.141 , pp. 1479-1487
    • Lin, K.-I.1    DiDonato, J.A.2    Hoffman, A.3    Hardwick, J.M.4    Ratan, R.R.5
  • 11
    • 0031938280 scopus 로고    scopus 로고
    • Nuclear factor-κB contributes to excitotoxin-induced apoptosis in rat striatum
    • Qin ZH, Wang Y, Nakai M, Chase TN: Nuclear factor-κB contributes to excitotoxin-induced apoptosis in rat striatum. Mol Pharmacol 53:33-42, 1998
    • (1998) Mol Pharmacol , vol.53 , pp. 33-42
    • Qin, Z.H.1    Wang, Y.2    Nakai, M.3    Chase, T.N.4
  • 13
    • 0035026932 scopus 로고    scopus 로고
    • NF-κB activation and susceptibility to apoptosis after polyamine depletion in intestinal epitelial cells
    • Li L, Rao JN, Bass BL, and Wang J-Y: NF-κB activation and susceptibility to apoptosis after polyamine depletion in intestinal epitelial cells. Am J Physiol Gastrointest Liver Phsyiol 280:G992-G1004, 2001
    • (2001) Am J Physiol Gastrointest Liver Phsyiol , vol.280
    • Li, L.1    Rao, J.N.2    Bass, B.L.3    Wang, J.-Y.4
  • 14
    • 0029059060 scopus 로고
    • Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-κB
    • Beg AA, Sha WC, Bronson RT, Ghosh S, Baltimore D: Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-κB. Nature 376:167-170, 1995
    • (1995) Nature , vol.376 , pp. 167-170
    • Beg, A.A.1    Sha, W.C.2    Bronson, R.T.3    Ghosh, S.4    Baltimore, D.5
  • 16
    • 0027209224 scopus 로고
    • Decreased expression of protooncogenes c-fos, c-myc and c-jun following polyamine depletion in IEC-6 cells
    • Gastrointest Liver Physiol 30
    • Wang, J-Y, McCormack SA, Viar MJ, et al.: Decreased expression of protooncogenes c-fos, c-myc and c-jun following polyamine depletion in IEC-6 cells. Am J Physiol 265 (Gastrointest Liver Physiol 30):G331-G338, 1993
    • (1993) Am J Physiol , vol.265
    • Wang, J.-Y.1    McCormack, S.A.2    Viar, M.J.3
  • 17
    • 0026691240 scopus 로고
    • The A20 zinc finger protein protects cells from tumor necrosis factor cytotoxicity
    • Opipari AW jr, Hu HM, Yabknoitz R, Dixit VM: The A20 zinc finger protein protects cells from tumor necrosis factor cytotoxicity. J Biol Chem 267:12424-12427, 1992
    • (1992) J Biol Chem , vol.267 , pp. 12424-12427
    • Opipari Jr., A.W.1    Hu, H.M.2    Yabknoitz, R.3    Dixit, V.M.4
  • 18
    • 0037975615 scopus 로고    scopus 로고
    • NF-κB regulates intestinal epithelial cell and bile salt induced migration after injury
    • Strauch ED, Bass BL, Rao JN, Vann JA, Wang J-Y: NF-κB regulates intestinal epithelial cell and bile salt induced migration after injury. Ann Surg 237:494-501, 2003
    • (2003) Ann Surg , vol.237 , pp. 494-501
    • Strauch, E.D.1    Bass, B.L.2    Rao, J.N.3    Vann, J.A.4    Wang, J.-Y.5
  • 19
    • 0022336367 scopus 로고
    • Effect of luminal contents on postresectional longtiduninal and mucosal growth in the ileum of suckling rats
    • Ford WD, de Vries JE, Ross JS, Malt RA: Effect of luminal contents on postresectional longtiduninal and mucosal growth in the ileum of suckling rats. Surgery 98:935-941, 1985
    • (1985) Surgery , vol.98 , pp. 935-941
    • Ford, W.D.1    De Vries, J.E.2    Ross, J.S.3    Malt, R.A.4
  • 20
    • 0034220901 scopus 로고    scopus 로고
    • Effect of the distal remnant on ileal adaptation
    • Thompson JS, Ferguson DC: Effect of the distal remnant on ileal adaptation. J Gastrointest Surg 4:430-434, 2000
