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Volumn 57, Issue 1, 2008, Pages 9-23

l-Arginine metabolism in dog kidney and isolated nephron segments

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMMONIA; ARGINASE; ARGINASE 2; ARGININE; ARGININOSUCCINATE SYNTHASE; CITRULLINE; GLUCOSE; GLUTAMIC ACID; LYASE; ORNITHINE; ORNITHINE OXOACID AMINOTRANSFERASE; PROLINE; UNCLASSIFIED DRUG;

EID: 36849084090     PISSN: 00260495     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.metabol.2007.06.001     Document Type: Article
Times cited : (9)

References (77)
  • 1
    • 0032533159 scopus 로고    scopus 로고
    • Arginine metabolism: nitric oxide and beyond
    • Wu G.Y., and Morris Jr. S.M. Arginine metabolism: nitric oxide and beyond. Biochem J 336 (1998) 1-17
    • (1998) Biochem J , vol.336 , pp. 1-17
    • Wu, G.Y.1    Morris Jr., S.M.2
  • 3
    • 0005143632 scopus 로고
    • The conversion of citrulline to arginine in kidney
    • Borsook H., and Dubnoff J.W. The conversion of citrulline to arginine in kidney. J Biol Chem 140 (1941) 717-738
    • (1941) J Biol Chem , vol.140 , pp. 717-738
    • Borsook, H.1    Dubnoff, J.W.2
  • 4
    • 0015547712 scopus 로고
    • Relative importance of kidney and liver in synthesis of arginine by the rat
    • Featherston W.R., Rogers Q.R., and Freedland R.A. Relative importance of kidney and liver in synthesis of arginine by the rat. Am J Physiol 224 (1973) 127-129
    • (1973) Am J Physiol , vol.224 , pp. 127-129
    • Featherston, W.R.1    Rogers, Q.R.2    Freedland, R.A.3
  • 6
    • 0032850644 scopus 로고    scopus 로고
    • Expression of the genes of arginine-synthesizing enzymes in the rat during development
    • Goutal I., Fairand A., and Husson A. Expression of the genes of arginine-synthesizing enzymes in the rat during development. Biol Neonate 76 (1999) 253-260
    • (1999) Biol Neonate , vol.76 , pp. 253-260
    • Goutal, I.1    Fairand, A.2    Husson, A.3
  • 7
    • 0037198034 scopus 로고    scopus 로고
    • The "intestinal-renal" arginine biosynthetic axis in the aging rat
    • Mistry S.K., Greenfeld Z., Morris Jr. S.M., and Baylis C. The "intestinal-renal" arginine biosynthetic axis in the aging rat. Mech Ageing Dev 123 (2002) 1159-1165
    • (2002) Mech Ageing Dev , vol.123 , pp. 1159-1165
    • Mistry, S.K.1    Greenfeld, Z.2    Morris Jr., S.M.3    Baylis, C.4
  • 8
    • 0025963628 scopus 로고
    • Localization of arginine biosynthetic enzymes in renal proximal tubules and abundance of mRNA during development
    • Morris Jr. S.M., Sweeney Jr. W.E., Kepka D.M., O'brien W.E., and Avner E.D. Localization of arginine biosynthetic enzymes in renal proximal tubules and abundance of mRNA during development. Ped Res 25 (1991) 151-154
    • (1991) Ped Res , vol.25 , pp. 151-154
    • Morris Jr., S.M.1    Sweeney Jr., W.E.2    Kepka, D.M.3    O'brien, W.E.4    Avner, E.D.5
  • 9
    • 0015373190 scopus 로고
    • In vivo synthesis and utilization of arginine in the rat
    • Rogers Q.R., Freedland R.A., and Symmons R.A. In vivo synthesis and utilization of arginine in the rat. Am J Physiol 223 (1972) 236-240
    • (1972) Am J Physiol , vol.223 , pp. 236-240
    • Rogers, Q.R.1    Freedland, R.A.2    Symmons, R.A.3
  • 10
    • 0024321362 scopus 로고
    • Nutritional and hormonal regulation of mRNA abundance for arginine biosynthetic enzymes in kidney
