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- Abramson R. D., Barbosa P., Kalumuck K., O'Brien W. E. Characterization of the human argininosuccinate lyase gene and analysis of exon skipping. Genomics. 1991 May;10(1):126–132. doi: 10.1016/0888-7543(91)90492-w. [DOI] [PubMed] [Google Scholar]
- Adachi H., Iida S., Oguchi S., Ohshima H., Suzuki H., Nagasaki K., Kawasaki H., Sugimura T., Esumi H. Molecular cloning of a cDNA encoding an inducible calmodulin-dependent nitric-oxide synthase from rat liver and its expression in COS 1 cells. Eur J Biochem. 1993 Oct 1;217(1):37–43. doi: 10.1111/j.1432-1033.1993.tb18215.x. [DOI] [PubMed] [Google Scholar]
- Adcock M. W., O'Brien W. E. Molecular cloning of cDNA for rat and human carbamyl phosphate synthetase I. J Biol Chem. 1984 Nov 10;259(21):13471–13476. [PubMed] [Google Scholar]
- Akira S., Isshiki H., Sugita T., Tanabe O., Kinoshita S., Nishio Y., Nakajima T., Hirano T., Kishimoto T. A nuclear factor for IL-6 expression (NF-IL6) is a member of a C/EBP family. EMBO J. 1990 Jun;9(6):1897–1906. doi: 10.1002/j.1460-2075.1990.tb08316.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Amaya Y., Matsubasa T., Takiguchi M., Kobayashi K., Saheki T., Kawamoto S., Mori M. Amino acid sequence of rat argininosuccinate lyase deduced from cDNA. J Biochem. 1988 Jan;103(1):177–181. doi: 10.1093/oxfordjournals.jbchem.a122227. [DOI] [PubMed] [Google Scholar]
- Anderson G. M., Freytag S. O. Synergistic activation of a human promoter in vivo by transcription factor Sp1. Mol Cell Biol. 1991 Apr;11(4):1935–1943. doi: 10.1128/mcb.11.4.1935. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Anderson P. M. Purification and properties of the glutamine- and N-acetyl-L-glutamate-dependent carbamoyl phosphate synthetase from liver of Squalus acanthias. J Biol Chem. 1981 Dec 10;256(23):12228–12238. [PubMed] [Google Scholar]
- Bachmann C., Colombo J. P., Jaggi K. N-acetylglutamate synthetase (NAGS) deficiency: diagnosis, clinical observations and treatment. Adv Exp Med Biol. 1982;153:39–45. doi: 10.1007/978-1-4757-6903-6_6. [DOI] [PubMed] [Google Scholar]
- Bachmann C., Krähenbühl S., Colombo J. P. Purification and properties of acetyl-CoA:L-glutamate N-acetyltransferase from human liver. Biochem J. 1982 Jul 1;205(1):123–127. doi: 10.1042/bj2050123. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Baker B. S., Tata J. R. Accumulation of proto-oncogene c-erb-A related transcripts during Xenopus development: association with early acquisition of response to thyroid hormone and estrogen. EMBO J. 1990 Mar;9(3):879–885. doi: 10.1002/j.1460-2075.1990.tb08185.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Barbosa P., Wistow G. J., Cialkowski M., Piatigorsky J., O'Brien W. E. Expression of duck lens delta-crystallin cDNAs in yeast and bacterial hosts. Delta 2-crystallin is an active argininosuccinate lyase. J Biol Chem. 1991 Nov 25;266(33):22319–22322. [PubMed] [Google Scholar]
- Baumann H., Morella K. K., Campos S. P., Cao Z., Jahreis G. P. Role of CAAT-enhancer binding protein isoforms in the cytokine regulation of acute-phase plasma protein genes. J Biol Chem. 1992 Sep 25;267(27):19744–19751. [PubMed] [Google Scholar]
- Baumhueter S., Mendel D. B., Conley P. B., Kuo C. J., Turk C., Graves M. K., Edwards C. A., Courtois G., Crabtree G. R. HNF-1 shares three sequence motifs with the POU domain proteins and is identical to LF-B1 and APF. Genes Dev. 1990 Mar;4(3):372–379. doi: 10.1101/gad.4.3.372. [DOI] [PubMed] [Google Scholar]
- Beggs A. H., Migeon B. R. Chromatin loop structure of the human X chromosome: relevance to X inactivation and CpG clusters. Mol Cell Biol. 1989 Jun;9(6):2322–2331. doi: 10.1128/mcb.9.6.2322. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bein K., Simmer J. P., Evans D. R. Molecular cloning of a cDNA encoding the amino end of the mammalian multifunctional protein CAD and analysis of the 5'-flanking region of the CAD gene. J Biol Chem. 1991 Feb 25;266(6):3791–3799. [PubMed] [Google Scholar]
- Benamar M., Gautier C., Renouf S., Fairand A., Husson A. Changes in argininosuccinate lyase gene expression in the rat liver during development. Biol Neonate. 1992;61(6):381–390. doi: 10.1159/000243825. [DOI] [PubMed] [Google Scholar]
- Berüter J., Colombo J. P., Bachmann C. Purification and properties of arginase from human liver and erythrocytes. Biochem J. 1978 Nov 1;175(2):449–454. doi: 10.1042/bj1750449. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bock H. G., Su T. S., O'Brien W. E., Beaudet A. L. Sequence for human argininosuccinate synthetase cDNA. Nucleic Acids Res. 1983 Sep 24;11(18):6505–6512. doi: 10.1093/nar/11.18.6505. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Boshart M., Weih F., Nichols M., Schütz G. The tissue-specific extinguisher locus TSE1 encodes a regulatory subunit of cAMP-dependent protein kinase. Cell. 1991 Sep 6;66(5):849–859. doi: 10.1016/0092-8674(91)90432-x. [DOI] [PubMed] [Google Scholar]
- Boyce F. M., 3rd, Freytag S. O. Regulation of human argininosuccinate synthetase gene: induction by positive-acting nuclear mechanism in canavanine-resistant cell variants. Somat Cell Mol Genet. 1989 Mar;15(2):113–121. doi: 10.1007/BF01535071. [DOI] [PubMed] [Google Scholar]
- Boyce F. M., 3rd, Pogulis R. J., Freytag S. O. Paradoxical regulation of human argininosuccinate synthetase cDNA minigene in opposition to endogenous gene: evidence for intragenic control sequences. Somat Cell Mol Genet. 1989 Mar;15(2):123–129. doi: 10.1007/BF01535072. [DOI] [PubMed] [Google Scholar]
- Boyce F. M., Anderson G. M., Rusk C. D., Freytag S. O. Human argininosuccinate synthetase minigenes are subject to arginine-mediated repression but not to trans induction. Mol Cell Biol. 1986 Apr;6(4):1244–1252. doi: 10.1128/mcb.6.4.1244. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bredt D. S., Hwang P. M., Glatt C. E., Lowenstein C., Reed R. R., Snyder S. H. Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase. Nature. 1991 Jun 27;351(6329):714–718. doi: 10.1038/351714a0. [DOI] [PubMed] [Google Scholar]
- Bredt D. S., Snyder S. H. Nitric oxide: a physiologic messenger molecule. Annu Rev Biochem. 1994;63:175–195. doi: 10.1146/annurev.bi.63.070194.001135. [DOI] [PubMed] [Google Scholar]
- Brusdeilins M., Kühner R., Schumacher K. Purification, affinity to anti-human arginase immunoglobulin-Sepharose 4B and subunit molecular weights of mammalian arginases. Biochim Biophys Acta. 1985 May 29;840(1):79–90. doi: 10.1016/0304-4165(85)90164-3. [DOI] [PubMed] [Google Scholar]
- Campos S. P., Baumann H. Insulin is a prominent modulator of the cytokine-stimulated expression of acute-phase plasma protein genes. Mol Cell Biol. 1992 Apr;12(4):1789–1797. doi: 10.1128/mcb.12.4.1789. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cao Z., Umek R. M., McKnight S. L. Regulated expression of three C/EBP isoforms during adipose conversion of 3T3-L1 cells. Genes Dev. 1991 Sep;5(9):1538–1552. doi: 10.1101/gad.5.9.1538. [DOI] [PubMed] [Google Scholar]
- Carritt B., Povey S. Regional asssignments of the loci AK3, ACONS, and ASS on human chromosome 9. Cytogenet Cell Genet. 1979;23(3):171–181. doi: 10.1159/000131323. [DOI] [PubMed] [Google Scholar]
- Chang C. J., Chen T. T., Lei H. Y., Chen D. S., Lee S. C. Molecular cloning of a transcription factor, AGP/EBP, that belongs to members of the C/EBP family. Mol Cell Biol. 1990 Dec;10(12):6642–6653. doi: 10.1128/mcb.10.12.6642. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Charles I. G., Palmer R. M., Hickery M. S., Bayliss M. T., Chubb A. P., Hall V. S., Moss D. W., Moncada S. Cloning, characterization, and expression of a cDNA encoding an inducible nitric oxide synthase from the human chondrocyte. Proc Natl Acad Sci U S A. 1993 Dec 1;90(23):11419–11423. doi: 10.1073/pnas.90.23.11419. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chin A. C., Fournier R. E. A genetic analysis of extinction: trans-regulation of 16 liver-specific genes in hepatoma-fibroblast hybrid cells. Proc Natl Acad Sci U S A. 1987 Mar;84(6):1614–1618. doi: 10.1073/pnas.84.6.1614. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Clarke S. A major polypeptide component of rat liver mitochondria: carbamyl phosphate synthetase. J Biol Chem. 1976 Feb 25;251(4):950–961. [PubMed] [Google Scholar]
- Cohen P. P. Biochemical differentiation during amphibian metamorphosis. Science. 1970 May 1;168(3931):533–543. doi: 10.1126/science.168.3931.533. [DOI] [PubMed] [Google Scholar]
- Coleman P. F., Suttle D. P., Stark G. R. Purification from hamster cells of the multifunctional protein that initiates de novo synthesis of pyrimidine nucleotides. J Biol Chem. 1977 Sep 25;252(18):6379–6385. [PubMed] [Google Scholar]
