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Volumn 46, Issue 3, 2014, Pages 565-573

Regulation of intestinal mucosal growth by amino acids

Author keywords

Antizyme; Apoptosis; Asparagine; Glutamine; Mucosal cell proliferation; Polyamines

Indexed keywords

AMINO ACID; ANTIZYME; ASPARAGINE; AURORA A KINASE; CAMPTOTHECIN; CYCLIN D1; EFLORNITHINE; GLUTAMINE; LYSINE; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 2; ORNITHINE; ORNITHINE DECARBOXYLASE INHIBITOR; POLYAMINE; PUTRESCINE; RAPAMYCIN; SMAD1 PROTEIN; VALINE; ORNITHINE DECARBOXYLASE; PROTEIN;

EID: 84896314562     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-013-1565-2     Document Type: Short Survey
Times cited : (25)

References (53)
  • 1
    • 0015253193 scopus 로고
    • Protein synthesis in intestinal mucosa: The effect of route of administration of precursor amino acids
    • Alpers DH (1972) Protein synthesis in intestinal mucosa: the effect of route of administration of precursor amino acids. J Clin Invest 51:167-173
    • (1972) J Clin Invest , vol.51 , pp. 167-173
    • Alpers, D.H.1
  • 2
    • 0028356034 scopus 로고
    • Supplemental alanylglutamine, organ growth, and nitrogen metabolism in neonatal pigs fed by total parenteral nutrition
    • Burrin DG, Shulman RJ, Langston C, Storm MC (1994) Supplemental alanyl glutamine, organ growth and nitrogen metabolism in neonatal pigs fed by total parenteral nutrition. J Parenter Enteral Nutr 18:313-319 (Pubitemid 24222345)
    • (1994) Journal of Parenteral and Enteral Nutrition , vol.18 , Issue.4 , pp. 313-319
    • Burrin, D.G.1    Shulman, R.J.2    Langston, C.3    Storm, M.C.4
  • 3
    • 0017743914 scopus 로고
    • Enzyme regulation in neuroblastoma cells in a salts-glucose medium: Induction of ornithine decarboxylase by asparagine and glutamine
    • Chen KY, Canellakis ES (1977) Enzyme regulation in neuroblastoma cells in a salts-glucose medium: induction of ornithine decarboxylase by asparagine and glutamine. Proc Natl Acad Sci USA 74:3791-3795
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 3791-3795
    • Chen, K.Y.1    Canellakis, E.S.2
  • 4
    • 0017710205 scopus 로고
    • "Luminal nutrition" versus "functional workload" as controllers of mucosal morphology and epithelial replacement in the rat small intestine
    • Clarke RM (1977) "Luminal nutrition" versus "functional workload" as controllers of mucosal morphology and epithelial replacement in the rat small intestine. Digestion 15:411-412
    • (1977) Digestion , vol.15 , pp. 411-412
    • Clarke, R.M.1
  • 7
    • 77950430911 scopus 로고    scopus 로고
    • The antiapoptotic delta Np73 is degraded in a c-Jun-dependent manner upon genotoxic stress through the antizyme-mediated pathway
    • Dulloo I, Gopalan G, Melino G, Sabapathy K (2010) The antiapoptotic delta Np73 is degraded in a c-Jun-dependent manner upon genotoxic stress through the antizyme-mediated pathway. Proc Natl Acad Sci USA 107:4902-4917
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 4902-4917
    • Dulloo, I.1    Gopalan, G.2    Melino, G.3    Sabapathy, K.4
  • 8
    • 0015244131 scopus 로고
    • The control of ornithine decarboxylase activity during liver regeneration