    • Morris Jr. S.M., Moncman C.L., Holub J.S., and Hod Y. Nutritional and hormonal regulation of mRNA abundance for arginine biosynthetic enzymes in kidney. Arch Biochem Biophys 273 (1989) 230-237
    • (1989) Arch Biochem Biophys , vol.273 , pp. 230-237
    • Morris Jr., S.M.1    Moncman, C.L.2    Holub, J.S.3    Hod, Y.4
  • 11
    • 0029013321 scopus 로고
    • Preparation of recombinant argininosuccinate synthetase and argininosuccinate lyase: expression of the enzymes in rat tissues
    • Yu Y., Terada K., Nagasaki A., Takiguchi M., and Mori M. Preparation of recombinant argininosuccinate synthetase and argininosuccinate lyase: expression of the enzymes in rat tissues. J Biochem 117 (1995) 952-957
    • (1995) J Biochem , vol.117 , pp. 952-957
    • Yu, Y.1    Terada, K.2    Nagasaki, A.3    Takiguchi, M.4    Mori, M.5
  • 12
    • 0034751685 scopus 로고    scopus 로고
    • Compensatory changes in enzymes of arginine metabolism during renal hypertrophy in mice
    • Natesan S., and Reddy S.R. Compensatory changes in enzymes of arginine metabolism during renal hypertrophy in mice. Comp Biochem Physiol B 130 (2001) 585-595
    • (2001) Comp Biochem Physiol B , vol.130 , pp. 585-595
    • Natesan, S.1    Reddy, S.R.2
  • 14
    • 0027376333 scopus 로고
    • Renal synthesis of arginine in chronic renal failure: in vivo and in vitro studies in rats with 5/6 nephrectomy
    • Bouby N., Hassler C., Parvy P., and Bankir L. Renal synthesis of arginine in chronic renal failure: in vivo and in vitro studies in rats with 5/6 nephrectomy. Kidney Int 44 (1993) 676-683
    • (1993) Kidney Int , vol.44 , pp. 676-683
    • Bouby, N.1    Hassler, C.2    Parvy, P.3    Bankir, L.4
  • 15
  • 16
    • 4744340573 scopus 로고    scopus 로고
    • In vivo whole body and organ arginine metabolism during endotoxemia (sepsis) is dependent on mouse strain and gender
    • [discussion 2796S-97S]
    • Luiking Y.C., Hallemeesch M.M., Vissers Y.L., Lamers W.H., and Deutz N.E. In vivo whole body and organ arginine metabolism during endotoxemia (sepsis) is dependent on mouse strain and gender. J Nutr 134 (2004) 2768S-2774S [discussion 2796S-97S]
    • (2004) J Nutr , vol.134
    • Luiking, Y.C.1    Hallemeesch, M.M.2    Vissers, Y.L.3    Lamers, W.H.4    Deutz, N.E.5
  • 17
    • 25444452126 scopus 로고    scopus 로고
    • Intestinal renal metabolism of l-citrulline and l-arginine following enteral or parenteral infusion of l-alanyl-l-[2,15N]glutamine or l-[2,15N]glutamine in mice
    • Boelens P.G., van Leeuwen P.A., Dejong C.H., and Deutz N.E. Intestinal renal metabolism of l-citrulline and l-arginine following enteral or parenteral infusion of l-alanyl-l-[2,15N]glutamine or l-[2,15N]glutamine in mice. Am J Physiol Gastrointest Liver Physiol 289 (2005) G679-G685
    • (2005) Am J Physiol Gastrointest Liver Physiol , vol.289
    • Boelens, P.G.1    van Leeuwen, P.A.2    Dejong, C.H.3    Deutz, N.E.4
  • 18
    • 0018953706 scopus 로고
    • Renal metabolism of amino acids and ammonia in subjects with normal renal function and in patients with chronic renal insufficiency
    • Tizianello A., De Ferrari G., Garibotto G., Gurreri G., and Robaudo C. Renal metabolism of amino acids and ammonia in subjects with normal renal function and in patients with chronic renal insufficiency. J Clin Invest 65 (1980) 1162-1173
    • (1980) J Clin Invest , vol.65 , pp. 1162-1173
    • Tizianello, A.1    De Ferrari, G.2    Garibotto, G.3    Gurreri, G.4    Robaudo, C.5
  • 19
    • 0026579609 scopus 로고