- Cooney A. J., Tsai S. Y., O'Malley B. W., Tsai M. J. Chicken ovalbumin upstream promoter transcription factor (COUP-TF) dimers bind to different GGTCA response elements, allowing COUP-TF to repress hormonal induction of the vitamin D3, thyroid hormone, and retinoic acid receptors. Mol Cell Biol. 1992 Sep;12(9):4153–4163. doi: 10.1128/mcb.12.9.4153. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Coustry F., Maity S. N., de Crombrugghe B. Studies on transcription activation by the multimeric CCAAT-binding factor CBF. J Biol Chem. 1995 Jan 6;270(1):468–475. doi: 10.1074/jbc.270.1.468. [DOI] [PubMed] [Google Scholar]
- Delers A., Szpirer J., Szpirer C., Saggioro D. Spontaneous and 5-azacytidine-induced reexpression of ornithine carbamoyl transferase in hepatoma cells. Mol Cell Biol. 1984 Apr;4(4):809–812. doi: 10.1128/mcb.4.4.809. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dennis J. A., Healy P. J., Beaudet A. L., O'Brien W. E. Molecular definition of bovine argininosuccinate synthetase deficiency. Proc Natl Acad Sci U S A. 1989 Oct;86(20):7947–7951. doi: 10.1073/pnas.86.20.7947. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Descombes P., Chojkier M., Lichtsteiner S., Falvey E., Schibler U. LAP, a novel member of the C/EBP gene family, encodes a liver-enriched transcriptional activator protein. Genes Dev. 1990 Sep;4(9):1541–1551. doi: 10.1101/gad.4.9.1541. [DOI] [PubMed] [Google Scholar]
- Dhanakoti S. N., Brosnan M. E., Herzberg G. R., Brosnan J. T. Cellular and subcellular localization of enzymes of arginine metabolism in rat kidney. Biochem J. 1992 Mar 1;282(Pt 2):369–375. doi: 10.1042/bj2820369. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dizikes G. J., Grody W. W., Kern R. M., Cederbaum S. D. Isolation of human liver arginase cDNA and demonstration of nonhomology between the two human arginase genes. Biochem Biophys Res Commun. 1986 Nov 26;141(1):53–59. doi: 10.1016/s0006-291x(86)80333-3. [DOI] [PubMed] [Google Scholar]
- Dizikes G. J., Spector E. B., Cederbaum S. D. Cloning of rat liver arginase cDNA and elucidation of regulation of arginase gene expression in H4 rat hepatoma cells. Somat Cell Mol Genet. 1986 Jul;12(4):375–384. doi: 10.1007/BF01570732. [DOI] [PubMed] [Google Scholar]
- Dorn A., Bollekens J., Staub A., Benoist C., Mathis D. A multiplicity of CCAAT box-binding proteins. Cell. 1987 Sep 11;50(6):863–872. doi: 10.1016/0092-8674(87)90513-7. [DOI] [PubMed] [Google Scholar]
- Dubois N., Cavard C., Chasse J. F., Kamoun P., Briand P. Compared expression levels of ornithine transcarbamylase and carbamylphosphate synthetase in liver and small intestine of normal and mutant mice. Biochim Biophys Acta. 1988 Sep 7;950(3):321–328. doi: 10.1016/0167-4781(88)90128-5. [DOI] [PubMed] [Google Scholar]
- Elliott K. R., Tipton K. F. Purification and characterisation of carbamoyl phosphate synthetase from beef liver. FEBS Lett. 1973 Nov 15;37(1):79–81. doi: 10.1016/0014-5793(73)80430-2. [DOI] [PubMed] [Google Scholar]
- Engelhardt J. F., Steel G., Valle D. Transcriptional analysis of the human ornithine aminotransferase promoter. J Biol Chem. 1991 Jan 15;266(2):752–758. [PubMed] [Google Scholar]
- Frain M., Swart G., Monaci P., Nicosia A., Stämpfli S., Frank R., Cortese R. The liver-specific transcription factor LF-B1 contains a highly diverged homeobox DNA binding domain. Cell. 1989 Oct 6;59(1):145–157. doi: 10.1016/0092-8674(89)90877-5. [DOI] [PubMed] [Google Scholar]
- Freytag S. O., Beaudet A. L., Bock H. G., O'Brien W. E. Molecular structure of the human argininosuccinate synthetase gene: occurrence of alternative mRNA splicing. Mol Cell Biol. 1984 Oct;4(10):1978–1984. doi: 10.1128/mcb.4.10.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Freytag S. O., Bock H. G., Beaudet A. L., O'Brien W. E. Molecular structures of human argininosuccinate synthetase pseudogenes. Evolutionary and mechanistic implications. J Biol Chem. 1984 Mar 10;259(5):3160–3166. [PubMed] [Google Scholar]
- Gaasbeek Janzen J. W., Lamers W. H., Moorman A. F., de Graaf A., Los J. A., Charles R. Immunohistochemical localization of carbamoyl-phosphate synthetase (ammonia) in adult rat liver; evidence for a heterogeneous distribution. J Histochem Cytochem. 1984 Jun;32(6):557–564. doi: 10.1177/32.6.6373912. [DOI] [PubMed] [Google Scholar]
- Gaasbeek Janzen J. W., Moorman A. F., Lamers W. H., Charles R. Development of the heterogeneous distribution of carbamoyl-phosphate synthetase (ammonia) in rat-liver parenchyma during postnatal development. J Histochem Cytochem. 1985 Dec;33(12):1205–1211. doi: 10.1177/33.12.4067274. [DOI] [PubMed] [Google Scholar]
- Gaasbeek Janzen J. W., Westenend P. J., Charles R., Lamers W. H., Moorman A. F. Gene expression in derivatives of embryonic foregut during prenatal development of the rat. J Histochem Cytochem. 1988 Oct;36(10):1223–1230. doi: 10.1177/36.10.2458406. [DOI] [PubMed] [Google Scholar]
- Gebhardt R., Mecke D. Permissive effect of dexamethasone on glucagon induction of urea-cycle enzymes in perifused primary monolayer cultures of rat hepatocytes. Eur J Biochem. 1979 Jun;97(1):29–35. doi: 10.1111/j.1432-1033.1979.tb13082.x. [DOI] [PubMed] [Google Scholar]
- Geller D. A., Lowenstein C. J., Shapiro R. A., Nussler A. K., Di Silvio M., Wang S. C., Nakayama D. K., Simmons R. L., Snyder S. H., Billiar T. R. Molecular cloning and expression of inducible nitric oxide synthase from human hepatocytes. Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3491–3495. doi: 10.1073/pnas.90.8.3491. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Glass R. D., Knox W. E. Arginase isozymes of rat mammary gland, liver, and other tissues. J Biol Chem. 1973 Aug 25;248(16):5785–5789. [PubMed] [Google Scholar]
- Gluecksohn-Waelsch S. Genetic control of morphogenetic and biochemical differentiation: lethal albino deletions in the mouse. Cell. 1979 Feb;16(2):225–237. doi: 10.1016/0092-8674(79)90001-1. [DOI] [PubMed] [Google Scholar]
- Gonzalez F. J., Liu S. Y., Kozak C. A., Nebert D. W. Decreased Hnf-1 gene expression in mice homozygous for a 1.2-centiMorgan deletion on chromosome 7. DNA Cell Biol. 1990 Dec;9(10):771–776. doi: 10.1089/dna.1990.9.771. [DOI] [PubMed] [Google Scholar]
- Goping I. S., Lagacé M., Shore G. C. Factors interacting with the rat carbamyl phosphate synthetase promoter in expressing and nonexpressing tissues. Gene. 1992 Sep 10;118(2):283–287. doi: 10.1016/0378-1119(92)90201-y. [DOI] [PubMed] [Google Scholar]
- Goping I. S., Lamontagne S., Shore G. C., Nguyen M. A gene-type-specific enhancer regulates the carbamyl phosphate synthetase I promoter by cooperating with the proximal GAG activating element. Nucleic Acids Res. 1995 May 25;23(10):1717–1721. doi: 10.1093/nar/23.10.1717. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Goping I. S., Shore G. C. Interactions between repressor and anti-repressor elements in the carbamyl phosphate synthetase I promoter. J Biol Chem. 1994 Feb 4;269(5):3891–3896. [PubMed] [Google Scholar]
- Goss S. J. The associated reactivation of two X-linked genes. The spontaneous and azacytidine-induced reexpression of ornithine transcarbamoylase and glucose-6-phosphate dehydrogenase in a rat hepatoma. J Cell Sci. 1984 Dec;72:241–257. doi: 10.1242/jcs.72.1.241. [DOI] [PubMed] [Google Scholar]
- Goto K., Okada T. S., Kondoh H. Functional cooperation of lens-specific and nonspecific elements in the delta 1-crystallin enhancer. Mol Cell Biol. 1990 Mar;10(3):958–964. doi: 10.1128/mcb.10.3.958. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gotoh T., Haraguchi Y., Takiguchi M., Mori M. The delayed glucocorticoid-responsive and hepatoma cell-selective enhancer of the rat arginase gene is located around intron 7. J Biochem. 1994 Apr;115(4):778–788. doi: 10.1093/oxfordjournals.jbchem.a124409. [DOI] [PubMed] [Google Scholar]
- Grompe M., al-Dhalimy M., Finegold M., Ou C. N., Burlingame T., Kennaway N. G., Soriano P. Loss of fumarylacetoacetate hydrolase is responsible for the neonatal hepatic dysfunction phenotype of lethal albino mice. Genes Dev. 1993 Dec;7(12A):2298–2307. doi: 10.1101/gad.7.12a.2298. [DOI] [PubMed] [Google Scholar]
- Guthöhrlein G., Knappe J. Structure and function of carbamoylphosphate synthase. I. Transitions between two catalytically inactive forms and the active form. Eur J Biochem. 1968 Dec;7(1):119–127. doi: 10.1111/j.1432-1033.1968.tb19582.x. [DOI] [PubMed] [Google Scholar]
- Hamano Y., Kodama H., Yanagisawa M., Haraguchi Y., Mori M., Yokota S. Immunocytochemical localization of ornithine transcarbamylase in rat intestinal mucosa. Light and electron microscopic study. J Histochem Cytochem. 1988 Jan;36(1):29–35. doi: 10.1177/36.1.3275711. [DOI] [PubMed] [Google Scholar]
