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Volumn 155, Issue 4, 1999, Pages 1105-1113

Overexpression of Pterin-4a-carbinolamine dehydratase/dimerization cofactor of hepatocyte nuclear factor 1 in human colon cancer

Author keywords

[No Author keywords available]

Indexed keywords

HYDROLYASE; NUCLEAR FACTOR I; POLYCLONAL ANTIBODY; PTERIN DERIVATIVE; TETRAHYDROBIOPTERIN;

EID: 2442763214     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0002-9440(10)65213-3     Document Type: Article
Times cited : (18)

References (50)
  • 1
    • 0027079977 scopus 로고
    • Identity of 4a-carbinolamine dehydratase, a component of the phenylalanine hydroxylation system, and DCoH, a transregulator of homeodomain proteins
    • Citron BA, Davis MD, Milstien S, Gutierrez J, Mendel DB, Crabtree GR, Kaufman S: Identity of 4a-carbinolamine dehydratase, a component of the phenylalanine hydroxylation system, and DCoH, a transregulator of homeodomain proteins Proc Natl Acad Sci USA 1992, 89:11891-11894
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11891-11894
    • Citron, B.A.1    Davis, M.D.2    Milstien, S.3    Gutierrez, J.4    Mendel, D.B.5    Crabtree, G.R.6    Kaufman, S.7
  • 2
    • 0027364768 scopus 로고
    • Molecular cloning and recombinant expression of the human liver phenylalanine hydroxylase stimulating factor revealed structural and functional identity to the dimerization cofactor for nuclear transcription factor HNF1 alpha
    • Thöny B, Neuheiser F, Hauer CR, Heizmann CW: Molecular cloning and recombinant expression of the human liver phenylalanine hydroxylase stimulating factor revealed structural and functional identity to the dimerization cofactor for nuclear transcription factor HNF1 alpha. Adv Exp Med Biol 1993, 338:103-106
    • (1993) Adv Exp Med Biol , vol.338 , pp. 103-106
    • Thöny, B.1    Neuheiser, F.2    Hauer, C.R.3    Heizmann, C.W.4
  • 3
    • 0001465946 scopus 로고
    • Phenylalanine hydroxylase stimulator protein is a 4a-carbinolamine dehydratase
    • Lazarus RA, Benkovic SJ, Kaufman S: Phenylalanine hydroxylase stimulator protein is a 4a-carbinolamine dehydratase. J Biol Chem 1983, 258:10960-10962
    • (1983) J Biol Chem , vol.258 , pp. 10960-10962
    • Lazarus, R.A.1    Benkovic, S.J.2    Kaufman, S.3
  • 5
    • 0021891891 scopus 로고
    • Biosynthesis and metabolism of tetrahydrobiopterin and molybdopterin
    • Nichol CA, Smith GK, Duch DS: Biosynthesis and metabolism of tetrahydrobiopterin and molybdopterin. Ann Rev Biochem 1985, 54: 729-764
    • (1985) Ann Rev Biochem , vol.54 , pp. 729-764
    • Nichol, C.A.1    Smith, G.K.2    Duch, D.S.3
  • 7
    • 0027975453 scopus 로고
    • Nitric oxide: A physiologic messenger molecule
    • Bredt DS, Snyder SH: Nitric oxide: a physiologic messenger molecule. Annu Rev Biochem 1994, 63:175-195
    • (1994) Annu Rev Biochem , vol.63 , pp. 175-195
    • Bredt, D.S.1    Snyder, S.H.2
  • 8
    • 0002610221 scopus 로고
    • The hyperphenylalaninemias
    • Edited by CR Scriver, AL Beaudet, WS Sly, D Valle. New York, McGraw-Hill
    • Scriver CR, Kaufman S, Woo SLC: The hyperphenylalaninemias. The Metabolic Basis of Inherited Disease, Vol. 1. Edited by CR Scriver, AL Beaudet, WS Sly, D Valle. New York, McGraw-Hill, 1989, pp 495-546
    • (1989) The Metabolic Basis of Inherited Disease , vol.1 , pp. 495-546
    • Scriver, C.R.1    Kaufman, S.2    Woo, S.L.C.3
  • 9
    • 0002756708 scopus 로고
    • Tetrahydrobiopterin deficiency: From phenotype to genotype
    • Blau N, Thöny B, Heizmann CW, Dhondt JL: Tetrahydrobiopterin deficiency: from phenotype to genotype. Pteridines 1993, 4:1-10
    • (1993) Pteridines , vol.4 , pp. 1-10