    • Cellular and subcellular localization of enzymes of arginine metabolism in rat kidney
    • Dhanakoti S.N., Brosnan M.E., Herzberg G.R., and Brosnan J.T. Cellular and subcellular localization of enzymes of arginine metabolism in rat kidney. Biochem J 282 (1992) 369-375
    • (1992) Biochem J , vol.282 , pp. 369-375
    • Dhanakoti, S.N.1    Brosnan, M.E.2    Herzberg, G.R.3    Brosnan, J.T.4
  • 20
    • 36849076918 scopus 로고    scopus 로고
    • Renal arginine synthesis in mammals
    • Pandalai S.G. (Ed), Research Signpost, Trivandrum
    • Levillain O. Renal arginine synthesis in mammals. In: Pandalai S.G. (Ed). Recent res dev physiol vol. 1 (2003), Research Signpost, Trivandrum 67-83
    • (2003) Recent res dev physiol , vol.1 , pp. 67-83
    • Levillain, O.1
  • 23
    • 7844225152 scopus 로고    scopus 로고
    • Immunohistochemical localization of arginase II and other enzymes of arginine metabolism in rat kidney and liver
    • Miyanaka K., Gotoh T., Nagasaki A., Takeya M., Ozaki M., Iwase K., et al. Immunohistochemical localization of arginase II and other enzymes of arginine metabolism in rat kidney and liver. Histochem J 30 (1998) 741-751
    • (1998) Histochem J , vol.30 , pp. 741-751
    • Miyanaka, K.1    Gotoh, T.2    Nagasaki, A.3    Takeya, M.4    Ozaki, M.5    Iwase, K.6
  • 24
    • 0014990892 scopus 로고
    • Arginase isoenzymes in liver and kidney of some mammals
    • Porembska Z., Baranczyk A., and Jachimowicz J. Arginase isoenzymes in liver and kidney of some mammals. Acta Biochim Pol 18 (1971) 77-85
    • (1971) Acta Biochim Pol , vol.18 , pp. 77-85
    • Porembska, Z.1    Baranczyk, A.2    Jachimowicz, J.3
  • 25
    • 0030477682 scopus 로고    scopus 로고
    • Comparison of influence of 2-oxoglutarate and glutamate on arginase activities in liver and kidney-cortex of rabbit, Oryctolagus cuniculus
    • Pietkiewicz J., and Bryla J. Comparison of influence of 2-oxoglutarate and glutamate on arginase activities in liver and kidney-cortex of rabbit, Oryctolagus cuniculus. Comp Biochem Physiol B 115 (1996) 393-398
    • (1996) Comp Biochem Physiol B , vol.115 , pp. 393-398
    • Pietkiewicz, J.1    Bryla, J.2
  • 26
    • 12344263036 scopus 로고
    • Effect of testosterone propionate and growth hormone on the arginase and phosphatases of the organs of the mouse
    • Kochakian C.D., and Stettner C.E. Effect of testosterone propionate and growth hormone on the arginase and phosphatases of the organs of the mouse. Am J Physiol 155 (1948) 262-264
    • (1948) Am J Physiol , vol.155 , pp. 262-264
    • Kochakian, C.D.1    Stettner, C.E.2
  • 27
    • 0343554767 scopus 로고    scopus 로고
    • Human type II arginase: sequence analysis and tissue-specific expression
    • Morris Jr. S.M., Bhamidipati D., and Kepka-Lenhart D. Human type II arginase: sequence analysis and tissue-specific expression. Gene 193 (1997) 157-161
    • (1997) Gene , vol.193 , pp. 157-161
    • Morris Jr., S.M.1    Bhamidipati, D.2    Kepka-Lenhart, D.3
  • 28
    • 0039131545 scopus 로고
    • Distribution of arginase within the kidneys of several vertebrate species
    • Robinson R.R., and Schmidt-Nielsen B. Distribution of arginase within the kidneys of several vertebrate species. J Cell Comp Physiol 62 (1963) 147-157
    • (1963) J Cell Comp Physiol , vol.62 , pp. 147-157
    • Robinson, R.R.1    Schmidt-Nielsen, B.2
  • 29
    • 0026697780 scopus 로고
    • Arginase distribution in tissues of domestic animals