- Haraguchi Y., Takiguchi M., Amaya Y., Kawamoto S., Matsuda I., Mori M. Molecular cloning and nucleotide sequence of cDNA for human liver arginase. Proc Natl Acad Sci U S A. 1987 Jan;84(2):412–415. doi: 10.1073/pnas.84.2.412. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Haraguchi Y., Uchino T., Takiguchi M., Endo F., Mori M., Matsuda I. Cloning and sequence of a cDNA encoding human carbamyl phosphate synthetase I: molecular analysis of hyperammonemia. Gene. 1991 Nov 15;107(2):335–340. doi: 10.1016/0378-1119(91)90336-a. [DOI] [PubMed] [Google Scholar]
- Hartman D. J., Hoogenraad N. J., Condron R., Høj P. B. Identification of a mammalian 10-kDa heat shock protein, a mitochondrial chaperonin 10 homologue essential for assisted folding of trimeric ornithine transcarbamoylase in vitro. Proc Natl Acad Sci U S A. 1992 Apr 15;89(8):3394–3398. doi: 10.1073/pnas.89.8.3394. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hata A., Tsuzuki T., Shimada K., Takiguchi M., Mori M., Matsuda I. Structure of the human ornithine transcarbamylase gene. J Biochem. 1988 Feb;103(2):302–308. doi: 10.1093/oxfordjournals.jbchem.a122265. [DOI] [PubMed] [Google Scholar]
- Hattori Y., Campbell E. B., Gross S. S. Argininosuccinate synthetase mRNA and activity are induced by immunostimulants in vascular smooth muscle. Role in the regeneration or arginine for nitric oxide synthesis. J Biol Chem. 1994 Apr 1;269(13):9405–9408. [PubMed] [Google Scholar]
- Hayashi S., Goto K., Okada T. S., Kondoh H. Lens-specific enhancer in the third intron regulates expression of the chicken delta 1-crystallin gene. Genes Dev. 1987 Oct;1(8):818–828. doi: 10.1101/gad.1.8.818. [DOI] [PubMed] [Google Scholar]
- Helbing C. C., Atkinson B. G. 3,5,3'-Triiodothyronine-induced carbamyl-phosphate synthetase gene expression is stabilized in the liver of Rana catesbeiana tadpoles during heat shock. J Biol Chem. 1994 Apr 22;269(16):11743–11750. [PubMed] [Google Scholar]
- Helbing C., Gergely G., Atkinson B. G. Sequential up-regulation of thyroid hormone beta receptor, ornithine transcarbamylase, and carbamyl phosphate synthetase mRNAs in the liver of Rana catesbeiana tadpoles during spontaneous and thyroid hormone-induced metamorphosis. Dev Genet. 1992;13(4):289–301. doi: 10.1002/dvg.1020130406. [DOI] [PubMed] [Google Scholar]
- Herzfeld A., Raper S. M. The heterogeneity of arginases in rat tissues. Biochem J. 1976 Feb 1;153(2):469–478. doi: 10.1042/bj1530469. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hirsch-Kolb H., Greenberg D. M. Molecular characteristics of rat liver arginase. J Biol Chem. 1968 Dec 10;243(23):6123–6129. [PubMed] [Google Scholar]
- Hokari A., Zeniya M., Esumi H. Cloning and functional expression of human inducible nitric oxide synthase (NOS) cDNA from a glioblastoma cell line A-172. J Biochem. 1994 Sep;116(3):575–581. doi: 10.1093/oxfordjournals.jbchem.a124563. [DOI] [PubMed] [Google Scholar]
- Hong J., Salo W. L., Lusty C. J., Anderson P. M. Carbamyl phosphate synthetase III, an evolutionary intermediate in the transition between glutamine-dependent and ammonia-dependent carbamyl phosphate synthetases. J Mol Biol. 1994 Oct 14;243(1):131–140. doi: 10.1006/jmbi.1994.1638. [DOI] [PubMed] [Google Scholar]
- Hooft van Huijsduijnen R., Li X. Y., Black D., Matthes H., Benoist C., Mathis D. Co-evolution from yeast to mouse: cDNA cloning of the two NF-Y (CP-1/CBF) subunits. EMBO J. 1990 Oct;9(10):3119–3127. doi: 10.1002/j.1460-2075.1990.tb07509.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Horiuchi M., Kobayashi K., Tomomura M., Kuwajima M., Imamura Y., Koizumi T., Nikaido H., Hayakawa J., Saheki T. Carnitine administration to juvenile visceral steatosis mice corrects the suppressed expression of urea cycle enzymes by normalizing their transcription. J Biol Chem. 1992 Mar 15;267(8):5032–5035. [PubMed] [Google Scholar]
- Horiuchi M., Kobayashi K., Yamaguchi S., Shimizu N., Koizumi T., Nikaido H., Hayakawa J., Kuwajima M., Saheki T. Primary defect of juvenile visceral steatosis (jvs) mouse with systemic carnitine deficiency is probably in renal carnitine transport system. Biochim Biophys Acta. 1994 Apr 12;1226(1):25–30. doi: 10.1016/0925-4439(94)90054-x. [DOI] [PubMed] [Google Scholar]
- Horwich A. L., Fenton W. A., Williams K. R., Kalousek F., Kraus J. P., Doolittle R. F., Konigsberg W., Rosenberg L. E. Structure and expression of a complementary DNA for the nuclear coded precursor of human mitochondrial ornithine transcarbamylase. Science. 1984 Jun 8;224(4653):1068–1074. doi: 10.1126/science.6372096. [DOI] [PubMed] [Google Scholar]
- Horwich A. L., Kalousek F., Fenton W. A., Pollock R. A., Rosenberg L. E. Targeting of pre-ornithine transcarbamylase to mitochondria: definition of critical regions and residues in the leader peptide. Cell. 1986 Feb 14;44(3):451–459. doi: 10.1016/0092-8674(86)90466-6. [DOI] [PubMed] [Google Scholar]
- Howell B. W., Lagacé M., Shore G. C. Activity of the carbamyl phosphate synthetase I promoter in liver nuclear extracts is dependent on a cis-acting C/EBP recognition element. Mol Cell Biol. 1989 Jul;9(7):2928–2933. doi: 10.1128/mcb.9.7.2928. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hurwitz R., Kretchmer N. Development of arginine-synthesizing enzymes in mouse intestine. Am J Physiol. 1986 Jul;251(1 Pt 1):G103–G110. doi: 10.1152/ajpgi.1986.251.1.G103. [DOI] [PubMed] [Google Scholar]
- Husson A., Renouf S., Fairand A., Buquet C., Benamar M., Vaillant R. Expression of argininosuccinate lyase mRNA in foetal hepatocytes. Regulation by glucocorticoids and insulin. Eur J Biochem. 1990 Sep 24;192(3):677–681. doi: 10.1111/j.1432-1033.1990.tb19275.x. [DOI] [PubMed] [Google Scholar]
- Imamura Y., Saheki T., Arakawa H., Noda T., Koizumi T., Nikaido H., Hayakawa J. Urea cycle disorder in C3H-H-2 degree mice with juvenile steatosis of viscera. FEBS Lett. 1990 Jan 15;260(1):119–121. doi: 10.1016/0014-5793(90)80081-s. [DOI] [PubMed] [Google Scholar]
- Irr J. D., Jacoby L. B. Control of argininosuccinate synthetase by arginine in human lymphoblasts. Somatic Cell Genet. 1978 Jan;4(1):111–124. doi: 10.1007/BF01546496. [DOI] [PubMed] [Google Scholar]
- Iwase K., Yamauchi K., Ishikawa K. Cloning of cDNAs encoding argininosuccinate lyase and arginase from Rana catesbeiana liver and regulation of their mRNAs during spontaneous and thyroid hormone-induced metamorphosis. Biochim Biophys Acta. 1995 Jan 25;1260(2):139–146. doi: 10.1016/0167-4781(94)00183-4. [DOI] [PubMed] [Google Scholar]
- Jackson M. J., Allen S. J., Beaudet A. L., O'Brien W. E. Metabolite regulation of argininosuccinate synthetase in cultured human cells. J Biol Chem. 1988 Nov 5;263(31):16388–16394. [PubMed] [Google Scholar]
- Jackson M. J., O'Brien W. E., Beaudet A. L. Arginine-mediated regulation of an argininosuccinate synthetase minigene in normal and canavanine-resistant human cells. Mol Cell Biol. 1986 Jun;6(6):2257–2261. doi: 10.1128/mcb.6.6.2257. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jackson M. J., Surh L. C., O'Brien W. E., Beaudet A. L. Assignment of the structural gene for argininosuccinate synthetase to proximal mouse chromosome 2. Genomics. 1990 Mar;6(3):545–547. doi: 10.1016/0888-7543(90)90484-c. [DOI] [PubMed] [Google Scholar]
- Jacoby L. B. Canavanine-resistant variants of human lymphoblasts. Somatic Cell Genet. 1978 Mar;4(2):221–231. doi: 10.1007/BF01538986. [DOI] [PubMed] [Google Scholar]
- Janssens S. P., Shimouchi A., Quertermous T., Bloch D. B., Bloch K. D. Cloning and expression of a cDNA encoding human endothelium-derived relaxing factor/nitric oxide synthase. J Biol Chem. 1992 Jul 25;267(21):14519–14522. [PubMed] [Google Scholar]
- Jones K. W., Shapero M. H., Chevrette M., Fournier R. E. Subtractive hybridization cloning of a tissue-specific extinguisher: TSE1 encodes a regulatory subunit of protein kinase A. Cell. 1991 Sep 6;66(5):861–872. doi: 10.1016/0092-8674(91)90433-y. [DOI] [PubMed] [Google Scholar]
- Jones S. N., Grompe M., Munir M. I., Veres G., Craigen W. J., Caskey C. T. Ectopic correction of ornithine transcarbamylase deficiency in sparse fur mice. J Biol Chem. 1990 Aug 25;265(24):14684–14690. [PubMed] [Google Scholar]
- Kadowaki Y., Toyoshima K., Yamamoto T. Ear3/COUP-TF binds most tightly to a response element with tandem repeat separated by one nucleotide. Biochem Biophys Res Commun. 1992 Mar 16;183(2):492–498. doi: 10.1016/0006-291x(92)90509-j. [DOI] [PubMed] [Google Scholar]
- Kalousek F., François B., Rosenberg L. E. Isolation and characterization of ornithine transcarbamylase from normal human liver. J Biol Chem. 1978 Jun 10;253(11):3939–3944. [PubMed] [Google Scholar]