    • Blau, N.1    Thöny, B.2    Heizmann, C.W.3    Dhondt, J.L.4
  • 10
    • 0025203727 scopus 로고
    • 7-Substituted pterins: Formation during phenylalanine hydroxylation in the absence of dehydratase
    • Curtius HC, Adler C, Rebrin I, Heizmann C, Ghisla S: 7-Substituted pterins: formation during phenylalanine hydroxylation in the absence of dehydratase. Biochem Biophys Res Commun 1990, 172:1060-1066
    • (1990) Biochem Biophys Res Commun , vol.172 , pp. 1060-1066
    • Curtius, H.C.1    Adler, C.2    Rebrin, I.3    Heizmann, C.4    Ghisla, S.5
  • 11
    • 0026667893 scopus 로고
    • 7-Substituted pterins in humans with suspected pterin-4a-carbinolamine dehydratase deficiency. Mechanism of formation via non-enzymatic transformation from 6-substituted pterins
    • Adler C, Ghisla S, Rebrin I, Haavik J, Heizmann CW, Blau N, Kuster T, Curtius HC: 7-Substituted pterins in humans with suspected pterin-4a-carbinolamine dehydratase deficiency. Mechanism of formation via non-enzymatic transformation from 6-substituted pterins. Eur J Biochem 1992, 208:139-144
    • (1992) Eur J Biochem , vol.208 , pp. 139-144
    • Adler, C.1    Ghisla, S.2    Rebrin, I.3    Haavik, J.4    Heizmann, C.W.5    Blau, N.6    Kuster, T.7    Curtius, H.C.8
  • 12
    • 0026025853 scopus 로고
    • Conversion of 6-substituted tetrahydropterins to 7-isomers via phenylalanine hydroxylase-generated intermediates
    • Davis MD, Kaufman S, Milstien S: Conversion of 6-substituted tetrahydropterins to 7-isomers via phenylalanine hydroxylase-generated intermediates. Proc Natl Acad Sci USA 1991, 88:385-389
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 385-389
    • Davis, M.D.1    Kaufman, S.2    Milstien, S.3
  • 13
    • 0027367110 scopus 로고
    • Mutation in the 4a-oarbinolamine dehydratase gene leads to mild hyperphenylalaninemia with defective cofactor metabolism
    • Citron BA, Kaufman S, Milstien S, Naylor EW, Greene CL, Davis MD: Mutation in the 4a-oarbinolamine dehydratase gene leads to mild hyperphenylalaninemia with defective cofactor metabolism. Am J Hum Genet 1993, 53:768-774
    • (1993) Am J Hum Genet , vol.53 , pp. 768-774
    • Citron, B.A.1    Kaufman, S.2    Milstien, S.3    Naylor, E.W.4    Greene, C.L.5    Davis, M.D.6
  • 14
    • 0031750012 scopus 로고    scopus 로고
    • Hyperphenylalaninemia with high levels of 7-biopterin is associated with mutations in the PCBD gene encoding the bifunctional protein pterin-4a-carbinolamine dehydratase (PCD) and transcriptional coactivator (DCoH)
    • Thöny B, Neuheiser F, Kierat L, Blaskovics M, Arn PH, Ferreira P, Rebrin I, Ayling J, Blau N: Hyperphenylalaninemia with high levels of 7-biopterin is associated with mutations in the PCBD gene encoding the bifunctional protein pterin-4a-carbinolamine dehydratase (PCD) and transcriptional coactivator (DCoH). Am J Hum Genet 1998, 62: 1302-1311
    • (1998) Am J Hum Genet , vol.62 , pp. 1302-1311
    • Thöny, B.1    Neuheiser, F.2    Kierat, L.3    Blaskovics, M.4    Arn, P.H.5    Ferreira, P.6    Rebrin, I.7    Ayling, J.8    Blau, N.9
  • 18
    • 0026928723 scopus 로고
    • HNF1, a homeoprotein member of the hepatic transcription regulatory network
    • Tronche F, Yaniv M: HNF1, a homeoprotein member of the hepatic transcription regulatory network. Bioessays 1992, 14:579-587
    • (1992) Bioessays , vol.14 , pp. 579-587
    • Tronche, F.1    Yaniv, M.2
  • 19
    • 0025892211 scopus 로고
    • HNF-1 alpha and HNF-1 beta (vHNF-1) share dimerization and homeo domains, but not activation domains, and form heterodimers in vitro
    • Mendel DB, Hansen LP, Graves MK, Conley PB, Crabtree GR: HNF-1 alpha and HNF-1 beta (vHNF-1) share dimerization and homeo domains, but not activation domains, and form heterodimers in vitro. Genes Dev 1991, 5:1042-1056