    • Aminlari M., and Vaseghi T. Arginase distribution in tissues of domestic animals. Comp Biochem Physiol B 103 (1992) 385-389
    • (1992) Comp Biochem Physiol B , vol.103 , pp. 385-389
    • Aminlari, M.1    Vaseghi, T.2
  • 30
    • 0031575915 scopus 로고    scopus 로고
    • Chromosomal localization of the human arginase II gene and tissue distribution of its mRNA
    • Gotoh T., Araki M., and Mori M. Chromosomal localization of the human arginase II gene and tissue distribution of its mRNA. Biochem Biophys Res Commun 233 (1997) 487-491
    • (1997) Biochem Biophys Res Commun , vol.233 , pp. 487-491
    • Gotoh, T.1    Araki, M.2    Mori, M.3
  • 34
    • 4243326460 scopus 로고    scopus 로고
    • Distribution of arginase along the mammalian nephron
    • De Deyn P.P., Marescau B., Qureshi I.A., and Mori A. (Eds), John Libbey & Company, London
    • Levillain O., and Hus-citharel A. Distribution of arginase along the mammalian nephron. In: De Deyn P.P., Marescau B., Qureshi I.A., and Mori A. (Eds). Guanidino compounds: 2 (1996), John Libbey & Company, London 77-85
    • (1996) Guanidino compounds: 2 , pp. 77-85
    • Levillain, O.1    Hus-citharel, A.2
  • 35
    • 13744252283 scopus 로고    scopus 로고
    • Localization and differential expression of arginase II in male and female mouse kidney
    • Levillain O., Balvay S., and Peyrol S. Localization and differential expression of arginase II in male and female mouse kidney. Pflugers Arch 449 (2005) 491-503
    • (2005) Pflugers Arch , vol.449 , pp. 491-503
    • Levillain, O.1    Balvay, S.2    Peyrol, S.3
  • 36
    • 0016008023 scopus 로고
    • Activity of glycine amidinotransferase and its isoforms in dog kidney tissue normally and in acute renal insufficiency
    • Petrun N.M. Activity of glycine amidinotransferase and its isoforms in dog kidney tissue normally and in acute renal insufficiency. Ukr Biokhim Zh 46 (1974) 51-53
    • (1974) Ukr Biokhim Zh , vol.46 , pp. 51-53
    • Petrun, N.M.1
  • 37
    • 0022912744 scopus 로고
    • The purification and characterization of human kidney l-arginine:glycine amidinotransferase
    • Gross M.D., Eggen M.A., Simon A.M., and Van Pilsum J.F. The purification and characterization of human kidney l-arginine:glycine amidinotransferase. Arch Biochem Biophys 251 (1986) 747-755
    • (1986) Arch Biochem Biophys , vol.251 , pp. 747-755
    • Gross, M.D.1    Eggen, M.A.2    Simon, A.M.3    Van Pilsum, J.F.4
  • 38
    • 0022650095 scopus 로고
    • Localization of l-arginine-glycine amidinotransferase protein in rat tissues by immunofluorescence microscopy
    • McGuire D.M., Gross M.D., Elde P., and Van Pilsum J.F. Localization of l-arginine-glycine amidinotransferase protein in rat tissues by immunofluorescence microscopy. J Histochem Cytochem 34 (1986) 429-435
    • (1986) J Histochem Cytochem , vol.34 , pp. 429-435
    • McGuire, D.M.1    Gross, M.D.2    Elde, P.3    Van Pilsum, J.F.4
  • 39
    • 0003798396 scopus 로고
    • Heterogeneity of transamidinase activity and creatine content along the rat nephron
    • De Deyn P.P., Marescau B., Stalon V., and Qureshi I.A. (Eds), John Libbey & Company, London
    • Takeda M., Nakayama S., Tomino Y., Jung K.J., Endou H., and Koide H. Heterogeneity of transamidinase activity and creatine content along the rat nephron. In: De Deyn P.P., Marescau B., Stalon V., and Qureshi I.A. (Eds). Guanidino compounds in biology and medicine (1992), John Libbey & Company, London 153-157