    • Fausto N (1971) The control of ornithine decarboxylase activity during liver regeneration. Biochim Biophys Acta 238:116-128
    • (1971) Biochim Biophys Acta , vol.238 , pp. 116-128
    • Fausto, N.1
  • 9
    • 0035881620 scopus 로고    scopus 로고
    • Targeted antizyme expression in the skin of transgenic mice reduces tumor promoter induction of ornithine decarboxylase and decreases sensitivity to chemical carcinogenesis
    • Feith DJ, Shantz LM, Pegg AE (2001) Targeted antizyme expression in the skin of transgenic mice reduces tumor promoter induction of ornithine decarboxylase and decreases sensitivity to chemical carcinogenesis. Cancer Res 61:6073-6081 (Pubitemid 32762542)
    • (2001) Cancer Research , vol.61 , Issue.16 , pp. 6073-6081
    • Feith, D.J.1    Shantz, L.M.2    Pegg, A.E.3
  • 10
    • 0041853847 scopus 로고    scopus 로고
    • Antizyme overexpression in transgenic mice reduces cell proliferation, increases apoptosis, and reduces N-nitrosomethylbenzylamine-induced forestomach carcinogenesis
    • Fong LYY, Feith DJ, Pegg AE (2003) Antizyme over expression in transgenic mice reduces cell proliferation, increases apoptosis, and reduces N -nitrosomethylbenzylamide-induced forestomach carcinogenesis. Cancer Res 63:3945-3954 (Pubitemid 36917910)
    • (2003) Cancer Research , vol.63 , Issue.14 , pp. 3945-3954
    • Fong, L.Y.Y.1    Feith, D.J.2    Pegg, A.E.3
  • 12
    • 0345955882 scopus 로고
    • Induction of a protein inhibitor to ornithine decarboxylase by the end products of its reaction
    • Heller JS, Fong WF, Canellakis ES (1976) Induction of a protein inhibitor to ornithine decarboxylase by the end products of its reaction. Proc Natl Acad Sci USA 73:1858-1862
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 1858-1862
    • Heller, J.S.1    Fong, W.F.2    Canellakis, E.S.3
  • 14
    • 0014546292 scopus 로고
    • Protein starvation and the small intestine. III. Incorporation of orally and intraperitoneally administered L-leucine 4,55-3H into intestinal protein of protein-deprived rats
    • Hirschfield JS, Kern F (1969) Protein starvation and the small intestine. III. Incorporation of orally and intraperitoneally administered L-leucine 4,55-3H into intestinal protein of protein-deprived rats. J Clin Invest 48:1224-1229
    • (1969) J Clin Invest , vol.48 , pp. 1224-1229
    • Hirschfield, J.S.1    Kern, F.2
  • 15
    • 0016171980 scopus 로고
    • Effect of growth conditions on the activity of ornithine decarboxylase in cultured hepatoma cells: I. Effect of amino acid supply
    • Hogan BLM, Murden S (1974) Effect of growth conditions on the activity of ornithine decarboxylase in cultured hepatoma cells: I. Effect of amino acid supply. J Cell Physiol 83:345-352
    • (1974) J Cell Physiol , vol.83 , pp. 345-352
    • Hogan, B.L.M.1    Murden, S.2
  • 16
    • 7944235758 scopus 로고    scopus 로고
    • Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
    • DOI 10.1038/ncb1183
    • Jacinto E, Loewith R, Schmidt A, Liu S, Ruegg MA, Hall A, Hall MN (2004) Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive. Nat Cell Biol 6:1122-1128 (Pubitemid 39468014)
    • (2004) Nature Cell Biology , vol.6 , Issue.11 , pp. 1122-1128
    • Jacinto, E.1    Loewith, R.2    Schmidt, A.3    Lin, S.4    Ruegg, M.A.5    Hall, A.6    Hall, M.N.7
