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Volumn 100, Issue SUPPL., 2010, Pages

New insights in nutritional management and amino acid supplementation in urea cycle disorders

Author keywords

Branched chain amino acids; Sodium phenylbutyrate; Urea cycle disorders

Indexed keywords

4 PHENYLBUTYRIC ACID; AMINO ACID; BRANCHED CHAIN AMINO ACID; ESSENTIAL AMINO ACID; GLUTAMINE; GLUTAMINE DERIVATIVE; PHENYLACETIC ACID; PHENYLACETYLGLUTAMINE; STABLE ISOTOPE; UNCLASSIFIED DRUG;

EID: 77950313953     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2010.02.019     Document Type: Review
Times cited : (28)

References (47)
  • 1
    • 0026029242 scopus 로고
    • Phenylacetylglutamine may replace urea as a vehicle for waste nitrogen excretion
    • Brusilow S.W. Phenylacetylglutamine may replace urea as a vehicle for waste nitrogen excretion. Pediatr. Res. 29 2 (1991) 147-150
    • (1991) Pediatr. Res. , vol.29 , Issue.2 , pp. 147-150
    • Brusilow, S.W.1
  • 2
    • 0015523324 scopus 로고
    • The conjugation of phenylacetic acid in man, sub-human primates and some non-primate species
    • James M.O., Smith R.L., Williams R.T., and Reidenberg M. The conjugation of phenylacetic acid in man, sub-human primates and some non-primate species. Proc. R. Soc. Lond. B Biol. Sci. 182 66 (1972) 25-35
    • (1972) Proc. R. Soc. Lond. B Biol. Sci. , vol.182 , Issue.66 , pp. 25-35
    • James, M.O.1    Smith, R.L.2    Williams, R.T.3    Reidenberg, M.4
  • 3
    • 0026665643 scopus 로고
    • Plasma glutamine concentration: a guide in the management of urea cycle disorders
    • Maestri N.E., McGowan K.D., and Brusilow S.W. Plasma glutamine concentration: a guide in the management of urea cycle disorders. J. Pediatr. 121 2 (1992) 259-261
    • (1992) J. Pediatr. , vol.121 , Issue.2 , pp. 259-261
    • Maestri, N.E.1    McGowan, K.D.2    Brusilow, S.W.3
  • 4
    • 0034608941 scopus 로고    scopus 로고
    • In vivo urea cycle flux distinguishes and correlates with phenotypic severity in disorders of the urea cycle
    • Lee B., Yu H., Jahoor F., O'Brien W., Beaudet A.L., and Reeds P. In vivo urea cycle flux distinguishes and correlates with phenotypic severity in disorders of the urea cycle. Proc. Natl. Acad. Sci. U. S. A. 97 14 (2000) 8021-8026
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , Issue.14 , pp. 8021-8026
    • Lee, B.1    Yu, H.2    Jahoor, F.3    O'Brien, W.4    Beaudet, A.L.5    Reeds, P.6
  • 6
    • 0029614698 scopus 로고
    • Long-term survival of patients with argininosuccinate synthetase deficiency
    • Maestri N.E., Clissold D.B., and Brusilow S.W. Long-term survival of patients with argininosuccinate synthetase deficiency. J. Pediatr. 127 6 (1995) 929-935
    • (1995) J. Pediatr. , vol.127 , Issue.6 , pp. 929-935
    • Maestri, N.E.1    Clissold, D.B.2    Brusilow, S.W.3
  • 7
    • 0031831277 scopus 로고    scopus 로고
    • Phenylbutyrate-induced glutamine depletion in humans: effect on leucine metabolism
    • Darmaun D., Welch S., Rini A., Sager B.K., Altomare A., and Haymond M.W. Phenylbutyrate-induced glutamine depletion in humans: effect on leucine metabolism. Am. J. Physiol. 274 5 Pt. 1 (1998) E801-E807
    • (1998) Am. J. Physiol. , vol.274 , Issue.5 PART 1