    • (1992) Guanidino compounds in biology and medicine , pp. 153-157
    • Takeda, M.1    Nakayama, S.2    Tomino, Y.3    Jung, K.J.4    Endou, H.5    Koide, H.6
  • 40
    • 0023710732 scopus 로고
    • Characterization and metabolism of canine proximal tubules, thick ascending limbs, and collecting ducts in suspension
    • Tejedor A., Noel J., Vinay P., Boulanger Y., and Gougoux A. Characterization and metabolism of canine proximal tubules, thick ascending limbs, and collecting ducts in suspension. Can J Physiol Pharmacol 66 (1988) 997-1009
    • (1988) Can J Physiol Pharmacol , vol.66 , pp. 997-1009
    • Tejedor, A.1    Noel, J.2    Vinay, P.3    Boulanger, Y.4    Gougoux, A.5
  • 41
    • 36849047515 scopus 로고
    • BBM H+-ATPase activity in the dog kidney: modulation by substrate availability
    • Noel J., Vinay P., Laprade R., and Gougoux A. BBM H+-ATPase activity in the dog kidney: modulation by substrate availability. Kidney Int 37 (1990) 529
    • (1990) Kidney Int , vol.37 , pp. 529
    • Noel, J.1    Vinay, P.2    Laprade, R.3    Gougoux, A.4
  • 42
    • 84912681122 scopus 로고
    • Chemical methods for detection, quantitation, and identification of amino acids in body fluids
    • Bremer H.J., Duran M., Duran M., Kamerling J.P., Przyrembel H., and Wadman S.K. (Eds), Urban and Schwarzenberg, Germany
    • Bremer H.J., Duran M., Kamerling J.P., Przyrembel H., and Wadman S.K. Chemical methods for detection, quantitation, and identification of amino acids in body fluids. In: Bremer H.J., Duran M., Duran M., Kamerling J.P., Przyrembel H., and Wadman S.K. (Eds). Disturbances of amino acid metabolism: clinical chemistry and diagnosis (1981), Urban and Schwarzenberg, Germany 421-442
    • (1981) Disturbances of amino acid metabolism: clinical chemistry and diagnosis , pp. 421-442
    • Bremer, H.J.1    Duran, M.2    Kamerling, J.P.3    Przyrembel, H.4    Wadman, S.K.5
  • 43
    • 84951404090 scopus 로고
    • Photometric ninhydrin method for use in the chromatography of amino acids
    • Moore S., and Stein W.H. Photometric ninhydrin method for use in the chromatography of amino acids. J Biol Chem 176 (1948) 367-388
    • (1948) J Biol Chem , vol.176 , pp. 367-388
    • Moore, S.1    Stein, W.H.2
  • 44
    • 0021312893 scopus 로고
    • Amino acid analysis by reverse phase high-performance liquid chromatography: precolumn derivatization with phenylisothiocyanate
    • Heinrikson R.L., and Meredith S.C. Amino acid analysis by reverse phase high-performance liquid chromatography: precolumn derivatization with phenylisothiocyanate. Anal Biochem 136 (1984) 65-74
    • (1984) Anal Biochem , vol.136 , pp. 65-74
    • Heinrikson, R.L.1    Meredith, S.C.2
  • 45
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 46
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 47
    • 0031045504 scopus 로고    scopus 로고
    • Presence of argininosuccinate synthetase in glial cells as revealed by peptide-specific antisera
    • Schmidlin A., Kalbacher H., and Wiesinger H. Presence of argininosuccinate synthetase in glial cells as revealed by peptide-specific antisera. Biol Chem 378 (1997) 47-50
    • (1997) Biol Chem , vol.378 , pp. 47-50
    • Schmidlin, A.1    Kalbacher, H.2    Wiesinger, H.3
  • 48
    • 4243526712 scopus 로고    scopus 로고
    • Argininosuccinate lyase: generation of antisera against peptide sequences of the rat brain enzyme and immunochemical studies on glial cells