    • (1991) Genes Dev , vol.5 , pp. 1042-1056
    • Mendel, D.B.1    Hansen, L.P.2    Graves, M.K.3    Conley, P.B.4    Crabtree, G.R.5
  • 20
    • 0031561807 scopus 로고    scopus 로고
    • The bifunctional protein DCoH modulates interactions of the homeodomain transcription factor HNF1 with nucleic acids
    • Rhee KH, Stier G, Becker PB, Suck D, Sandaltzopoulos R: The bifunctional protein DCoH modulates interactions of the homeodomain transcription factor HNF1 with nucleic acids. J Mol Biol 1997, 265:20-29
    • (1997) J Mol Biol , vol.265 , pp. 20-29
    • Rhee, K.H.1    Stier, G.2    Becker, P.B.3    Suck, D.4    Sandaltzopoulos, R.5
  • 21
    • 0027462074 scopus 로고
    • Regulation of the HNF-1 homeoproteins by DCoH
    • Hansen LP, Crabtree GR: Regulation of the HNF-1 homeoproteins by DCoH. Curr Opin Genet Dev 1993, 3:246-253
    • (1993) Curr Opin Genet Dev , vol.3 , pp. 246-253
    • Hansen, L.P.1    Crabtree, G.R.2
  • 22
    • 0025775278 scopus 로고
    • vHNF1 is a homeoprotein that activates transcription and forms heterodimers with HNF1
    • Rey-Campos J, Chouard T, Yaniv M, Cereghini S: vHNF1 is a homeoprotein that activates transcription and forms heterodimers with HNF1. EMBO J 1991, 10:1445-1457
    • (1991) EMBO J , vol.10 , pp. 1445-1457
    • Rey-Campos, J.1    Chouard, T.2    Yaniv, M.3    Cereghini, S.4
  • 23
    • 0025678378 scopus 로고
    • Molecular cloning, functional expression, and chromosomal localization of mouse hepatocyte nuclear factor 1
    • Kuo CJ, Conley PB, Hsieh CL, Francke U, Crabtree GR: Molecular cloning, functional expression, and chromosomal localization of mouse hepatocyte nuclear factor 1. Proc Natl Acad Sci USA 1990, 87:9838-9842
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 9838-9842
    • Kuo, C.J.1    Conley, P.B.2    Hsieh, C.L.3    Francke, U.4    Crabtree, G.R.5
  • 24
    • 0028910712 scopus 로고
    • Developmental expression of the maternal protein XDCoH, the dimerization cofactor of the homeoprotein LFB1 (HNF1)
    • Pogge von Strandmann E, Ryffel GU: Developmental expression of the maternal protein XDCoH, the dimerization cofactor of the homeoprotein LFB1 (HNF1). Development 1995, 121:1217-1226
    • (1995) Development , vol.121 , pp. 1217-1226
    • Pogge Von Strandmann, E.1    Ryffel, G.U.2
  • 25
    • 0028980949 scopus 로고
    • Human pterin-4a-carbinolamine dehydratase/ dimerization cofactor of hepatocyte nuclear factor 1: Characterization and kinetic analysis of wild-type and mutant enzymes
    • Köster S, Thöny B, Macheroux P, Curtius HC, Heizmann CW, Pfleiderer W, Ghisla S: Human pterin-4a-carbinolamine dehydratase/ dimerization cofactor of hepatocyte nuclear factor 1: characterization and kinetic analysis of wild-type and mutant enzymes. Eur J Biochem 1995, 231:414-423
    • (1995) Eur J Biochem , vol.231 , pp. 414-423
    • Köster, S.1    Thöny, B.2    Macheroux, P.3    Curtius, H.C.4    Heizmann, C.W.5    Pfleiderer, W.6    Ghisla, S.7
  • 26
    • 2442765048 scopus 로고
    • Colorectal carcinoma pathology
    • Edited by Rustgi AK. Philadelphia, Lippincott-Raven Publishers
    • Lev R, Lee M: Colorectal carcinoma pathology. Gastrointestinal Cancers: Biology, Diagnosis and Therapy. Edited by Rustgi AK. Philadelphia, Lippincott-Raven Publishers, 1995, p 385
    • (1995) Gastrointestinal Cancers: Biology, Diagnosis and Therapy , pp. 385
    • Lev, R.1    Lee, M.2
  • 28
    • 0026596920 scopus 로고
    • Distribution of 4a-hydroxytetrahydropterin dehydratase in rat tissues
    • Davis MD, Kaufman S, Milstien S: Distribution of 4a-hydroxytetrahydropterin dehydratase in rat tissues. FEBS Lett 1992, 302:73-76