    • Darmaun, D.1    Welch, S.2    Rini, A.3    Sager, B.K.4    Altomare, A.5    Haymond, M.W.6
  • 8
    • 1642424401 scopus 로고    scopus 로고
    • Effect of alternative pathway therapy on branched chain amino acid metabolism in urea cycle disorder patients
    • Scaglia F., Carter S., O'Brien W.E., and Lee B. Effect of alternative pathway therapy on branched chain amino acid metabolism in urea cycle disorder patients. Mol. Genet. Metab. 81 Suppl. 1 (2004) S79-S85
    • (2004) Mol. Genet. Metab. , vol.81 , Issue.SUPPL. 1
    • Scaglia, F.1    Carter, S.2    O'Brien, W.E.3    Lee, B.4
  • 9
    • 77950308258 scopus 로고    scopus 로고
    • Role of branched-chain amino acids in patients with urea cycle disorders
    • Bachmann C., Haberle J., and Leonard J. (Eds), SPS Verlagsgesellschaft, Germany
    • Scaglia F., Lampher B., Marini J., and Lee B. Role of branched-chain amino acids in patients with urea cycle disorders. In: Bachmann C., Haberle J., and Leonard J. (Eds). International Symposium on Pathophysiology and Management of Hyperammonemia, Fulda (2007), SPS Verlagsgesellschaft, Germany 65-75
    • (2007) International Symposium on Pathophysiology and Management of Hyperammonemia, Fulda , pp. 65-75
    • Scaglia, F.1    Lampher, B.2    Marini, J.3    Lee, B.4
  • 10
    • 33947721888 scopus 로고    scopus 로고
    • Acute depletion of plasma glutamine increases leucine oxidation in prednisone-treated humans
    • Le Bacquer O., Mauras N., Welch S., Haymond M., and Darmaun D. Acute depletion of plasma glutamine increases leucine oxidation in prednisone-treated humans. Clin. Nutr. 26 2 (2007) 231-238
    • (2007) Clin. Nutr. , vol.26 , Issue.2 , pp. 231-238
    • Le Bacquer, O.1    Mauras, N.2    Welch, S.3    Haymond, M.4    Darmaun, D.5
  • 11
    • 0016220406 scopus 로고
    • Intracellular free amino acid concentration in human muscle tissue
    • Bergstrom J., Furst P., Noree L.O., and Vinnars E. Intracellular free amino acid concentration in human muscle tissue. J. Appl. Physiol. 36 6 (1974) 693-697
    • (1974) J. Appl. Physiol. , vol.36 , Issue.6 , pp. 693-697
    • Bergstrom, J.1    Furst, P.2    Noree, L.O.3    Vinnars, E.4
  • 12
    • 0025475371 scopus 로고
    • Is glutamine a conditionally essential amino acid?
    • Lacey J.M., and Wilmore D.W. Is glutamine a conditionally essential amino acid?. Nutr. Rev. 48 8 (1990) 297-309
    • (1990) Nutr. Rev. , vol.48 , Issue.8 , pp. 297-309
    • Lacey, J.M.1    Wilmore, D.W.2
  • 13
    • 0029862520 scopus 로고    scopus 로고
    • Effect of glutamine on leucine metabolism in humans
    • Hankard R.G., Haymond M.W., and Darmaun D. Effect of glutamine on leucine metabolism in humans. Am. J. Physiol. 271 4 Pt. 1 (1996) E748-E754
    • (1996) Am. J. Physiol. , vol.271 , Issue.4 PART 1
    • Hankard, R.G.1    Haymond, M.W.2    Darmaun, D.3
  • 14
    • 0025360991 scopus 로고
    • Alpha-ketoglutarate and postoperative muscle catabolism
    • Wernerman J., Hammarqvist F., and Vinnars E. Alpha-ketoglutarate and postoperative muscle catabolism. Lancet 335 8691 (1990) 701-703
    • (1990) Lancet , vol.335 , Issue.8691 , pp. 701-703
    • Wernerman, J.1    Hammarqvist, F.2    Vinnars, E.3
  • 15
    • 0036253146 scopus 로고    scopus 로고
    • Does enteral glutamine modulate whole-body leucine kinetics in hypercatabolic dogs in a fed state?