- Kamachi Y., Kondoh H. Overlapping positive and negative regulatory elements determine lens-specific activity of the delta 1-crystallin enhancer. Mol Cell Biol. 1993 Sep;13(9):5206–5215. doi: 10.1128/mcb.13.9.5206. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kanyo Z. F., Chen C. Y., Daghigh F., Ash D. E., Christianson D. W. Crystallization and oligomeric structure of rat liver arginase. J Mol Biol. 1992 Apr 20;224(4):1175–1177. doi: 10.1016/0022-2836(92)90479-4. [DOI] [PubMed] [Google Scholar]
- Kawamoto S., Amaya Y., Murakami K., Tokunaga F., Iwanaga S., Kobayashi K., Saheki T., Kimura S., Mori M. Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver arginase. J Biol Chem. 1987 May 5;262(13):6280–6283. [PubMed] [Google Scholar]
- Kaysen G. A., Strecker H. J. Purification and properties of arginase of rat kidney. Biochem J. 1973 Aug;133(4):779–788. doi: 10.1042/bj1330779. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kelsey G., Ruppert S., Beermann F., Grund C., Tanguay R. M., Schütz G. Rescue of mice homozygous for lethal albino deletions: implications for an animal model for the human liver disease tyrosinemia type 1. Genes Dev. 1993 Dec;7(12A):2285–2297. doi: 10.1101/gad.7.12a.2285. [DOI] [PubMed] [Google Scholar]
- Kelsey G., Schütz G. Lessons from lethal albino mice. Curr Opin Genet Dev. 1993 Apr;3(2):259–264. doi: 10.1016/0959-437x(93)90032-k. [DOI] [PubMed] [Google Scholar]
- Kimball M. E., Jacoby L. B. Purification and properties of argininosuccinate synthetase from normal and canavanine-resistant human lymphoblasts. Biochemistry. 1980 Feb 19;19(4):705–709. doi: 10.1021/bi00545a015. [DOI] [PubMed] [Google Scholar]
- Kimura A., Nishiyori A., Murakami T., Tsukamoto T., Hata S., Osumi T., Okamura R., Mori M., Takiguchi M. Chicken ovalbumin upstream promoter-transcription factor (COUP-TF) represses transcription from the promoter of the gene for ornithine transcarbamylase in a manner antagonistic to hepatocyte nuclear factor-4 (HNF-4). J Biol Chem. 1993 May 25;268(15):11125–11133. [PubMed] [Google Scholar]
- Kitagawa Y. Hormonal regulation of carbamoyl-phosphate synthetase I synthesis in primary cultured hepatocytes and Reuber hepatoma H-35. Defective regulation in hepatoma cells. Eur J Biochem. 1987 Aug 17;167(1):19–25. doi: 10.1111/j.1432-1033.1987.tb13299.x. [DOI] [PubMed] [Google Scholar]
- Kitagawa Y., Ryall J., Nguyen M., Shore G. C. Expression of carbamoyl-phosphate synthetase I mRNA in Reuber hepatoma H-35 cells. Regulation by glucocorticoid and insulin. Biochim Biophys Acta. 1985 Jun 24;825(2):148–153. doi: 10.1016/0167-4781(85)90098-3. [DOI] [PubMed] [Google Scholar]
- Kitagawa Y., Sugimoto E. Interaction between glucocorticoids, 8-bromoadenosine 3',5'-monophosphate, and insulin in regulation of synthesis of carbamoyl-phosphate synthetase I in Reuber hepatoma H-35. Eur J Biochem. 1985 Jul 15;150(2):249–254. doi: 10.1111/j.1432-1033.1985.tb09014.x. [DOI] [PubMed] [Google Scholar]
- Klebig M. L., Russell L. B., Rinchik E. M. Murine fumarylacetoacetate hydrolase (Fah) gene is disrupted by a neonatally lethal albino deletion that defines the hepatocyte-specific developmental regulation 1 (hsdr-1) locus. Proc Natl Acad Sci U S A. 1992 Feb 15;89(4):1363–1367. doi: 10.1073/pnas.89.4.1363. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kliewer S. A., Umesono K., Heyman R. A., Mangelsdorf D. J., Dyck J. A., Evans R. M. Retinoid X receptor-COUP-TF interactions modulate retinoic acid signaling. Proc Natl Acad Sci U S A. 1992 Feb 15;89(4):1448–1452. doi: 10.1073/pnas.89.4.1448. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kliewer S. A., Umesono K., Noonan D. J., Heyman R. A., Evans R. M. Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors. Nature. 1992 Aug 27;358(6389):771–774. doi: 10.1038/358771a0. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Knowles R. G., Moncada S. Nitric oxide synthases in mammals. Biochem J. 1994 Mar 1;298(Pt 2):249–258. doi: 10.1042/bj2980249. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kondoh H., Araki I., Yasuda K., Matsubasa T., Mori M. Expression of the chicken 'delta 2-crystallin' gene in mouse cells: evidence for encoding of argininosuccinate lyase. Gene. 1991 Mar 15;99(2):267–271. doi: 10.1016/0378-1119(91)90137-z. [DOI] [PubMed] [Google Scholar]
- Kraus J. P., Hodges P. E., Williamson C. L., Horwich A. L., Kalousek F., Williams K. R., Rosenberg L. E. A cDNA clone for the precursor of rat mitochondrial ornithine transcarbamylase: comparison of rat and human leader sequences and conservation of catalytic sites. Nucleic Acids Res. 1985 Feb 11;13(3):943–952. doi: 10.1093/nar/13.3.943. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lagacé M., Goping I. S., Mueller C. R., Lazzaro M., Shore G. C. The carbamyl phosphate synthetase promoter contains multiple binding sites for C/EBP-related proteins. Gene. 1992 Sep 10;118(2):231–238. doi: 10.1016/0378-1119(92)90193-s. [DOI] [PubMed] [Google Scholar]
- Lagacé M., Howell B. W., Burak R., Lusty C. J., Shore G. C. Rat carbamyl-phosphate synthetase I gene. Promoter sequence and tissue-specific transcriptional regulation in vitro. J Biol Chem. 1987 Aug 5;262(22):10415–10418. [PubMed] [Google Scholar]
- Lai E., Prezioso V. R., Smith E., Litvin O., Costa R. H., Darnell J. E., Jr HNF-3A, a hepatocyte-enriched transcription factor of novel structure is regulated transcriptionally. Genes Dev. 1990 Aug;4(8):1427–1436. doi: 10.1101/gad.4.8.1427. [DOI] [PubMed] [Google Scholar]
- Lai E., Prezioso V. R., Tao W. F., Chen W. S., Darnell J. E., Jr Hepatocyte nuclear factor 3 alpha belongs to a gene family in mammals that is homologous to the Drosophila homeotic gene fork head. Genes Dev. 1991 Mar;5(3):416–427. doi: 10.1101/gad.5.3.416. [DOI] [PubMed] [Google Scholar]
- Lamas S., Marsden P. A., Li G. K., Tempst P., Michel T. Endothelial nitric oxide synthase: molecular cloning and characterization of a distinct constitutive enzyme isoform. Proc Natl Acad Sci U S A. 1992 Jul 15;89(14):6348–6352. doi: 10.1073/pnas.89.14.6348. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lambert M. A., Simard L. R., Ray P. N., McInnes R. R. Molecular cloning of cDNA for rat argininosuccinate lyase and its expression in rat hepatoma cell lines. Mol Cell Biol. 1986 May;6(5):1722–1728. doi: 10.1128/mcb.6.5.1722. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Landschulz W. H., Johnson P. F., Adashi E. Y., Graves B. J., McKnight S. L. Isolation of a recombinant copy of the gene encoding C/EBP. Genes Dev. 1988 Jul;2(7):786–800. doi: 10.1101/gad.2.7.786. [DOI] [PubMed] [Google Scholar]
- Levillain O., Hus-Citharel A., Morel F., Bankir L. Localization of arginine synthesis along rat nephron. Am J Physiol. 1990 Dec;259(6 Pt 2):F916–F923. doi: 10.1152/ajprenal.1990.259.6.F916. [DOI] [PubMed] [Google Scholar]
- Li X., Beebe D. C. Transcriptional control of delta-crystallin gene expression in the chicken embryo lens: demonstration by a new method for measuring mRNA metabolism. Mol Cell Biol. 1993 Jun;13(6):3282–3290. doi: 10.1128/mcb.13.6.3282. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Li X., Zelenka P. S., Piatigorsky J. Differential expression of the two delta-crystallin genes in lens and non-lens tissues: shift favoring delta 2 expression from embryonic to adult chickens. Dev Dyn. 1993 Feb;196(2):114–123. doi: 10.1002/aja.1001960205. [DOI] [PubMed] [Google Scholar]
- Lin R. C., Snodgrass P. J., Rabier D. Induction of urea cycle enzymes by glucagon and dexamethasone in monolayer cultures of adult rat hepatocytes. J Biol Chem. 1982 May 10;257(9):5061–5067. [PubMed] [Google Scholar]
- Lindgren V., de Martinville B., Horwich A. L., Rosenberg L. E., Francke U. Human ornithine transcarbamylase locus mapped to band Xp21.1 near the Duchenne muscular dystrophy locus. Science. 1984 Nov 9;226(4675):698–700. doi: 10.1126/science.6494904. [DOI] [PubMed] [Google Scholar]
- Lowenstein C. J., Glatt C. S., Bredt D. S., Snyder S. H. Cloned and expressed macrophage nitric oxide synthase contrasts with the brain enzyme. Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):6711–6715. doi: 10.1073/pnas.89.15.6711. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lusty C. J. Carbamoylphosphate synthetase I of rat-liver mitochondria. Purification, properties, and polypeptide molecular weight. Eur J Biochem. 1978 Apr 17;85(2):373–383. doi: 10.1111/j.1432-1033.1978.tb12249.x. [DOI] [PubMed] [Google Scholar]
- Lusty C. J., Ratner S. Biosynthesis of urea. XIV. The quaternary structure of argininosuccinase. J Biol Chem. 1972 Nov 10;247(21):7010–7022. [PubMed] [Google Scholar]