    • (1992) FEBS Lett , vol.302 , pp. 73-76
    • Davis, M.D.1    Kaufman, S.2    Milstien, S.3
  • 29
    • 0024411870 scopus 로고
    • Protein measurement using bicinchoninic acid: Elimination of interfering substances
    • Brown RE, Jarvis KL, Hyland KJ: Protein measurement using bicinchoninic acid: elimination of interfering substances. Anal Biochem 1989, 180:136-139
    • (1989) Anal Biochem , vol.180 , pp. 136-139
    • Brown, R.E.1    Jarvis, K.L.2    Hyland, K.J.3
  • 30
    • 0021848205 scopus 로고
    • Microassay for proteins on nitrocellulose filter using protein dye-staining procedure
    • Nakamura K, Tanaka T, Kuwahara A, Takeo K: Microassay for proteins on nitrocellulose filter using protein dye-staining procedure. Anal Biochem 1985, 148:311-319
    • (1985) Anal Biochem , vol.148 , pp. 311-319
    • Nakamura, K.1    Tanaka, T.2    Kuwahara, A.3    Takeo, K.4
  • 31
    • 0025312728 scopus 로고
    • A genetic model for colorectal tumorigenesis
    • Fearon ER, Vogelsteln B: A genetic model for colorectal tumorigenesis. Cell 1990, 61:759-767
    • (1990) Cell , vol.61 , pp. 759-767
    • Fearon, E.R.1    Vogelsteln, B.2
  • 33
    • 0011908028 scopus 로고
    • Tetrahydrobiopterin, the cofactor for aromatic amino acid hydroxylases, is synthesized by and regulates proliferation of erythroid cells
    • Tanaka K, Kaufman S, Milstien S: Tetrahydrobiopterin, the cofactor for aromatic amino acid hydroxylases, is synthesized by and regulates proliferation of erythroid cells. Proc Natl Acad Sci USA 1989, 86: 5864-5867
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5864-5867
    • Tanaka, K.1    Kaufman, S.2    Milstien, S.3
  • 34
    • 0023022209 scopus 로고
    • Pteridines are produced during interteukin 2-induced T-cell proliferation and modulate transmission of this signal
    • Ziegler I, Schwulera U, Ellwart J: Pteridines are produced during interteukin 2-induced T-cell proliferation and modulate transmission of this signal. Exp Cell Res 1986, 167:531-538
    • (1986) Exp Cell Res , vol.167 , pp. 531-538
    • Ziegler, I.1    Schwulera, U.2    Ellwart, J.3
  • 36
    • 0025281209 scopus 로고
    • Synthesis of tetrahydrobiopterin in Friend erythroleukemia cells and its modulator effect on cell proliferation
    • Kerler F, Ziegler I, Schmid C, Bacher A: Synthesis of tetrahydrobiopterin in Friend erythroleukemia cells and its modulator effect on cell proliferation. Exp Cell Res 1990, 189:151-156
    • (1990) Exp Cell Res , vol.189 , pp. 151-156
    • Kerler, F.1    Ziegler, I.2    Schmid, C.3    Bacher, A.4
  • 38
    • 0028026868 scopus 로고
    • Nitric oxide synthase: Aspects concerning structure and catalysis
    • Marietta MA: Nitric oxide synthase: aspects concerning structure and catalysis. Cell 1994, 78:927-930
    • (1994) Cell , vol.78 , pp. 927-930
    • Marietta, M.A.1
  • 39
    • 0027325255 scopus 로고
    • Nitric oxide synthase structure and mechanism
    • Marietta MA: Nitric oxide synthase structure and mechanism. J Biol Chem 1993, 268:12231-12234
    • (1993) J Biol Chem , vol.268 , pp. 12231-12234
    • Marietta, M.A.1
  • 40
    • 0027441142 scopus 로고
    • Macrophage nitric oxide synthase subunits. Purification, characterization, and role of prosthetic groups and substrate in regulating their association into a dimeric enzyme
    • Baek KJ, Thiel BA, Lucas S, Stuehr DJ: Macrophage nitric oxide synthase subunits. Purification, characterization, and role of prosthetic groups and substrate in regulating their association into a dimeric enzyme. J Biol Chem 1993, 268:21120-21129
    • (1993) J Biol Chem , vol.268 , pp. 21120-21129