    • Humbert B., Nguyen P., Dumon H., Deschamps J.Y., and Darmaun D. Does enteral glutamine modulate whole-body leucine kinetics in hypercatabolic dogs in a fed state?. Metabolism 51 5 (2002) 628-635
    • (2002) Metabolism , vol.51 , Issue.5 , pp. 628-635
    • Humbert, B.1    Nguyen, P.2    Dumon, H.3    Deschamps, J.Y.4    Darmaun, D.5
  • 16
    • 0035142258 scopus 로고    scopus 로고
    • Effect of glutamine supplementation of the diet on tissue protein synthesis rate of glucocorticoid-treated rats
    • Boza J.J., Turini M., Moennoz D., Montigon F., Vuichoud J., Gueissaz N., et al. Effect of glutamine supplementation of the diet on tissue protein synthesis rate of glucocorticoid-treated rats. Nutrition 17 1 (2001) 35-40
    • (2001) Nutrition , vol.17 , Issue.1 , pp. 35-40
    • Boza, J.J.1    Turini, M.2    Moennoz, D.3    Montigon, F.4    Vuichoud, J.5    Gueissaz, N.6
  • 18
    • 0038339459 scopus 로고    scopus 로고
    • Glutamine preserves protein synthesis and paracellular permeability in Caco-2 cells submitted to "luminal fasting"
    • Le Bacquer O., Laboisse C., and Darmaun D. Glutamine preserves protein synthesis and paracellular permeability in Caco-2 cells submitted to "luminal fasting". Am. J. Physiol. Gastrointest. Liver Physiol. 285 1 (2003) G128-G136
    • (2003) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.285 , Issue.1
    • Le Bacquer, O.1    Laboisse, C.2    Darmaun, D.3
  • 19
    • 77950317019 scopus 로고    scopus 로고
    • Ammonia production and detoxification
    • Bachmann C., Haberle J., and Leonard J. (Eds), SPS Verlagsgesellschaft, Germany
    • Rabier D. Ammonia production and detoxification. In: Bachmann C., Haberle J., and Leonard J. (Eds). International Symposium on Pathophysiology and Management of Hyperammonemia, Fulda (2007), SPS Verlagsgesellschaft, Germany 11-24
    • (2007) International Symposium on Pathophysiology and Management of Hyperammonemia, Fulda , pp. 11-24
    • Rabier, D.1
  • 20
    • 0024492090 scopus 로고
    • Effect of parenteral glutamine peptide supplements on muscle glutamine loss and nitrogen balance after major surgery
    • Stehle P., Zander J., Mertes N., Albers S., Puchstein C., Lawin P., et al. Effect of parenteral glutamine peptide supplements on muscle glutamine loss and nitrogen balance after major surgery. Lancet 1 8632 (1989) 231-233
    • (1989) Lancet , vol.1 , Issue.8632 , pp. 231-233
    • Stehle, P.1    Zander, J.2    Mertes, N.3    Albers, S.4    Puchstein, C.5    Lawin, P.6
  • 21
    • 0031884978 scopus 로고    scopus 로고
    • Total parenteral nutrition with glutamine dipeptide after major abdominal surgery: a randomized, double-blind, controlled study
    • Morlion B.J., Stehle P., Wachtler P., Siedhoff H.P., Koller M., Konig W., et al. Total parenteral nutrition with glutamine dipeptide after major abdominal surgery: a randomized, double-blind, controlled study. Ann. Surg. 227 2 (1998) 302-308
    • (1998) Ann. Surg. , vol.227 , Issue.2 , pp. 302-308
    • Morlion, B.J.1    Stehle, P.2    Wachtler, P.3    Siedhoff, H.P.4    Koller, M.5    Konig, W.6
  • 22
    • 0029917785 scopus 로고    scopus 로고
    • ESPEN research fellows symposia-presented at ESPEN 1995, Effect of enteral glutamine on glutamine and leucine metabolism in humans