    • (2000) J Gastrointest Surg , vol.4 , pp. 430-434
    • Thompson, J.S.1    Ferguson, D.C.2
  • 21
    • 0016708813 scopus 로고
    • The effect of bile and of sodium taurocholate on the epithelial cell dynamics of the rat small intestine
    • Roy CC, Laurendeau G, Doyon G, Chartran L, Rivest MR: The effect of bile and of sodium taurocholate on the epithelial cell dynamics of the rat small intestine. Proc Soc Exp Biol Med 149:1000-1004, 1975
    • (1975) Proc Soc Exp Biol Med , vol.149 , pp. 1000-1004
    • Roy, C.C.1    Laurendeau, G.2    Doyon, G.3    Chartran, L.4    Rivest, M.R.5
  • 22
    • 0017867076 scopus 로고
    • Contributions of bile and pancreatic juice to cell proliferation in ileal mucosa
    • Williamson RC, Bauer FL, Ross JS, Malt RA: Contributions of bile and pancreatic juice to cell proliferation in ileal mucosa. Surgery 83:570-576, 1978
    • (1978) Surgery , vol.83 , pp. 570-576
    • Williamson, R.C.1    Bauer, F.L.2    Ross, J.S.3    Malt, R.A.4
  • 23
    • 0020595095 scopus 로고
    • The role of pancreatico-biliary secretions in intestinal adaptation after resection, and its relationship to plasma enteroglucagon
    • Al-Mukhtar MY, Sagor GR, Ghatei MA, Bloom SR, Wright NA: The role of pancreatico-biliary secretions in intestinal adaptation after resection, and its relationship to plasma enteroglucagon. Br J Surg 70:398-400, 1983
    • (1983) Br J Surg , vol.70 , pp. 398-400
    • Al-Mukhtar, M.Y.1    Sagor, G.R.2    Ghatei, M.A.3    Bloom, S.R.4    Wright, N.A.5
  • 25
    • 0023644777 scopus 로고
    • Cell- and sequence-specific binding of nuclear protein to 5′-flanking DNA of the rat growth hormone gene
    • Ye ZS, Samuels HH: Cell- and sequence-specific binding of nuclear protein to 5′-flanking DNA of the rat growth hormone gene. J Biol Chem 262:6313-6317, 1987
    • (1987) J Biol Chem , vol.262 , pp. 6313-6317
    • Ye, Z.S.1    Samuels, H.H.2
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the priciple of protein-dye binding
    • Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the priciple of protein-dye binding. Anal Biochem 72:248-254, 1976
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685, 1970
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0028559768 scopus 로고
    • An efficient and flexible system for construction of adenovirus vectors with insertion of deletions in regions 1 and 3
    • Bett AJ, Haddara L, Prevec L, Graham FL: An efficient and flexible system for construction of adenovirus vectors with insertion of deletions in regions 1 and 3. Proc Natl Acad Sci USA 91:8802-8806, 1994
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8802-8806
    • Bett, A.J.1    Haddara, L.2    Prevec, L.3    Graham, F.L.4
  • 31
    • 0000525434 scopus 로고
    • Intestinal absorption of bile acids and biliary constituents
    • Hoffman AF: Intestinal absorption of bile acids and biliary constituents Physiol Gastrointest Tract 2:1845-1865, 1994
    • (1994) Physiol Gastrointest Tract , vol.2 , pp. 1845-1865
    • Hoffman, A.F.1
  • 32
    • 0030904110 scopus 로고    scopus 로고
    • Bile acid concentrations in serum and duodenal aspirates of healthy and preterm infants: Effects of gestational and postnatal age
    • Boehm G, Braun W, Moro G, Minoli I: Bile acid concentrations in serum and duodenal aspirates of healthy and preterm infants: Effects of gestational and postnatal age. Biol Neonate 71:207-214, 1997