- Lyons C. R., Orloff G. J., Cunningham J. M. Molecular cloning and functional expression of an inducible nitric oxide synthase from a murine macrophage cell line. J Biol Chem. 1992 Mar 25;267(9):6370–6374. [PubMed] [Google Scholar]
- MCLEAN P., GURNEY M. W. Effect of adrenalectomy and of growth hormone on enzymes concerned with urea synthesis in rat liver. Biochem J. 1963 Apr;87:96–104. doi: 10.1042/bj0870096. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MCLEAN P., NOVELLO F. INFLUENCE OF PANCREATIC HORMONES ON ENZYMES CONCERNED WITH UREA SYNTHESIS IN RAT LIVER. Biochem J. 1965 Feb;94:410–422. doi: 10.1042/bj0940410. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MacDougald O. A., Cornelius P., Lin F. T., Chen S. S., Lane M. D. Glucocorticoids reciprocally regulate expression of the CCAAT/enhancer-binding protein alpha and delta genes in 3T3-L1 adipocytes and white adipose tissue. J Biol Chem. 1994 Jul 22;269(29):19041–19047. [PubMed] [Google Scholar]
- Maity S. N., Sinha S., Ruteshouser E. C., de Crombrugghe B. Three different polypeptides are necessary for DNA binding of the mammalian heteromeric CCAAT binding factor. J Biol Chem. 1992 Aug 15;267(23):16574–16580. [PubMed] [Google Scholar]
- Maity S. N., Vuorio T., de Crombrugghe B. The B subunit of a rat heteromeric CCAAT-binding transcription factor shows a striking sequence identity with the yeast Hap2 transcription factor. Proc Natl Acad Sci U S A. 1990 Jul;87(14):5378–5382. doi: 10.1073/pnas.87.14.5378. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Malo C., Qureshi I. A., Letarte J. Postnatal maturation of enterocytes in sparse-fur mutant mice. Am J Physiol. 1986 Feb;250(2 Pt 1):G177–G184. doi: 10.1152/ajpgi.1986.250.2.G177. [DOI] [PubMed] [Google Scholar]
- Marshall M., Cohen P. P. Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. I. Isolation and subunit structure. J Biol Chem. 1972 Mar 25;247(6):1641–1653. [PubMed] [Google Scholar]
- Matsubasa T., Takiguchi M., Amaya Y., Matsuda I., Mori M. Structure of the rat argininosuccinate lyase gene: close similarity to chicken delta-crystallin genes. Proc Natl Acad Sci U S A. 1989 Jan;86(2):592–596. doi: 10.1073/pnas.86.2.592. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Matsubasa T., Takiguchi M., Matsuda I., Mori M. Rat argininosuccinate lyase promoter: the dyad-symmetric CCAAT box sequence CCAATTGG in the promoter is recognized by NF-Y. J Biochem. 1994 Nov;116(5):1044–1055. doi: 10.1093/oxfordjournals.jbchem.a124626. [DOI] [PubMed] [Google Scholar]
- Matuo S., Tatsuno M., Kobayashi K., Saheki T., Miyata T., Iwanaga S., Amaya Y., Mori M. Isolation of cDNA clones of human argininosuccinate lyase and corrected amino acid sequence. FEBS Lett. 1988 Jul 18;234(2):395–399. doi: 10.1016/0014-5793(88)80124-8. [DOI] [PubMed] [Google Scholar]
- McIntyre P., Graf L., Mercer J. F., Wake S. A., Hudson P., Hoogenraad N. The primary structure of the imported mitochondrial protein, ornithine transcarbamylase from rat liver: mRNA levels during ontogeny. DNA. 1985 Apr;4(2):147–156. doi: 10.1089/dna.1985.4.147. [DOI] [PubMed] [Google Scholar]
- McKnight S. L., Lane M. D., Gluecksohn-Waelsch S. Is CCAAT/enhancer-binding protein a central regulator of energy metabolism? Genes Dev. 1989 Dec;3(12B):2021–2024. doi: 10.1101/gad.3.12b.2021. [DOI] [PubMed] [Google Scholar]
- Meijer A. J., Lamers W. H., Chamuleau R. A. Nitrogen metabolism and ornithine cycle function. Physiol Rev. 1990 Jul;70(3):701–748. doi: 10.1152/physrev.1990.70.3.701. [DOI] [PubMed] [Google Scholar]
- Mietus-Snyder M., Sladek F. M., Ginsburg G. S., Kuo C. F., Ladias J. A., Darnell J. E., Jr, Karathanasis S. K. Antagonism between apolipoprotein AI regulatory protein 1, Ear3/COUP-TF, and hepatocyte nuclear factor 4 modulates apolipoprotein CIII gene expression in liver and intestinal cells. Mol Cell Biol. 1992 Apr;12(4):1708–1718. doi: 10.1128/mcb.12.4.1708. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mitchell G. A., Looney J. E., Brody L. C., Steel G., Suchanek M., Engelhardt J. F., Willard H. F., Valle D. Human ornithine-delta-aminotransferase. cDNA cloning and analysis of the structural gene. J Biol Chem. 1988 Oct 5;263(28):14288–14295. [PubMed] [Google Scholar]
- Miyajima N., Kadowaki Y., Fukushige S., Shimizu S., Semba K., Yamanashi Y., Matsubara K., Toyoshima K., Yamamoto T. Identification of two novel members of erbA superfamily by molecular cloning: the gene products of the two are highly related to each other. Nucleic Acids Res. 1988 Dec 9;16(23):11057–11074. doi: 10.1093/nar/16.23.11057. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Moorman A. F., De Boer P. A., Das A. T., Labruyère W. T., Charles R., Lamers W. H. Expression patterns of mRNAs for ammonia-metabolizing enzymes in the developing rat: the ontogenesis of hepatocyte heterogeneity. Histochem J. 1990 Sep;22(9):457–468. doi: 10.1007/BF01007229. [DOI] [PubMed] [Google Scholar]
- Moorman A. F., de Boer P. A., Charles R., Lamers W. H. Diet- and hormone-induced reversal of the carbamoylphosphate synthetase mRNA gradient in the rat liver lobulus. FEBS Lett. 1990 Dec 10;276(1-2):9–13. doi: 10.1016/0014-5793(90)80494-4. [DOI] [PubMed] [Google Scholar]
- Mori M., Miura S., Tatibana M., Cohen P. P. Cell-free translation of carbamyl phosphate synthetase I and ornithine transcarbamylase messenger RNAs of rat liver. Effect of dietary protein and fasting on translatable mRNA levels. J Biol Chem. 1981 Apr 25;256(8):4127–4132. [PubMed] [Google Scholar]
- Mori M., Tatibana M. Purification of homogeneous glutamine-dependent carbamyl phosphate synthetase from ascites hepatoma cells as a complex with aspartate transcarbamylase and dihydroorotase. J Biochem. 1975 Jul;78(1):239–242. [PubMed] [Google Scholar]
- Morris S. M., Jr, Kepka D. M., Sweeney W. E., Jr, Avner E. D. Abundance of mRNAs encoding urea cycle enzymes in fetal and neonatal mouse liver. Arch Biochem Biophys. 1989 Feb 15;269(1):175–180. doi: 10.1016/0003-9861(89)90097-0. [DOI] [PubMed] [Google Scholar]
- Morris S. M., Jr, Moncman C. L., Holub J. S., Hod Y. Nutritional and hormonal regulation of mRNA abundance for arginine biosynthetic enzymes in kidney. Arch Biochem Biophys. 1989 Aug 15;273(1):230–237. doi: 10.1016/0003-9861(89)90183-5. [DOI] [PubMed] [Google Scholar]
- Morris S. M., Jr, Moncman C. L., Kepka D. M., Nebes V. L., Diven W. F., Dizikes G. J., Cederbaum S. D., DeFranco D. Effects of deletions in mouse chromosome 7 on expression of genes encoding the urea-cycle enzymes and phosphoenolpyruvate carboxykinase (GTP) in liver, kidney, and intestine. Biochem Genet. 1988 Dec;26(11-12):769–781. doi: 10.1007/BF02395522. [DOI] [PubMed] [Google Scholar]
- Morris S. M., Jr, Moncman C. L., Rand K. D., Dizikes G. J., Cederbaum S. D., O'Brien W. E. Regulation of mRNA levels for five urea cycle enzymes in rat liver by diet, cyclic AMP, and glucocorticoids. Arch Biochem Biophys. 1987 Jul;256(1):343–353. doi: 10.1016/0003-9861(87)90455-3. [DOI] [PubMed] [Google Scholar]
- Morris S. M., Jr Regulation of enzymes of urea and arginine synthesis. Annu Rev Nutr. 1992;12:81–101. doi: 10.1146/annurev.nu.12.070192.000501. [DOI] [PubMed] [Google Scholar]
- Morris S. M., Jr, Sweeney W. E., Jr, Kepka D. M., O'Brien W. E., Avner E. D. Localization of arginine biosynthetic enzymes in renal proximal tubules and abundance of mRNA during development. Pediatr Res. 1991 Feb;29(2):151–154. doi: 10.1203/00006450-199102000-00010. [DOI] [PubMed] [Google Scholar]
- Morris S. M., Jr Thyroxine elicits divergent changes in mRNA levels for two urea cycle enzymes and one gluconeogenic enzyme in tadpole liver. Arch Biochem Biophys. 1987 Nov 15;259(1):144–148. doi: 10.1016/0003-9861(87)90479-6. [DOI] [PubMed] [Google Scholar]
- Mueller C. R., Maire P., Schibler U. DBP, a liver-enriched transcriptional activator, is expressed late in ontogeny and its tissue specificity is determined posttranscriptionally. Cell. 1990 Apr 20;61(2):279–291. doi: 10.1016/0092-8674(90)90808-r. [DOI] [PubMed] [Google Scholar]
- Mullins L. J., Veres G., Caskey C. T., Chapman V. Differential methylation of the ornithine carbamoyl transferase gene on active and inactive mouse X chromosomes. Mol Cell Biol. 1987 Nov;7(11):3916–3922. doi: 10.1128/mcb.7.11.3916. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Murakami T., Nishiyori A., Takiguchi M., Mori M. Promoter and 11-kilobase upstream enhancer elements responsible for hepatoma cell-specific expression of the rat ornithine transcarbamylase gene. Mol Cell Biol. 1990 Mar;10(3):1180–1191. doi: 10.1128/mcb.10.3.1180. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Murakami T., Takiguchi M., Inomoto T., Yamamura K., Mori M. Tissue- and developmental stage-specific expression of the rat ornithine carbamoyltransferase gene in transgenic mice. Dev Genet. 1989;10(5):393–401. doi: 10.1002/dvg.1020100507. [DOI] [PubMed] [Google Scholar]