    • Hankard R.G., Haymond M.W., and Darmaun D. ESPEN research fellows symposia-presented at ESPEN 1995, Effect of enteral glutamine on glutamine and leucine metabolism in humans. Clin. Nutr. 15 2 (1996) 84-85
    • (1996) Clin. Nutr. , vol.15 , Issue.2 , pp. 84-85
    • Hankard, R.G.1    Haymond, M.W.2    Darmaun, D.3
  • 23
    • 0031911224 scopus 로고    scopus 로고
    • Oral glutamine slows down whole body protein breakdown in Duchenne muscular dystrophy
    • Hankard R.G., Hammond D., Haymond M.W., and Darmaun D. Oral glutamine slows down whole body protein breakdown in Duchenne muscular dystrophy. Pediatr. Res. 43 2 (1998) 222-226
    • (1998) Pediatr. Res. , vol.43 , Issue.2 , pp. 222-226
    • Hankard, R.G.1    Hammond, D.2    Haymond, M.W.3    Darmaun, D.4
  • 24
  • 25
    • 0016328152 scopus 로고
    • Origin and possible significance of alanine production by skeletal muscle
    • Odessey R., Khairallah E.A., and Goldberg A.L. Origin and possible significance of alanine production by skeletal muscle. J. Biol. Chem. 249 23 (1974) 7623-7629
    • (1974) J. Biol. Chem. , vol.249 , Issue.23 , pp. 7623-7629
    • Odessey, R.1    Khairallah, E.A.2    Goldberg, A.L.3
  • 27
    • 0019477082 scopus 로고
    • Why decreased serum branched-chain amino acids in cirrhosis
    • Limberg B., and Kommerell B. Why decreased serum branched-chain amino acids in cirrhosis. Gastroenterology 80 1 (1981) 211-212
    • (1981) Gastroenterology , vol.80 , Issue.1 , pp. 211-212
    • Limberg, B.1    Kommerell, B.2
  • 28
    • 0018850124 scopus 로고
    • Effect of spontaneous portal-systemic shunting on plasma insulin and amino acid concentrations
    • Iwasaki Y., Sato H., Ohkubo A., Sanjo T., Futagawa S., Sugiura M., et al. Effect of spontaneous portal-systemic shunting on plasma insulin and amino acid concentrations. Gastroenterology 78 4 (1980) 677-683
    • (1980) Gastroenterology , vol.78 , Issue.4 , pp. 677-683
    • Iwasaki, Y.1    Sato, H.2    Ohkubo, A.3    Sanjo, T.4    Futagawa, S.5    Sugiura, M.6
  • 29
    • 0024351050 scopus 로고
    • Clinical outcome of non-shunting operation for oesophageal varices in patients with liver cirrhosis
    • Matsubara S., Ouchi K., Okabe K., Suzuki M., and Matsuno S. Clinical outcome of non-shunting operation for oesophageal varices in patients with liver cirrhosis. J. Gastroenterol. Hepatol. 4 Suppl. 1 (1989) 235-238
    • (1989) J. Gastroenterol. Hepatol. , vol.4 , Issue.SUPPL. 1 , pp. 235-238
    • Matsubara, S.1    Ouchi, K.2    Okabe, K.3    Suzuki, M.4    Matsuno, S.5
  • 30
    • 0019455264 scopus 로고
    • Effects of ammonia infusion on plasma glucagon, insulin, and amino acids in intact, pancreatectomized, and adrenalectomized dogs
    • Strombeck D.R., Rogers Q.R., and Stern J.S. Effects of ammonia infusion on plasma glucagon, insulin, and amino acids in intact, pancreatectomized, and adrenalectomized dogs. Am. J. Vet. Res. 42 5 (1981) 810-818
    • (1981) Am. J. Vet. Res. , vol.42 , Issue.5 , pp. 810-818
    • Strombeck, D.R.1    Rogers, Q.R.2    Stern, J.S.3
  • 31
    • 0030296683 scopus 로고    scopus 로고
    • Hyperammonemia-induced depletion of glutamate and branched-chain amino acids in muscle and plasma
    • Leweling H., Breitkreutz R., Behne F., Staedt U., Striebel J.P., and Holm E. Hyperammonemia-induced depletion of glutamate and branched-chain amino acids in muscle and plasma. J. Hepatol. 25 5 (1996) 756-762