  • 17
    • 0013503139 scopus 로고
    • Effect of luminal nutrition on intestinal adaptation following Thiry-Vella bypass in the dog
    • Jacobs LR, Taylor BR, Dowling RH (1975) Effect of luminal nutrition on intestinal adaptation following Thiry-Vella bypass in the dog. Clin Sci Mol Med 49:26
    • (1975) Clin Sci Mol Med , vol.49 , pp. 26
    • Jacobs, L.R.1    Taylor, B.R.2    Dowling, R.H.3
  • 18
    • 0000941353 scopus 로고
    • Regulation of gastrointestinal mucosal growth
    • Johnson LR (ed) 3rd edn. Raven, New York
    • Johnson LR, McCormack SA (1994) Regulation of gastrointestinal mucosal growth. In: Johnson LR (ed) Physiology of the gastrointestinal tract, 3rd edn. Raven, New York, pp 611-642
    • (1994) Physiology of the Gastrointestinal Tract , pp. 611-642
    • Johnson, L.R.1    McCormack, S.A.2
  • 19
    • 78649648081 scopus 로고    scopus 로고
    • Antizyme restrains centrosome amplification by regulating the accumulation of Mps1 at centrosomes
    • Kasbek C, Yang CH, Fisk HA (2010) Antizyme restrains centrosome amplification by regulating the accumulation of Mps1 at centrosomes. Mol Biol Cell 21:3878-3889
    • (2010) Mol Biol Cell , vol.21 , pp. 3878-3889
    • Kasbek, C.1    Yang, C.H.2    Fisk, H.A.3
  • 20
    • 49649144250 scopus 로고
    • Ornithine decarboxylase in phytohaemagglutinin stimulated lymphocytes: Control of degradation by amino acids
    • Kay JE, Lindsay VJ, Cooke A (1972) Ornithine decarboxylase in phytohaemagglutinin stimulated lymphocytes: control of degradation by amino acids. FEBS Lett 21:123-126
    • (1972) FEBS Lett , vol.21 , pp. 123-126
    • Kay, J.E.1    Lindsay, V.J.2    Cooke, A.3
  • 21
    • 0026667106 scopus 로고
    • Regulated degradation of ornithine decarboxylase requires interaction with the polyamine-inducible protein antizyme
    • Li X, Coffino P (1992) Regulated degradation of ornithine decarboxylase requires interaction with the polyamine-inducible protein antizyme. Mol Cell Biol 12:3556-3562
    • (1992) Mol Cell Biol , vol.12 , pp. 3556-3562
    • Li, X.1    Coffino, P.2
  • 22
    • 35348851301 scopus 로고    scopus 로고
    • Antizyme1 mediates AURKAIP1-dependent degradation of Aurora-A
    • DOI 10.1038/sj.onc.1210482, PII 1210482
    • Lim SK, Gopalan G (2007) Antizyme mediates AURKA1P1-dependent degradation of Aurora-A. Oncogene 26:6593-6603 (Pubitemid 47573681)
    • (2007) Oncogene , vol.26 , Issue.46 , pp. 6593-6603
    • Lim, S.K.1    Gopalan, G.2
  • 24
    • 6944246205 scopus 로고    scopus 로고
    • Multiple stress signals induce p73beta accumulation
    • DOI 10.1593/neo.04205
    • Lin KW, Nam SY, Toh WH, Dulloo I, Sabapathy K (2004) Multiple stress signals induce p73 beta accumulation. Neoplasia 6:546-557 (Pubitemid 39411092)
    • (2004) Neoplasia , vol.6 , Issue.5 , pp. 546-557
    • Kai, W.L.1    Shin, Y.N.2    Wen, H.T.3    Dulloo, I.4    Sabapathy, K.5
  • 27
    • 0028016495 scopus 로고
    • Ornithine decarboxylase is a mediator of c-Myc-induced apoptosis
    • Packham G, Cleveland JL (1994) Ornithine decarboxylase is a mediator of c-Myc induced apoptosis. Mol Cell Biol 14:5741-5747 (Pubitemid 24264402)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.9 , pp. 5741-5747