- Nakane M., Schmidt H. H., Pollock J. S., Förstermann U., Murad F. Cloned human brain nitric oxide synthase is highly expressed in skeletal muscle. FEBS Lett. 1993 Jan 25;316(2):175–180. doi: 10.1016/0014-5793(93)81210-q. [DOI] [PubMed] [Google Scholar]
- Nakshatri H., Chambon P. The directly repeated RG(G/T)TCA motifs of the rat and mouse cellular retinol-binding protein II genes are promiscuous binding sites for RAR, RXR, HNF-4, and ARP-1 homo- and heterodimers. J Biol Chem. 1994 Jan 14;269(2):890–902. [PubMed] [Google Scholar]
- Nathan C., Xie Q. W. Regulation of biosynthesis of nitric oxide. J Biol Chem. 1994 May 13;269(19):13725–13728. [PubMed] [Google Scholar]
- Nebes V. L., Morris S. M., Jr Regulation of messenger ribonucleic acid levels for five urea cycle enzymes in cultured rat hepatocytes. Requirements for cyclic adenosine monophosphate, glucocorticoids, and ongoing protein synthesis. Mol Endocrinol. 1988 May;2(5):444–451. doi: 10.1210/mend-2-5-444. [DOI] [PubMed] [Google Scholar]
- Nguyen M., Argan C., Lusty C. J., Shore G. C. Import and processing of hybrid proteins by mammalian mitochondria in vitro. J Biol Chem. 1986 Jan 15;261(2):800–805. [PubMed] [Google Scholar]
- Nickerson J. M., Wawrousek E. F., Borras T., Hawkins J. W., Norman B. L., Filpula D. R., Nagle J. W., Ally A. H., Piatigorsky J. Sequence of the chicken delta 2 crystallin gene and its intergenic spacer. Extreme homology with the delta 1 crystallin gene. J Biol Chem. 1986 Jan 15;261(2):552–557. [PubMed] [Google Scholar]
- Nickerson J. M., Wawrousek E. F., Hawkins J. W., Wakil A. S., Wistow G. J., Thomas G., Norman B. L., Piatigorsky J. The complete sequence of the chicken delta 1 crystallin gene and its 5' flanking region. J Biol Chem. 1985 Aug 5;260(16):9100–9105. [PubMed] [Google Scholar]
- Nicoletti M., Guerri C., Grisolia S. Turnover of carbamyl-phosphate synthase, of other mitochondrial enzymes and of rat tissues. Effect of diet and of thyroidectomy. Eur J Biochem. 1977 May 16;75(2):583–592. doi: 10.1111/j.1432-1033.1977.tb11558.x. [DOI] [PubMed] [Google Scholar]
- Nishiyori A., Tashiro H., Kimura A., Akagi K., Yamamura K., Mori M., Takiguchi M. Determination of tissue specificity of the enhancer by combinatorial operation of tissue-enriched transcription factors. Both HNF-4 and C/EBP beta are required for liver-specific activity of the ornithine transcarbamylase enhancer. J Biol Chem. 1994 Jan 14;269(2):1323–1331. [PubMed] [Google Scholar]
- Niwa A., Yamamoto K., Yasumura Y. Establishment of a rat hepatoma cell line which has ornithine carbamoyltransferase activity and grows continuously in arginine-deprived medium. J Cell Physiol. 1979 Jan;98(1):177–184. doi: 10.1002/jcp.1040980119. [DOI] [PubMed] [Google Scholar]
- Nomiyama H., Obaru K., Jinno Y., Matsuda I., Shimada K., Miyata T. Amplification of human argininosuccinate synthetase pseudogenes. J Mol Biol. 1986 Nov 20;192(2):221–233. doi: 10.1016/0022-2836(86)90361-x. [DOI] [PubMed] [Google Scholar]
- Northrup H., Lathrop M., Lu S. Y., Daiger S. P., Beaudet A. L., O'Brien W. E. Multilocus linkage analysis with the human argininosuccinate synthetase gene. Genomics. 1989 Oct;5(3):442–444. doi: 10.1016/0888-7543(89)90007-4. [DOI] [PubMed] [Google Scholar]
- Nunokawa Y., Ishida N., Tanaka S. Cloning of inducible nitric oxide synthase in rat vascular smooth muscle cells. Biochem Biophys Res Commun. 1993 Feb 26;191(1):89–94. doi: 10.1006/bbrc.1993.1188. [DOI] [PubMed] [Google Scholar]
- Nussler A. K., Billiar T. R., Liu Z. Z., Morris S. M., Jr Coinduction of nitric oxide synthase and argininosuccinate synthetase in a murine macrophage cell line. Implications for regulation of nitric oxide production. J Biol Chem. 1994 Jan 14;269(2):1257–1261. [PubMed] [Google Scholar]
- Nuzum C. T., Snodgrass P. J. Urea cycle enzyme adaptation to dietary protein in primates. Science. 1971 Jun 4;172(3987):1042–1043. doi: 10.1126/science.172.3987.1042. [DOI] [PubMed] [Google Scholar]
- Nyunoya H., Broglie K. E., Widgren E. E., Lusty C. J. Characterization and derivation of the gene coding for mitochondrial carbamyl phosphate synthetase I of rat. J Biol Chem. 1985 Aug 5;260(16):9346–9356. [PubMed] [Google Scholar]
- O'Brien W. E., Barr R. H. Argininosuccinate lyase: purification and characterization from human liver. Biochemistry. 1981 Mar 31;20(7):2056–2060. doi: 10.1021/bi00510a049. [DOI] [PubMed] [Google Scholar]
- O'Brien W. E. Isolation and characterization of argininosuccinate synthetase from human liver. Biochemistry. 1979 Nov 27;18(24):5353–5356. doi: 10.1021/bi00591a015. [DOI] [PubMed] [Google Scholar]
- O'Brien W. E., McInnes R., Kalumuck K., Adcock M. Cloning and sequence analysis of cDNA for human argininosuccinate lyase. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7211–7215. doi: 10.1073/pnas.83.19.7211. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ogura T., Yokoyama T., Fujisawa H., Kurashima Y., Esumi H. Structural diversity of neuronal nitric oxide synthase mRNA in the nervous system. Biochem Biophys Res Commun. 1993 Jun 30;193(3):1014–1022. doi: 10.1006/bbrc.1993.1726. [DOI] [PubMed] [Google Scholar]
- Ohno M., Sakamoto H., Yasuda K., Okada T. S., Shimura Y. Nucleotide sequence of a chicken delta-crystallin gene. Nucleic Acids Res. 1985 Mar 11;13(5):1593–1606. doi: 10.1093/nar/13.5.1593. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ohtake A., Takiguchi M., Shigeto Y., Amaya Y., Kawamoto S., Mori M. Structural organization of the gene for rat liver-type arginase. J Biol Chem. 1988 Feb 15;263(5):2245–2249. [PubMed] [Google Scholar]
- Palekar A. G., Mantagos S. Human liver arginiosuccinase purification and partial characterization. J Biol Chem. 1981 Sep 10;256(17):9192–9194. [PubMed] [Google Scholar]
- Parker D. S., Wawrousek E. F., Piatigorsky J. Expression of the delta-crystallin genes in the embryonic chicken lens. Dev Biol. 1988 Apr;126(2):375–381. doi: 10.1016/0012-1606(88)90147-9. [DOI] [PubMed] [Google Scholar]
- Patterton D., Shi Y. B. Thyroid hormone-dependent differential regulation of multiple arginase genes during amphibian metamorphosis. J Biol Chem. 1994 Oct 14;269(41):25328–25334. [PubMed] [Google Scholar]
- Paulus H. The evolutionary history of the ornithine cycle as a determinant of its structure and regulation. Curr Top Cell Regul. 1983;22:177–200. doi: 10.1016/b978-0-12-152822-5.50010-5. [DOI] [PubMed] [Google Scholar]
- Penninckx M., Simon J. P., Wiame J. M. Interaction between arginase and L-ornithine carbamoyltransferase in Saccharomyces cerevisiae. Purification of S. cerevisiae enzymes and evidence that these enzymes as well as rat-liver arginase are trimers. Eur J Biochem. 1974 Nov 15;49(2):429–442. doi: 10.1111/j.1432-1033.1974.tb03848.x. [DOI] [PubMed] [Google Scholar]
- Piatigorsky J. Puzzle of crystallin diversity in eye lenses. Dev Dyn. 1993 Apr;196(4):267–272. doi: 10.1002/aja.1001960408. [DOI] [PubMed] [Google Scholar]
- Pierson D. L., Brien J. M. Human carbamylphosphate synthetase I. Stabilization, purification, and partial characterization of the enzyme from human liver. J Biol Chem. 1980 Aug 25;255(16):7891–7895. [PubMed] [Google Scholar]
- Pierson D. L., Cox S. L., Gilbert B. E. Human ornithine transcarbamylase. Purification and characterization of the enzyme from normal liver and the liver of a Reye's syndrome patient. J Biol Chem. 1977 Sep 25;252(18):6464–6469. [PubMed] [Google Scholar]
- Poli V., Mancini F. P., Cortese R. IL-6DBP, a nuclear protein involved in interleukin-6 signal transduction, defines a new family of leucine zipper proteins related to C/EBP. Cell. 1990 Nov 2;63(3):643–653. doi: 10.1016/0092-8674(90)90459-r. [DOI] [PubMed] [Google Scholar]
- Raijman L., Jones M. E. Purification, composition, and some properties of rat liver carbamyl phosphate synthetase (ammonia). Arch Biochem Biophys. 1976 Jul;175(1):270–278. doi: 10.1016/0003-9861(76)90508-7. [DOI] [PubMed] [Google Scholar]
- Ratner S. A radiochemical assay for argininosuccinate synthetase with [U-14C]aspartate. Anal Biochem. 1983 Dec;135(2):479–488. doi: 10.1016/0003-2697(83)90716-9. [DOI] [PubMed] [Google Scholar]
- Ratner S. Argininosuccinate synthetase of bovine liver: chemical and physical properties. Proc Natl Acad Sci U S A. 1982 Sep;79(17):5197–5199. doi: 10.1073/pnas.79.17.5197. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ratner S., Murakami-Murofushi K. A new radiochemical assay for argininosuccinase with purified [14C]argininosuccinate. Anal Biochem. 1980 Jul 15;106(1):134–147. doi: 10.1016/0003-2697(80)90129-3. [DOI] [PubMed] [Google Scholar]