    • (1996) J. Hepatol. , vol.25 , Issue.5 , pp. 756-762
    • Leweling, H.1    Breitkreutz, R.2    Behne, F.3    Staedt, U.4    Striebel, J.P.5    Holm, E.6
  • 32
    • 0030861882 scopus 로고    scopus 로고
    • Impact of the putative differentiating agents sodium phenylbutyrate and sodium phenylacetate on proliferation, differentiation, and apoptosis of primary neoplastic myeloid cells
    • Gore S.D., Samid D., and Weng L.J. Impact of the putative differentiating agents sodium phenylbutyrate and sodium phenylacetate on proliferation, differentiation, and apoptosis of primary neoplastic myeloid cells. Clin. Cancer Res. 3 10 (1997) 1755-1762
    • (1997) Clin. Cancer Res. , vol.3 , Issue.10 , pp. 1755-1762
    • Gore, S.D.1    Samid, D.2    Weng, L.J.3
  • 33
    • 0034011754 scopus 로고    scopus 로고
    • Differentiation therapy in acute myelogenous leukemia (non-APL)
    • Waxman S. Differentiation therapy in acute myelogenous leukemia (non-APL). Leukemia 14 3 (2000) 491-496
    • (2000) Leukemia , vol.14 , Issue.3 , pp. 491-496
    • Waxman, S.1
  • 34
    • 0035570845 scopus 로고    scopus 로고
    • Perspectives in the treatment of malignant gliomas in adults
    • Andratschke N., Grosu A.L., Molls M., and Nieder C. Perspectives in the treatment of malignant gliomas in adults. Anticancer Res. 21 5 (2001) 3541-3550
    • (2001) Anticancer Res. , vol.21 , Issue.5 , pp. 3541-3550
    • Andratschke, N.1    Grosu, A.L.2    Molls, M.3    Nieder, C.4
  • 35
    • 33845220139 scopus 로고    scopus 로고
    • Arginase induction by sodium phenylbutyrate in mouse tissues and human cell lines
    • Kern R.M., Yang Z., Kim P.S., Grody W.W., Iyer R.K., and Cederbaum S.D. Arginase induction by sodium phenylbutyrate in mouse tissues and human cell lines. Mol. Genet. Metab. 90 1 (2007) 37-41
    • (2007) Mol. Genet. Metab. , vol.90 , Issue.1 , pp. 37-41
    • Kern, R.M.1    Yang, Z.2    Kim, P.S.3    Grody, W.W.4    Iyer, R.K.5    Cederbaum, S.D.6
  • 36
    • 0024578239 scopus 로고
    • The 2-oxo acid dehydrogenase complexes: recent advances
    • Yeaman S.J. The 2-oxo acid dehydrogenase complexes: recent advances. Biochem. J. 257 3 (1989) 625-632
    • (1989) Biochem. J. , vol.257 , Issue.3 , pp. 625-632
    • Yeaman, S.J.1
  • 37
    • 0036310982 scopus 로고    scopus 로고
    • The immunosuppressant rapamycin mimics a starvation-like signal distinct from amino acid and glucose deprivation
    • Peng T., Golub T.R., and Sabatini D.M. The immunosuppressant rapamycin mimics a starvation-like signal distinct from amino acid and glucose deprivation. Mol. Cell. Biol. 22 15 (2002) 5575-5584
    • (2002) Mol. Cell. Biol. , vol.22 , Issue.15 , pp. 5575-5584
    • Peng, T.1    Golub, T.R.2    Sabatini, D.M.3
  • 38
    • 0016824053 scopus 로고
    • Leucine. A possible regulator of protein turnover in muscle
    • Buse M.G., and Reid S.S. Leucine. A possible regulator of protein turnover in muscle. J. Clin. Invest. 56 5 (1975) 1250-1261
    • (1975) J. Clin. Invest. , vol.56 , Issue.5 , pp. 1250-1261
    • Buse, M.G.1    Reid, S.S.2
  • 39
    • 0033980371 scopus 로고    scopus 로고
    • Orally administered leucine stimulates protein synthesis in skeletal muscle of postabsorptive rats in association with increased eIF4F formation