    • Packham, G.1    Cleveland, J.L.2
  • 28
    • 33744951504 scopus 로고    scopus 로고
    • Regulation of ornithine decarboxylase
    • Pegg AE (2006) Regulation of ornithine decarboxylase. J Biol Chem 281:14529-14532
    • (2006) J Biol Chem , vol.281 , pp. 14529-14532
    • Pegg, A.E.1
  • 30
    • 0023098372 scopus 로고
    • Decarboxylation of alphadifluoromethylamine by ornithine decarboxylase
    • Pegg AE, McGovern KA, Weist L (1987) Decarboxylation of alphadifluoromethylamine by ornithine decarboxylase. Biochem J 241:305-307
    • (1987) Biochem J , vol.241 , pp. 305-307
    • Pegg, A.E.1    McGovern, K.A.2    Weist, L.3
  • 31
    • 0037397642 scopus 로고    scopus 로고
    • Transgenic mouse models for studies of the role of polyamines in normal, hypertrophic and neoplastic growth
    • DOI 10.1042/BST0310356
    • Pegg AE, Feith DJ, Fong LY, Coleman CS, O'Brien TG, Shantz LM (2003) Transgenic mouse models for studies of the role of polyamines in normal, hypertrophic and neoplastic growth. Biochem Soc Trans 31:356-360 (Pubitemid 36520676)
    • (2003) Biochemical Society Transactions , vol.31 , Issue.2 , pp. 356-360
    • Pegg, A.E.1    Feith, D.J.2    Fong, L.Y.Y.3    Coleman, C.S.4    O'Brien, T.G.5    Shantz, L.M.6
  • 32
    • 0028822437 scopus 로고
    • Induction of apoptosis by excessive polyamine accumulation in ornithine decarboxylase-overproducing L1210 cells
    • Pouline R, Pelletier G, Pegg AE (1995) Induction of apoptosis by excessive polyamine accumulation in ornithine decarboxylase-overproducing L1210 cells. Biochem J 311:723-727
    • (1995) Biochem J , vol.311 , pp. 723-727
    • Pouline, R.1    Pelletier, G.2    Pegg, A.E.3
  • 33
    • 0018394382 scopus 로고
    • Epithelioid cell cultures from rat small intestine. Characterization of morphologic and immunologic criteria
    • Quaroni A, Wands J, Trelstad RL, Isselbacher KJ (1979) Epithelioid cell culture from rat small intestine. Characterization by morphologic and immunologic criteria. J Cell Biol 80:248-265 (Pubitemid 9091502)
    • (1979) Journal of Cell Biology , vol.80 , Issue.2 , pp. 248-265
    • Quaroni, A.1    Wands, J.2    Trelstad, R.L.3    Isselbacher, K.J.4
  • 35
    • 0034066525 scopus 로고    scopus 로고
    • Polyamine depletion delays apoptosis of rat intestinal epithelial cells
    • Ray RM, Viar MJ, Yuan Q, Johnson LR (2000) Polyamine depletion delays apoptosis of rat intestinal epithelial cells. Am J Physiol 278:C400-C489
    • (2000) Am J Physiol , vol.278
    • Ray, R.M.1    Viar, M.J.2    Yuan, Q.3    Johnson, L.R.4
  • 36
    • 84856703513 scopus 로고    scopus 로고
    • Amino acids regulate the expression of antizyme-1 to modulate ornithine decarboxylase activity
    • Ray RM, Viar MJ, Johnson LR (2012) Amino acids regulate the expression of antizyme-1 to modulate ornithine decarboxylase activity. J Biol Chem 287:3674-3690
    • (2012) J Biol Chem , vol.287 , pp. 3674-3690
    • Ray, R.M.1    Viar, M.J.2    Johnson, L.R.3
  • 37
    • 0022415499 scopus 로고
    • Induction of ornithine decarboxylase activity by insulin and growth factors is mediated by amino acids
    • Rinehart CA Jr, Canellakis ES (1985) Induction of ornithine decarboxylase activity by insulin and growth factors is mediated by amino acids. Proc Natl Acad Sci USA 82:4365-4368