    • Bolla T., Kalbacher H., Vogel D., and Wiesinger H. Argininosuccinate lyase: generation of antisera against peptide sequences of the rat brain enzyme and immunochemical studies on glial cells. Biol Chem 380 (1999) S95
    • (1999) Biol Chem , vol.380
    • Bolla, T.1    Kalbacher, H.2    Vogel, D.3    Wiesinger, H.4
  • 49
    • 1642408705 scopus 로고    scopus 로고
    • Ornithine metabolism in male and female rat kidney: mitochondrial expression of ornithine aminotransferase and arginase II
    • Levillain O., Hus-Citharel A., Garvi S., Peyrol S., Reymond I., Mutin M., et al. Ornithine metabolism in male and female rat kidney: mitochondrial expression of ornithine aminotransferase and arginase II. Am J Physiol Renal Physiol 286 (2004) F727-F738
    • (2004) Am J Physiol Renal Physiol , vol.286
    • Levillain, O.1    Hus-Citharel, A.2    Garvi, S.3    Peyrol, S.4    Reymond, I.5    Mutin, M.6
  • 50
    • 0346365099 scopus 로고    scopus 로고
    • Redox-dependent modulation of aconitase activity in intact mitochondria
    • Bulteau A.L., Ikeda-Saito M., and Szweda L.I. Redox-dependent modulation of aconitase activity in intact mitochondria. Biochemistry 42 (2003) 14846-14855
    • (2003) Biochemistry , vol.42 , pp. 14846-14855
    • Bulteau, A.L.1    Ikeda-Saito, M.2    Szweda, L.I.3
  • 51
    • 0014847754 scopus 로고
    • Synthesis of serine by rat kidney in vivo and in vitro
    • Pitts R.F., Damian A.C., and MacLeod M.B. Synthesis of serine by rat kidney in vivo and in vitro. Am J Physiol 219 (1970) 584-589
    • (1970) Am J Physiol , vol.219 , pp. 584-589
    • Pitts, R.F.1    Damian, A.C.2    MacLeod, M.B.3
  • 52
    • 0015294795 scopus 로고
    • Synthesis of serine by the dog kidney in vivo
    • Pitts R.F., and MacLeod M.B. Synthesis of serine by the dog kidney in vivo. Am J Physiol 222 (1972) 394-398
    • (1972) Am J Physiol , vol.222 , pp. 394-398
    • Pitts, R.F.1    MacLeod, M.B.2
  • 53
    • 0033762719 scopus 로고    scopus 로고
    • Regional expression and histological localization of cysteine sulfate decarboxylase mRNA in the rat kidney
    • Reymond I., Bitoun M., Levillain O., and Tappaz M. Regional expression and histological localization of cysteine sulfate decarboxylase mRNA in the rat kidney. J Histochem Cytochem 48 (2000) 1461-1468
    • (2000) J Histochem Cytochem , vol.48 , pp. 1461-1468
    • Reymond, I.1    Bitoun, M.2    Levillain, O.3    Tappaz, M.4
  • 54
    • 0023687748 scopus 로고
    • The renal handling of amino acids and oligopeptides
    • Silbernagl S. The renal handling of amino acids and oligopeptides. Physiol Rev 68 (1988) 911-1007
    • (1988) Physiol Rev , vol.68 , pp. 911-1007
    • Silbernagl, S.1
  • 56
    • 0030993478 scopus 로고    scopus 로고
    • Renal handling of guanidino compounds in rat and rabbit
    • Levillain O., Marescau B., and De Deyn P.P. Renal handling of guanidino compounds in rat and rabbit. J Physiol London 499 (1997) 561-570
    • (1997) J Physiol London , vol.499 , pp. 561-570
    • Levillain, O.1    Marescau, B.2    De Deyn, P.P.3
  • 57
    • 0016863969 scopus 로고
    • Cellular localization of l-arginine reabsorption in proximal tubules of rat kidney cortex
    • Pfaller W., and Sibernagl S. Cellular localization of l-arginine reabsorption in proximal tubules of rat kidney cortex. Pflügers Arch 360 (1975) 189-192
    • (1975) Pflügers Arch , vol.360 , pp. 189-192
    • Pfaller, W.1    Sibernagl, S.2
  • 58
    • 0018938330 scopus 로고