- Renouf S., Buquet C., Fairand A., Benamar M., Husson A. Changes in levels of argininosuccinate lyase mRNA during induction by glucagon and cyclic AMP in cultured foetal-rat hepatocytes. Biochem J. 1993 Apr 15;291(Pt 2):609–613. doi: 10.1042/bj2910609. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ringold G. M., Yamamoto K. R., Bishop J. M., Varmus H. E. Glucocorticoid-stimulated accumulation of mouse mammary tumor virus RNA: increased rate of synthesis of viral RNA. Proc Natl Acad Sci U S A. 1977 Jul;74(7):2879–2883. doi: 10.1073/pnas.74.7.2879. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ruppert S., Boshart M., Bosch F. X., Schmid W., Fournier R. E., Schütz G. Two genetically defined trans-acting loci coordinately regulate overlapping sets of liver-specific genes. Cell. 1990 Jun 1;61(5):895–904. doi: 10.1016/0092-8674(90)90200-x. [DOI] [PubMed] [Google Scholar]
- Ruppert S., Kelsey G., Schedl A., Schmid E., Thies E., Schütz G. Deficiency of an enzyme of tyrosine metabolism underlies altered gene expression in newborn liver of lethal albino mice. Genes Dev. 1992 Aug;6(8):1430–1443. doi: 10.1101/gad.6.8.1430. [DOI] [PubMed] [Google Scholar]
- Russell L. B., Russell W. L., Kelly E. M. Analysis of the albino-locus region of the mouse. I. Origin and viability. Genetics. 1979 Jan;91(1):127–139. doi: 10.1093/genetics/91.1.127. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ryall J. C., Quantz M. A., Shore G. C. Rat liver and intestinal mucosa differ in the developmental pattern and hormonal regulation of carbamoyl-phosphate synthetase I and ornithine carbamoyl transferase gene expression. Eur J Biochem. 1986 May 2;156(3):453–458. doi: 10.1111/j.1432-1033.1986.tb09603.x. [DOI] [PubMed] [Google Scholar]
- Ryall J., Nguyen M., Bendayan M., Shore G. C. Expression of nuclear genes encoding the urea cycle enzymes, carbamoyl-phosphate synthetase I and ornithine carbamoyl transferase, in rat liver and intestinal mucosa. Eur J Biochem. 1985 Oct 15;152(2):287–292. doi: 10.1111/j.1432-1033.1985.tb09196.x. [DOI] [PubMed] [Google Scholar]
- SCHIMKE R. T. Adaptive characteristics of urea cycle enzymes in the rat. J Biol Chem. 1962 Feb;237:459–468. [PubMed] [Google Scholar]
- SCHIMKE R. T. Differential effects of fasting and protein-free diets on levels of urea cycle enzymes in rat liver. J Biol Chem. 1962 Jun;237:1921–1924. [PubMed] [Google Scholar]
- SCHIMKE R. T. ENZYMES OF ARGININE METABOLISM IN MAMMALIAN CELL CULTURE. I. REPRESSION OF ARGININOSUCCINATE SYNTHETASE AND ARGININOSUCCINASE. J Biol Chem. 1964 Jan;239:136–145. [PubMed] [Google Scholar]
- SCHIMKE R. T. Studies on factors affecting the levels of urea cycle enzymes in rat liver. J Biol Chem. 1963 Mar;238:1012–1018. [PubMed] [Google Scholar]
- SCHIMKE R. T. THE IMPORTANCE OF BOTH SYNTHESIS AND DEGRADATION IN THE CONTROL OF ARGINASE LEVELS IN RAT LIVER. J Biol Chem. 1964 Nov;239:3808–3817. [PubMed] [Google Scholar]
- Saheki T., Kusumi T., Takada S., Katsunuma T., Katunuma N. Crystallization and some properties of argininosuccinate synthase from rat liver. FEBS Lett. 1975 Oct 15;58(1):314–317. doi: 10.1016/0014-5793(75)80287-0. [DOI] [PubMed] [Google Scholar]
- Saheki T., Sase M., Nakano K., Azuma F., Katsunuma T. Some properties of argininosuccinate synthetase purified from human liver and a comparison with the rat liver enzyme. J Biochem. 1983 Jun;93(6):1531–1537. doi: 10.1093/oxfordjournals.jbchem.a134291. [DOI] [PubMed] [Google Scholar]
- Santoro C., Mermod N., Andrews P. C., Tjian R. A family of human CCAAT-box-binding proteins active in transcription and DNA replication: cloning and expression of multiple cDNAs. Nature. 1988 Jul 21;334(6179):218–224. doi: 10.1038/334218a0. [DOI] [PubMed] [Google Scholar]
- Scherer S. E., Veres G., Caskey C. T. The genetic structure of mouse ornithine transcarbamylase. Nucleic Acids Res. 1988 Feb 25;16(4):1593–1601. doi: 10.1093/nar/16.4.1593. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sherman P. A., Laubach V. E., Reep B. R., Wood E. R. Purification and cDNA sequence of an inducible nitric oxide synthase from a human tumor cell line. Biochemistry. 1993 Nov 2;32(43):11600–11605. doi: 10.1021/bi00094a017. [DOI] [PubMed] [Google Scholar]
- Shigesada K., Tatibana M. N-Acetylglutamate synthetase from rat-liver mitochondria. Partial purification and catalytic properties. Eur J Biochem. 1978 Mar;84(1):285–291. doi: 10.1111/j.1432-1033.1978.tb12167.x. [DOI] [PubMed] [Google Scholar]
- Shull J. D., Pennington K. L., Rader A. E. Promoter region of the rat gene encoding ornithine aminotransferase: transcriptional activity, sequence, and DNase-I-hypersensitive sites. Gene. 1993 Mar 30;125(2):169–175. doi: 10.1016/0378-1119(93)90324-v. [DOI] [PubMed] [Google Scholar]
- Simmer J. P., Kelly R. E., Rinker A. G., Jr, Scully J. L., Evans D. R. Mammalian carbamyl phosphate synthetase (CPS). DNA sequence and evolution of the CPS domain of the Syrian hamster multifunctional protein CAD. J Biol Chem. 1990 Jun 25;265(18):10395–10402. [PubMed] [Google Scholar]
- Skrzypek-Osiecka I., Robin Y., Porembska Z. Purification of rat kidney arginases A1 and A4 and their subcellular distribution. Acta Biochim Pol. 1983;30(1):83–92. [PubMed] [Google Scholar]
- Sladek F. M., Zhong W. M., Lai E., Darnell J. E., Jr Liver-enriched transcription factor HNF-4 is a novel member of the steroid hormone receptor superfamily. Genes Dev. 1990 Dec;4(12B):2353–2365. doi: 10.1101/gad.4.12b.2353. [DOI] [PubMed] [Google Scholar]
- Snodgrass P. J., Lin R. C., Müller W. A., Aoki T. T. Induction of urea cycle enzymes of rat liver by glucagon. J Biol Chem. 1978 Apr 25;253(8):2748–2753. [PubMed] [Google Scholar]
- Sonoda T., Tatibana M. Purification of N-acetyl-L-glutamate synthetase from rat liver mitochondria and substrate and activator specificity of the enzyme. J Biol Chem. 1983 Aug 25;258(16):9839–9844. [PubMed] [Google Scholar]
- Sparkes R. S., Dizikes G. J., Klisak I., Grody W. W., Mohandas T., Heinzmann C., Zollman S., Lusis A. J., Cederbaum S. D. The gene for human liver arginase (ARG1) is assigned to chromosome band 6q23. Am J Hum Genet. 1986 Aug;39(2):186–193. [PMC free article] [PubMed] [Google Scholar]
- Spolarics Z., Bond J. S. Multiple molecular forms of mouse liver arginase. Arch Biochem Biophys. 1988 Jan;260(1):469–479. doi: 10.1016/0003-9861(88)90471-7. [DOI] [PubMed] [Google Scholar]
- Su T. S., Beaudet A. L., O'Brien W. E. Increased translatable messenger ribonucleic acid for argininosuccinate synthetase in canavanine-resistant human cells. Biochemistry. 1981 May 12;20(10):2956–2960. doi: 10.1021/bi00513a037. [DOI] [PubMed] [Google Scholar]
- Su T. S., Bock H. G., O'Brien W. E., Beaudet A. L. Cloning of cDNA for argininosuccinate synthetase mRNA and study of enzyme overproduction in a human cell line. J Biol Chem. 1981 Nov 25;256(22):11826–11831. [PubMed] [Google Scholar]
- Surh L. C., Beaudet A. L., O'Brien W. E. Molecular characterization of the murine argininosuccinate synthetase locus. Gene. 1991 Mar 15;99(2):181–189. doi: 10.1016/0378-1119(91)90125-u. [DOI] [PubMed] [Google Scholar]
- Surh L. C., Morris S. M., O'Brien W. E., Beaudet A. L. Nucleotide sequence of the cDNA encoding the rat argininosuccinate synthetase. Nucleic Acids Res. 1988 Oct 11;16(19):9352–9352. doi: 10.1093/nar/16.19.9352. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Takiguchi M., Haraguchi Y., Mori M. Human liver-type arginase gene: structure of the gene and analysis of the promoter region. Nucleic Acids Res. 1988 Sep 26;16(18):8789–8802. doi: 10.1093/nar/16.18.8789. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Takiguchi M., Matsubasa T., Amaya Y., Mori M. Evolutionary aspects of urea cycle enzyme genes. Bioessays. 1989 May;10(5):163–166. doi: 10.1002/bies.950100506. [DOI] [PubMed] [Google Scholar]
- Takiguchi M., Miura S., Mori M., Tatibana M., Nagata S., Kaziro Y. Molecular cloning and nucleotide sequence of cDNA for rat ornithine carbamoyltransferase precursor. Proc Natl Acad Sci U S A. 1984 Dec;81(23):7412–7416. doi: 10.1073/pnas.81.23.7412. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Takiguchi M., Mori M. In vitro analysis of the rat liver-type arginase promoter. J Biol Chem. 1991 May 15;266(14):9186–9193. [PubMed] [Google Scholar]
- Takiguchi M., Murakami T., Miura S., Mori M. Structure of the rat ornithine carbamoyltransferase gene, a large, X chromosome-linked gene with an atypical promoter. Proc Natl Acad Sci U S A. 1987 Sep;84(17):6136–6140. doi: 10.1073/pnas.84.17.6136. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tanaka T., Akira S., Yoshida K., Umemoto M., Yoneda Y., Shirafuji N., Fujiwara H., Suematsu S., Yoshida N., Kishimoto T. Targeted disruption of the NF-IL6 gene discloses its essential role in bacteria killing and tumor cytotoxicity by macrophages. Cell. 1995 Jan 27;80(2):353–361. doi: 10.1016/0092-8674(95)90418-2. [DOI] [PubMed] [Google Scholar]