    • Anthony J.C., Anthony T.G., Kimball S.R., Vary T.C., and Jefferson L.S. Orally administered leucine stimulates protein synthesis in skeletal muscle of postabsorptive rats in association with increased eIF4F formation. J. Nutr. 130 2 (2000) 139-145
    • (2000) J. Nutr. , vol.130 , Issue.2 , pp. 139-145
    • Anthony, J.C.1    Anthony, T.G.2    Kimball, S.R.3    Vary, T.C.4    Jefferson, L.S.5
  • 40
    • 0033808169 scopus 로고    scopus 로고
    • Leucine stimulates translation initiation in skeletal muscle of postabsorptive rats via a rapamycin-sensitive pathway
    • Anthony J.C., Yoshizawa F., Anthony T.G., Vary T.C., Jefferson L.S., and Kimball S.R. Leucine stimulates translation initiation in skeletal muscle of postabsorptive rats via a rapamycin-sensitive pathway. J. Nutr. 130 10 (2000) 2413-2419
    • (2000) J. Nutr. , vol.130 , Issue.10 , pp. 2413-2419
    • Anthony, J.C.1    Yoshizawa, F.2    Anthony, T.G.3    Vary, T.C.4    Jefferson, L.S.5    Kimball, S.R.6
  • 41
    • 32044465506 scopus 로고    scopus 로고
    • Signaling in growth and metabolism
    • Wullschleger S., Loewith R., and Hall M.N. Signaling in growth and metabolism. Cell 124 3 (2006) 471-484
    • (2006) Cell , vol.124 , Issue.3 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 42
    • 84934444765 scopus 로고    scopus 로고
    • Amino acid regulation of autophagosome formation
    • Meijer A.J. Amino acid regulation of autophagosome formation. Methods Mol. Biol. 445 (2008) 89-109
    • (2008) Methods Mol. Biol. , vol.445 , pp. 89-109
    • Meijer, A.J.1
  • 43
    • 0034830022 scopus 로고    scopus 로고
    • Leucine and insulin activate p70 S6 kinase through different pathways in human skeletal muscle
    • Greiwe J.S., Kwon G., McDaniel M.L., and Semenkovich C.F. Leucine and insulin activate p70 S6 kinase through different pathways in human skeletal muscle. Am. J. Physiol. Endocrinol. Metab. 281 3 (2001) E466-E471
    • (2001) Am. J. Physiol. Endocrinol. Metab. , vol.281 , Issue.3
    • Greiwe, J.S.1    Kwon, G.2    McDaniel, M.L.3    Semenkovich, C.F.4
  • 44
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • Hay N., and Sonenberg N. Upstream and downstream of mTOR. Genes Dev. 18 16 (2004) 1926-1945
    • (2004) Genes Dev. , vol.18 , Issue.16 , pp. 1926-1945
    • Hay, N.1    Sonenberg, N.2
  • 45
    • 0037178786 scopus 로고    scopus 로고
    • mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery
    • Kim D.H., Sarbassov D.D., Ali S.M., King J.E., Latek R.R., Erdjument-Bromage H., et al. mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 110 2 (2002) 163-175
    • (2002) Cell , vol.110 , Issue.2 , pp. 163-175
    • Kim, D.H.1    Sarbassov, D.D.2    Ali, S.M.3    King, J.E.4    Latek, R.R.5    Erdjument-Bromage, H.6
  • 47
    • 40849103247 scopus 로고    scopus 로고
    • Hyperammonemia: Review of current treatment strategies
    • Bachmann C., Haberle J., and Leonard J. (Eds), SPS Verlagsgesellschaft, Germany
    • Bachmann C. Hyperammonemia: Review of current treatment strategies. In: Bachmann C., Haberle J., and Leonard J. (Eds). International Symposium on Pathophysiology and Management of Hyperammonemia, Fulda (2007), SPS Verlagsgesellschaft, Germany 157-173
    • (2007) International Symposium on Pathophysiology and Management of Hyperammonemia, Fulda , pp. 157-173
    • Bachmann, C.1


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