    • Quantitative morphology of the rat kidney
    • Pfaller W., and Rittinger M. Quantitative morphology of the rat kidney. Int J Biochem 12 (1980) 17-22
    • (1980) Int J Biochem , vol.12 , pp. 17-22
    • Pfaller, W.1    Rittinger, M.2
  • 59
    • 0021986944 scopus 로고
    • Deficiency of pyrroline-5-carboxylate synthase in the intestinal mucosa of the cat
    • Rogers Q.R., and Phang J.M. Deficiency of pyrroline-5-carboxylate synthase in the intestinal mucosa of the cat. J Nutr 115 (1985) 146-150
    • (1985) J Nutr , vol.115 , pp. 146-150
    • Rogers, Q.R.1    Phang, J.M.2
  • 60
    • 0035316199 scopus 로고    scopus 로고
    • Effects of dietary l-arginine on structure and function of flow-restricted vein grafts
    • Landis M.E., Ray E.C., Gloviczki P., and Miller V.M. Effects of dietary l-arginine on structure and function of flow-restricted vein grafts. J Vasc Surg 33 (2001) 829-839
    • (2001) J Vasc Surg , vol.33 , pp. 829-839
    • Landis, M.E.1    Ray, E.C.2    Gloviczki, P.3    Miller, V.M.4
  • 63
    • 0018339929 scopus 로고
    • Structural analysis of the rabbit kidney
    • Brodal A., Van Limborgh J., Schiebler T.H., Tondury G., and Wolff E. (Eds), Springer-Verlag, Berlin
    • Kaissling B., and Kriz W. Structural analysis of the rabbit kidney. In: Brodal A., Van Limborgh J., Schiebler T.H., Tondury G., and Wolff E. (Eds). Advances in anatomy embryology and cell biology vol. 56 (1979), Springer-Verlag, Berlin
    • (1979) Advances in anatomy embryology and cell biology , vol.56
    • Kaissling, B.1    Kriz, W.2
  • 64
    • 12644261037 scopus 로고
    • Renal handling of citrulline
    • Dzurik R., Lichardus B., Guder W., Dzurik R., Lichardus B., and Guder W. (Eds), Martinus Nijhoff Publishers, Dordrecht
    • Kettner A., and Silbernagl S. Renal handling of citrulline. In: Dzurik R., Lichardus B., Guder W., Dzurik R., Lichardus B., and Guder W. (Eds). Kidney metabolism and function (1985), Martinus Nijhoff Publishers, Dordrecht 51-60
    • (1985) Kidney metabolism and function , pp. 51-60
    • Kettner, A.1    Silbernagl, S.2
  • 65
    • 0024340138 scopus 로고
    • Purification and properties of a new enzyme, NG, NG-dimethylarginine dimethylaminohydrolase, from rat kidney
    • Ogawa T., Kimoto M., and Sasaoka K. Purification and properties of a new enzyme, NG, NG-dimethylarginine dimethylaminohydrolase, from rat kidney. J Biol Chem 264 (1989) 10205-10209
    • (1989) J Biol Chem , vol.264 , pp. 10205-10209
    • Ogawa, T.1    Kimoto, M.2    Sasaoka, K.3
  • 66
    • 0031464899 scopus 로고    scopus 로고
    • Colocalization of dimethylating enzymes and NOS functional effects of methylarginines in rat kidney
    • Tojo A., Welch W.J., Bremer V., Kimoto M., Kimura K., Omata M., et al. Colocalization of dimethylating enzymes and NOS functional effects of methylarginines in rat kidney. Kidney Int 52 (1997) 1593-1601
    • (1997) Kidney Int , vol.52 , pp. 1593-1601
    • Tojo, A.1    Welch, W.J.2    Bremer, V.3    Kimoto, M.4    Kimura, K.5    Omata, M.6
  • 67
    • 0015450081 scopus 로고
    • l-Arginine transport in rat proximal tubules
    • Silbernagl S., and Deetjen P. l-Arginine transport in rat proximal tubules. Pflügers Arch 336 (1972) 79-86
    • (1972) Pflügers Arch , vol.336 , pp. 79-86
    • Silbernagl, S.1    Deetjen, P.2
  • 68
    • 0030597114 scopus 로고    scopus 로고
    • Molecular cloning of cDNA for nonhepatic mitochondrial arginase (arginase II) and comparison of its induction with nitric oxide synthase in a murine macrophage-like cell line