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4365-4368
    • Rinehart Jr., C.A.1    Canellakis, E.S.2
  • 38
    • 0021804548 scopus 로고
    • The effect of transport system A and N amino acids and of nerve and epidermal growth factors on the induction of ornithine decarboxylase activity
    • DOI 10.1002/jcp.1041230321
    • Rinehart CA Jr, Viceps-Madore D, Fong WF, Ortiz JG, Canellakis ES (1985) The effect of transport system A and N amino acids and nerve and epidermal growth factors on the induction of ornithine decarboxylase activity. J Cell Physiol 123:435-441 (Pubitemid 15011381)
    • (1985) Journal of Cellular Physiology , vol.123 , Issue.3 , pp. 435-441
    • Rinehart Jr., C.A.1    Viceps-Madore, D.2    Fong, W.-F.3
  • 39
    • 0022341893 scopus 로고
    • Ornithine decarboxylase: A key regulatory enzyme in normal and neoplastic growth
    • Russell DH (1985) Ornithine decarboxylase: a key regulatory enzyme in normal and neoplastic growth. Drug Met Rev 16:1-88
    • (1985) Drug Met Rev , vol.16 , pp. 1-88
    • Russell, D.H.1
  • 40
    • 84874135468 scopus 로고    scopus 로고
    • Food as a hormone
    • Ryan KK, Seeley RJ (2013) Food as a hormone. Science 339:918-919
    • (2013) Science , vol.339 , pp. 918-919
    • Ryan, K.K.1    Seeley, R.J.2
  • 41
    • 3342895823 scopus 로고    scopus 로고
    • Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton
    • Sarbassov DD, Ali SM, Kim DH, Guertin DA, Latek RR, Erdjument-Bromage H, Tempst P, Sabitini DM (2004) Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr Biol 14:1296-1302
    • (2004) Curr Biol , vol.14 , pp. 1296-1302
    • Sarbassov, D.D.1    Ali, S.M.2    Kim, D.H.3    Guertin, D.A.4    Latek, R.R.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabitini, D.M.8
  • 42
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • DOI 10.1126/science.1106148
    • Sarbassov DD, Guertin DA, Ali SM, Sabatini DM (2005) Phosphorylation and regulation of Akt/PKB by Rictor mTOR complex. Science 307:1098-1101 (Pubitemid 40262113)
    • (2005) Science , vol.307 , Issue.5712 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 43
    • 67650445808 scopus 로고    scopus 로고
    • Antizyme is necessary for conversion of pancreatic tumor cells into glucagon-producing differentiated cells
    • Suzuki J, Murakami Y, Samejima K, Ontani KK, Oka T (2009) Antizyme is necessary for conversion of pancreatic tumor cells into glucagon-producing differentiated cells. Endocr Relat Cancer 16:649-659
    • (2009) Endocr Relat Cancer , vol.16 , pp. 649-659
    • Suzuki, J.1    Murakami, Y.2    Samejima, K.3    Ontani, K.K.4    Oka, T.5
  • 44
    • 84896316484 scopus 로고    scopus 로고
    • Amino acids activate mammalian target of rapamycin complex 2 (mTORC2) via P13K/Akt signaling
    • Tato I, Bartons R, Ventura F, Rosa JL (2011) Amino acids activate mammalian target of rapamycin complex 2 (mTORC2) via P13K/Akt signaling. J Biol Chem 272:26457-26463
    • (2011) J Biol Chem , vol.272 , pp. 26457-26463
    • Tato, I.1    Bartons, R.2    Ventura, F.3    Rosa, J.L.4
  • 45
    • 0028800002 scopus 로고
    • Exposure to ornithine results in excessive accumulation of putrescine and apoptotic cell death in ornithine decarboxylase overproducing mouse myeloma cells