- Tarrab R., Rodríguez J., Huitrón C., Palacios R., Soberón G. Molecular forms of rat-liver arginase. Isolation and characterization. Eur J Biochem. 1974 Nov 15;49(2):457–468. doi: 10.1111/j.1432-1033.1974.tb03850.x. [DOI] [PubMed] [Google Scholar]
- Terada K., Ohtsuka K., Imamoto N., Yoneda Y., Mori M. Role of heat shock cognate 70 protein in import of ornithine transcarbamylase precursor into mammalian mitochondria. Mol Cell Biol. 1995 Jul;15(7):3708–3713. doi: 10.1128/mcb.15.7.3708. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Thayer M. J., Fournier R. E. Hormonal regulation of TSE1-repressed genes: evidence for multiple genetic controls in extinction. Mol Cell Biol. 1989 Jul;9(7):2837–2846. doi: 10.1128/mcb.9.7.2837. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Thomas G., Zelenka P. S., Cuthbertson R. A., Norman B. L., Piatigorsky J. Differential expression of the two delta-crystallin/argininosuccinate lyase genes in lens, heart, and brain of chicken embryos. New Biol. 1990 Oct;2(10):903–914. [PubMed] [Google Scholar]
- Todd S., McGill J. R., McCombs J. L., Moore C. M., Weider I., Naylor S. L. cDNA sequence, interspecies comparison, and gene mapping analysis of argininosuccinate lyase. Genomics. 1989 Jan;4(1):53–59. doi: 10.1016/0888-7543(89)90314-5. [DOI] [PubMed] [Google Scholar]
- Tomomura M., Imamura Y., Horiuchi M., Koizumi T., Nikaido H., Hayakawa J., Saheki T. Abnormal expression of urea cycle enzyme genes in juvenile visceral steatosis (jvs) mice. Biochim Biophys Acta. 1992 Feb 14;1138(2):167–171. doi: 10.1016/0925-4439(92)90058-u. [DOI] [PubMed] [Google Scholar]
- Tomomura M., Imamura Y., Tomomura A., Horiuchi M., Saheki T. Abnormal gene expression and regulation in the liver of jvs mice with systemic carnitine deficiency. Biochim Biophys Acta. 1994 Jul 18;1226(3):307–314. doi: 10.1016/0925-4439(94)90042-6. [DOI] [PubMed] [Google Scholar]
- Tran P., Zhang X. K., Salbert G., Hermann T., Lehmann J. M., Pfahl M. COUP orphan receptors are negative regulators of retinoic acid response pathways. Mol Cell Biol. 1992 Oct;12(10):4666–4676. doi: 10.1128/mcb.12.10.4666. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tsuda M., Shikata Y., Katsunuma T. Effect of dietary proteins on the turnover of rat liver argininosuccinate synthetase. J Biochem. 1979 Mar;85(3):699–704. [PubMed] [Google Scholar]
- Tönjes R. R., Xanthopoulos K. G., Darnell J. E., Jr, Paul D. Transcriptional control in hepatocytes of normal and c14CoS albino deletion mice. EMBO J. 1992 Jan;11(1):127–133. doi: 10.1002/j.1460-2075.1992.tb05035.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ulbright C., Snodgrass P. J. Coordinate induction of the urea cycle enzymes by glucagon and dexamethasone is accomplished by three different mechanisms. Arch Biochem Biophys. 1993 Mar;301(2):237–243. doi: 10.1006/abbi.1993.1139. [DOI] [PubMed] [Google Scholar]
- Veres G., Craigen W. J., Caskey C. T. The 5' flanking region of the ornithine transcarbamylase gene contains DNA sequences regulating tissue-specific expression. J Biol Chem. 1986 Jun 15;261(17):7588–7591. [PubMed] [Google Scholar]
- Veres G., Gibbs R. A., Scherer S. E., Caskey C. T. The molecular basis of the sparse fur mouse mutation. Science. 1987 Jul 24;237(4813):415–417. doi: 10.1126/science.3603027. [DOI] [PubMed] [Google Scholar]
- Vielle-Breitburd F., Orth G. Rabbit liver L-arginase. Purification, properties, and subunit structure. J Biol Chem. 1972 Feb 25;247(4):1227–1235. [PubMed] [Google Scholar]
- Virden R. The molecular weights of two forms of carbamoyl phosphate synthase from rat liver. Biochem J. 1972 Apr;127(3):503–508. doi: 10.1042/bj1270503. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Vuorio T., Maity S. N., de Crombrugghe B. Purification and molecular cloning of the "A" chain of a rat heteromeric CCAAT-binding protein. Sequence identity with the yeast HAP3 transcription factor. J Biol Chem. 1990 Dec 25;265(36):22480–22486. [PubMed] [Google Scholar]
- Wakabayashi Y., Yamada E., Yoshida T., Takahashi H. Arginine becomes an essential amino acid after massive resection of rat small intestine. J Biol Chem. 1994 Dec 23;269(51):32667–32671. [PubMed] [Google Scholar]
- Wang L. H., Tsai S. Y., Cook R. G., Beattie W. G., Tsai M. J., O'Malley B. W. COUP transcription factor is a member of the steroid receptor superfamily. Nature. 1989 Jul 13;340(6229):163–166. doi: 10.1038/340163a0. [DOI] [PubMed] [Google Scholar]
- Wareham K. A., Lyon M. F., Glenister P. H., Williams E. D. Age related reactivation of an X-linked gene. 1987 Jun 25-Jul 1Nature. 327(6124):725–727. doi: 10.1038/327725a0. [DOI] [PubMed] [Google Scholar]
- Williams S. C., Cantwell C. A., Johnson P. F. A family of C/EBP-related proteins capable of forming covalently linked leucine zipper dimers in vitro. Genes Dev. 1991 Sep;5(9):1553–1567. doi: 10.1101/gad.5.9.1553. [DOI] [PubMed] [Google Scholar]
- Wistow G. J., Piatigorsky J. Gene conversion and splice-site slippage in the argininosuccinate lyases/delta-crystallins of the duck lens: members of an enzyme superfamily. Gene. 1990 Dec 15;96(2):263–270. doi: 10.1016/0378-1119(90)90262-p. [DOI] [PubMed] [Google Scholar]
- Wistow G. Lens crystallins: gene recruitment and evolutionary dynamism. Trends Biochem Sci. 1993 Aug;18(8):301–306. doi: 10.1016/0968-0004(93)90041-k. [DOI] [PubMed] [Google Scholar]
- Wood E. R., Berger H., Jr, Sherman P. A., Lapetina E. G. Hepatocytes and macrophages express an identical cytokine inducible nitric oxide synthase gene. Biochem Biophys Res Commun. 1993 Mar 31;191(3):767–774. doi: 10.1006/bbrc.1993.1283. [DOI] [PubMed] [Google Scholar]
- Wraight C., Lingelbach K., Hoogenraad N. Comparison of ornithine transcarbamylase from rat liver and intestine. Evidence for differential regulation of enzyme levels. Eur J Biochem. 1985 Dec 2;153(2):239–242. doi: 10.1111/j.1432-1033.1985.tb09292.x. [DOI] [PubMed] [Google Scholar]
- Xie Q. W., Cho H. J., Calaycay J., Mumford R. A., Swiderek K. M., Lee T. D., Ding A., Troso T., Nathan C. Cloning and characterization of inducible nitric oxide synthase from mouse macrophages. Science. 1992 Apr 10;256(5054):225–228. doi: 10.1126/science.1373522. [DOI] [PubMed] [Google Scholar]
- Xu Q., Baker B. S., Tata J. R. Developmental and hormonal regulation of the Xenopus liver-type arginase gene. Eur J Biochem. 1993 Feb 1;211(3):891–898. doi: 10.1111/j.1432-1033.1993.tb17622.x. [DOI] [PubMed] [Google Scholar]
- Yaoita Y., Brown D. D. A correlation of thyroid hormone receptor gene expression with amphibian metamorphosis. Genes Dev. 1990 Nov;4(11):1917–1924. doi: 10.1101/gad.4.11.1917. [DOI] [PubMed] [Google Scholar]
- Yu Y., Terada K., Nagasaki A., Takiguchi M., Mori M. Preparation of recombinant argininosuccinate synthetase and argininosuccinate lyase: expression of the enzymes in rat tissues. J Biochem. 1995 May;117(5):952–957. doi: 10.1093/oxfordjournals.jbchem.a124826. [DOI] [PubMed] [Google Scholar]
- Zintz C. B., Inana G. Analysis of the human ornithine aminotransferase gene family. Exp Eye Res. 1990 Jun;50(6):759–770. doi: 10.1016/0014-4835(90)90126-f. [DOI] [PubMed] [Google Scholar]
- de Groot C. J., Zonneveld D., de Laaf R. T., Dingemanse M. A., Mooren P. G., Moorman A. F., Lamers W. H., Charles R. Developmental and hormonal regulation of carbamoyl-phosphate synthase gene expression in rat liver: evidence for control mechanisms at different levels in the perinatal period. Biochim Biophys Acta. 1986 Feb 24;866(1):61–67. doi: 10.1016/0167-4781(86)90101-6. [DOI] [PubMed] [Google Scholar]
- de Groot C. J., van Zonneveld A. J., Mooren P. G., Zonneveld D., van den Dool A., van den Bogaert A. J., Lamers W. H., Moorman A. F., Charles R. Regulation of mRNA levels of rat liver carbamoylphosphate synthetase by glucocorticosteroids and cyclic AMP as estimated with a specific cDNA. Biochem Biophys Res Commun. 1984 Nov 14;124(3):882–888. doi: 10.1016/0006-291x(84)91040-4. [DOI] [PubMed] [Google Scholar]
- van Roon M. A., Zonneveld D., Charles R., Lamers W. H. Accumulation of carbamoylphosphate-synthetase and phosphoenolpyruvate-carboxykinase mRNA in embryonic rat hepatocytes. Evidence for translational control during the initial phases of hepatocyte-specific gene expression in vitro. Eur J Biochem. 1988 Dec 1;178(1):191–196. doi: 10.1111/j.1432-1033.1988.tb14443.x. [DOI] [PubMed] [Google Scholar]