    • Gotoh T., Sonoki T., Nagasaki A., Terada K., Takiguchi M., and Mori M. Molecular cloning of cDNA for nonhepatic mitochondrial arginase (arginase II) and comparison of its induction with nitric oxide synthase in a murine macrophage-like cell line. FEBS Lett 395 (1996) 119-122
    • (1996) FEBS Lett , vol.395 , pp. 119-122
    • Gotoh, T.1    Sonoki, T.2    Nagasaki, A.3    Terada, K.4    Takiguchi, M.5    Mori, M.6
  • 70
    • 0015864848 scopus 로고
    • Effects of high and low protein diets on sheep renal function and metabolism
    • Rabinowitz L., Gunther R.A., Shoji E.S., Freedland R.A., and Avery E.H. Effects of high and low protein diets on sheep renal function and metabolism. Kidney Int 4 (1973) 188-207
    • (1973) Kidney Int , vol.4 , pp. 188-207
    • Rabinowitz, L.1    Gunther, R.A.2    Shoji, E.S.3    Freedland, R.A.4    Avery, E.H.5
  • 71
    • 0024307184 scopus 로고
    • Production of urea from arginine in pars recta and collecting duct of the rat kidney
    • Levillain O., Hus-citharel A., Morel F., and Bankir L. Production of urea from arginine in pars recta and collecting duct of the rat kidney. Ren Physiol Biochem 12 (1989) 302-312
    • (1989) Ren Physiol Biochem , vol.12 , pp. 302-312
    • Levillain, O.1    Hus-citharel, A.2    Morel, F.3    Bankir, L.4
  • 72
    • 0020536675 scopus 로고
    • Mitochondrial metabolism of glutamine and glutamate and its physiological significance
    • Kovacevic Z., and McGivan J.D. Mitochondrial metabolism of glutamine and glutamate and its physiological significance. Physiol Rev 63 (1983) 547-605
    • (1983) Physiol Rev , vol.63 , pp. 547-605
    • Kovacevic, Z.1    McGivan, J.D.2
  • 73
    • 0023025425 scopus 로고
    • ATP turnover and renal response of dog tubules to pH changes in vitro
    • Manillier C., Vinay P., Lalonde L., and Gougoux A. ATP turnover and renal response of dog tubules to pH changes in vitro. Am J Physiol 251 (1986) F919-F932
    • (1986) Am J Physiol , vol.251
    • Manillier, C.1    Vinay, P.2    Lalonde, L.3    Gougoux, A.4
  • 74
    • 0025650951 scopus 로고
    • Phosphate-dependent glutaminase activity in renal cortical and medullary tubule segments
    • Wright P.A., and Knepper M.A. Phosphate-dependent glutaminase activity in renal cortical and medullary tubule segments. Am J Physiol Renal Fluid Electrolyte Physiol 259 (1990) F961-F970
    • (1990) Am J Physiol Renal Fluid Electrolyte Physiol , vol.259
    • Wright, P.A.1    Knepper, M.A.2
  • 75
    • 0025003679 scopus 로고
    • Glutamate dehydrogenase activities in microdissected rat nephron segments: effects of acid-base loading
    • Wright P.A., and Knepper M.A. Glutamate dehydrogenase activities in microdissected rat nephron segments: effects of acid-base loading. Am J Physiol Renal Fluid Electrolyte Physiol 259 (1990) F53-F59
    • (1990) Am J Physiol Renal Fluid Electrolyte Physiol , vol.259
    • Wright, P.A.1    Knepper, M.A.2
  • 77
    • 0017176862 scopus 로고
    • Glutamine synthetase and glutamyltransferase in the kidney of man, dog, and rat
    • Lemieux G., Baverel G., Vinay P., and Wadoux P. Glutamine synthetase and glutamyltransferase in the kidney of man, dog, and rat. Am J Physiol 231 (1976) 1068-1073
    • (1976) Am J Physiol , vol.231 , pp. 1068-1073
    • Lemieux, G.1    Baverel, G.2    Vinay, P.3    Wadoux, P.4


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