    • (1997) Biol Neonate , vol.71 , pp. 207-214
    • Boehm, G.1    Braun, W.2    Moro, G.3    Minoli, I.4
  • 33
    • 0030844964 scopus 로고    scopus 로고
    • The effect of oral sodium taurocholate on endotoxemia and intestinal anastomotic wound healing in rats with obstructive jaundice
    • Sayan M, Alponat A, Yavus N, Altinkaya E, Goksel S, Sariyar M: The effect of oral sodium taurocholate on endotoxemia and intestinal anastomotic wound healing in rats with obstructive jaundice. Surg Today 27:953-957, 1997
    • (1997) Surg Today , vol.27 , pp. 953-957
    • Sayan, M.1    Alponat, A.2    Yavus, N.3    Altinkaya, E.4    Goksel, S.5    Sariyar, M.6
  • 34
    • 0032508414 scopus 로고    scopus 로고
    • NF-κB antiapoptosis; Induction of TRAF1 and TRAF2 and c-IAP2 to suppress caspase-8 activation
    • Wang CY, Mayo MW, Korneluk RG, Goeddel DV, Baldwin DV Jr: NF-κB antiapoptosis; Induction of TRAF1 and TRAF2 and C-IAP2 to suppress caspase-8 activation. Science 281:1680-1683, 1998
    • (1998) Science , vol.281 , pp. 1680-1683
    • Wang, C.Y.1    Mayo, M.W.2    Korneluk, R.G.3    Goeddel, D.V.4    Baldwin Jr., D.V.5
  • 35
    • 0029949257 scopus 로고    scopus 로고
    • TNF-dependent recruitment of the protein kinase RIP to the TNF receptor I signaling complex
    • Hsu H, Huang J, Shu HB, et al.: TNF-dependent recruitment of the protein kinase RIP to the TNF receptor I signaling complex. Immunity 4:387-396, 1996
    • (1996) Immunity , vol.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.B.3
  • 36
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF-2 and TRAD-FADD interactions define two distinct TNF receptor signal transduction pathways
    • Hsu H, Shu HB, Pan MG, et al.: TRADD-TRAF-2 and TRAD-FADD interactions define two distinct TNF receptor signal transduction pathways. Cell 84:299-308, 1996
    • (1996) Cell , vol.84 , pp. 299-308
    • Hsu, H.1    Shu, H.B.2    Pan, M.G.3
  • 37
    • 0032524335 scopus 로고    scopus 로고
    • MYD88, and adaptor protein involved in interleukin-1 signaling
    • Burns K, Martinon F, Esslinger C, et al.: MYD88, and adaptor protein involved in interleukin-1 signaling. J Biol Chem 273:12203-12209, 1998
    • (1998) J Biol Chem , vol.273 , pp. 12203-12209
    • Burns, K.1    Martinon, F.2    Esslinger, C.3
  • 38
    • 0029865142 scopus 로고    scopus 로고
    • IRAK: A kinase associated with the interleukin-1 receptor
    • Cao Z, Henzel WJ, Gao X: IRAK: A kinase associated with the interleukin-1 receptor. Science 271:1128-1131, 1996
    • (1996) Science , vol.271 , pp. 1128-1131
    • Cao, Z.1    Henzel, W.J.2    Gao, X.3
  • 39
    • 0029761275 scopus 로고    scopus 로고
    • TRAF6 is a signal transductor for interleukin-1
    • Cao Z, Xiong J, Takeuchi M, et al.: TRAF6 is a signal transductor for interleukin-1. Nature 383:443-446, 1996
    • (1996) Nature , vol.383 , pp. 443-446
    • Cao, Z.1    Xiong, J.2    Takeuchi, M.3
  • 40
    • 0031423761 scopus 로고    scopus 로고
    • MYD88: An adaptor that recruits IRAK to the IL-1 receptor complex
    • Wesche H, Henzel WJ, Shillinglaw W, et al.: MYD88: An adaptor that recruits IRAK to the IL-1 receptor complex. Immunity 7:837-847, 1997
    • (1997) Immunity , vol.7 , pp. 837-847
    • Wesche, H.1    Henzel, W.J.2    Shillinglaw, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.