    • Tobias KE, Kahana C (1995) Exposure to ornithine results in excessive accumulation of putrescine and apoptotic cell death in ornithine decarboxylase overproducing mouse myeloma cells. Cell Growth Differ 10:1279-1285
    • (1995) Cell Growth Differ , vol.10 , pp. 1279-1285
    • Tobias, K.E.1    Kahana, C.2
  • 46
    • 0020379004 scopus 로고
    • Studies on the role of protein synthesis and of sodium on the regulation of ornithine decarboxylase activity
    • Viceps-Madore D, Chen KY, Tsou HR, Canellakis ES (1982) Studies on the role of protein synthesis and of sodium on the regulation of ornithine decarboxylase activity. Biochim Biophys Acta 717:305-315 (Pubitemid 13244683)
    • (1982) Biochimica et Biophysica Acta , vol.717 , Issue.2 , pp. 305-315
    • Viceps-Madore, D.1    Chen, K.Y.2    Tsou, H.3    Canellakis, E.S.4
  • 48
    • 0026025829 scopus 로고
    • Polyamines and ornithine decarboxylase during repair of duodenal mucosa after stress in rats
    • Wang J-Y, Johnson LR (1991) Polyamines and ornithine decarboxylase during repair of duodenal mucosa after stress in rats. Gastroenterology 100:333-343
    • (1991) Gastroenterology , vol.100 , pp. 333-343
    • Wang, J.-Y.1    Johnson, L.R.2
  • 49
    • 33749431713 scopus 로고    scopus 로고
    • The mTOR pathway in the control of protein synthesis
    • DOI 10.1152/physiol.00024.2006
    • Wang X, Proud CG (2006) The mTOR pathway in the control of protein synthesis. Physiology 21:362-369 (Pubitemid 44511764)
    • (2006) Physiology , vol.21 , Issue.5 , pp. 362-369
    • Wang, X.1    Proud, C.G.2
  • 50
    • 0142068802 scopus 로고    scopus 로고
    • Cyclin-dependent kinases and S phase control in mammalian cells
    • Woo RA, Poon RY (2003) Cyclin-dependent kinases and S phase control in mammalian cells. Cell Cycle 2:316-324
    • (2003) Cell Cycle , vol.2 , pp. 316-324
    • Woo, R.A.1    Poon, R.Y.2
  • 51
    • 0026768597 scopus 로고
    • Effect of total parenteral nutrition, systemic sepsis, and glutamine on gut mucosa in rats
    • Yoshida S, Leskiw MJ, Schulter MD et al (1992) Effect of total parenteral nutrition, systemic sepsis, and glutamine on gut mucosa in rats. Am J Physiol 263:E368-E373
    • (1992) Am J Physiol , vol.263
    • Yoshida, S.1    Leskiw, M.J.2    Schulter, M.D.3
  • 52
    • 0003217130 scopus 로고
    • Polyamine-mediated cell migration and growth: Structural requirement for diamine analogues to substitute for putrescine
    • Zimmerman BJ, McCormack SA, Israel M, Johnson LR (1995) Polyamine-mediated cell migration and growth: structural requirement for diamine analogues to substitute for putrescine. Cell Pharmacol 2:109-113
    • (1995) Cell Pharmacol , vol.2 , pp. 109-113
    • Zimmerman, B.J.1    McCormack, S.A.2    Israel, M.3    Johnson, L.R.4
  • 53
    • 78650510609 scopus 로고    scopus 로고
    • From growth signal integration to cancer, diabetes and aging
    • Zoncu R, Efeyan A, Sabitini DM (2011) From growth signal integration to cancer, diabetes and aging. Nature Rev Mol Cell Biol 12:21-35
    • (2011) Nature Rev Mol Cell Biol , vol.12 , pp. 21-35
    • Zoncu, R.1    Efeyan, A.2    Sabitini, D.M.3


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