    • Baek, K.J.1    Thiel, B.A.2    Lucas, S.3    Stuehr, D.J.4
  • 41
    • 0029125762 scopus 로고
    • Structural analysis of porcine brain nitric oxide synthase reveals a role for tetrahydrobiopterin and L-arginine in the formation of an SDS-resistant dimer
    • Klatt P, Schmidt K, Lehner D, Glatter O, Bachinger HP, Mayer B: Structural analysis of porcine brain nitric oxide synthase reveals a role for tetrahydrobiopterin and L-arginine in the formation of an SDS-resistant dimer. EMBO J 1995, 14:3687-3695
    • (1995) EMBO J , vol.14 , pp. 3687-3695
    • Klatt, P.1    Schmidt, K.2    Lehner, D.3    Glatter, O.4    Bachinger, H.P.5    Mayer, B.6
  • 42
    • 0027942862 scopus 로고
    • Aberrant expression of nitric oxide synthase in human polyps, neoplastic colonic mucosa and surrounding peritumoral normal mucosa
    • Chhatwal VJ, Ngoi SS, Chan ST, Chia YW, Moochhala SM: Aberrant expression of nitric oxide synthase in human polyps, neoplastic colonic mucosa and surrounding peritumoral normal mucosa. Carcinogenesis 1994, 15:2081-2085
    • (1994) Carcinogenesis , vol.15 , pp. 2081-2085
    • Chhatwal, V.J.1    Ngoi, S.S.2    Chan, S.T.3    Chia, Y.W.4    Moochhala, S.M.5
  • 44
    • 0030877443 scopus 로고    scopus 로고
    • Selective inhibition of inducible nitric oxide synthase inhibits tumor growth in vivo: Studies with 1400W, a novel inhibitor
    • Thomsen LL, Scott JM, Topley P, Knowles RG, Keerie AJ, Frend AJ: Selective inhibition of inducible nitric oxide synthase inhibits tumor growth in vivo: studies with 1400W, a novel inhibitor. Cancer Res 1997, 57:3300-3304
    • (1997) Cancer Res , vol.57 , pp. 3300-3304
    • Thomsen, L.L.1    Scott, J.M.2    Topley, P.3    Knowles, R.G.4    Keerie, A.J.5    Frend, A.J.6
  • 45
    • 0029866048 scopus 로고    scopus 로고
    • A cohort of supporting metabolic enzymes is coinduced with nitric oxide synthase in human tumor cell lines
    • Nussler AK, Liu ZZ, Hatakeyama K, Geller DA, Billiar TR, Morris SM Jr: A cohort of supporting metabolic enzymes is coinduced with nitric oxide synthase in human tumor cell lines. Cancer Lett 1996, 103: 79-84
    • (1996) Cancer Lett , vol.103 , pp. 79-84
    • Nussler, A.K.1    Liu, Z.Z.2    Hatakeyama, K.3    Geller, D.A.4    Billiar, T.R.5    Morris Jr., S.M.6
  • 47
    • 0025949056 scopus 로고
    • Hepatic nuclear factor 1 (HNF1) shows a wider distribution than products of its known target genes in developing mouse
    • Blumenfeld M, Maury M, Chouard T, Yaniv M, Condamine H: Hepatic nuclear factor 1 (HNF1) shows a wider distribution than products of its known target genes in developing mouse. Development 1991, 113:589-599
    • (1991) Development , vol.113 , pp. 589-599
    • Blumenfeld, M.1    Maury, M.2    Chouard, T.3    Yaniv, M.4    Condamine, H.5
  • 49
    • 0026670321 scopus 로고
    • Trans-dominant inhibition of transcription activator LFB1
    • Nicosia A, Tafi R, Monaci P: Trans-dominant inhibition of transcription activator LFB1. Nucleic Acids Res 1992, 20:5321-5328
    • (1992) Nucleic Acids Res , vol.20 , pp. 5321-5328
    • Nicosia, A.1    Tafi, R.2    Monaci, P.3
  • 50
    • 0032983657 scopus 로고    scopus 로고
    • Immunohistochemical localization of pterin 4-alpha-carbinolamine dehydratase in rat peripheral organs
    • Resibois A, Cuvelier L, Svoboda M, Heizmann CW, Thöny B: Immunohistochemical localization of pterin 4-alpha-carbinolamine dehydratase in rat peripheral organs. Histochem Cell Biol 1999, 111:381-390
    • (1999) Histochem Cell Biol , vol.111 , pp. 381-390
    • Resibois, A.1    Cuvelier, L.2    Svoboda, M.3    Heizmann, C.W.4    Thöny, B.5


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