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Volumn 108, Issue 3, 2005, Pages 185-194

New insights into amino acid metabolism, β-cell function and diabetes

Author keywords

Amino acids; Apoptosis; Diabetes; Gene expression; Metabolism; Mitochondria; Signal transduction

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALANINE; ALANINE AMINOTRANSFERASE; AMINO ACID; ARGININE; ASPARTATE AMINOTRANSFERASE; ASPARTIC ACID; CALCIUM ION; CYCLIC AMP; GLUCOSE; GLUTAMATE DEHYDROGENASE; GLUTAMIC ACID; GLUTAMINE; GUANOSINE TRIPHOSPHATE; INSULIN; LEUCINE; MALIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 14844296371     PISSN: 01435221     EISSN: None     Source Type: Journal    
DOI: 10.1042/CS20040290     Document Type: Review
Times cited : (201)

References (85)
  • 1
    • 0018879748 scopus 로고
    • Leucine assimilation in patients with diabetes mellitus
    • Bratusch-Marrain, P., Ferenci, P. and Waldhausl, W. (1980) Leucine assimilation in patients with diabetes mellitus. Acta Endocrinol. 93, 461-465
    • (1980) Acta Endocrinol. , vol.93 , pp. 461-465
    • Bratusch-Marrain, P.1    Ferenci, P.2    Waldhausl, W.3
  • 3
    • 0029932643 scopus 로고    scopus 로고
    • New insights into pancreatic β-cell metabolic signaling in insulin secretion
    • Prentki, M. (1996) New insights into pancreatic β-cell metabolic signaling in insulin secretion. Eur. J. Endocrinol. 134, 272-286
    • (1996) Eur. J. Endocrinol. , vol.134 , pp. 272-286
    • Prentki, M.1
  • 4
    • 0030981301 scopus 로고    scopus 로고
    • Electrogenic arginine transport mediates stimulus-secretion coupling in mouse pancreatic β-cells
    • Smith, P. A., Sakura, H., Coles, B., Gummerson, N., Proks, P. and Ashcroft, F. M. (1997) Electrogenic arginine transport mediates stimulus-secretion coupling in mouse pancreatic β-cells. J. Physiol. 499, 625-635
    • (1997) J. Physiol. , vol.499 , pp. 625-635
    • Smith, P.A.1    Sakura, H.2    Coles, B.3    Gummerson, N.4    Proks, P.5    Ashcroft, F.M.6
  • 5
    • 0002582739 scopus 로고
    • Action mechanisms of amino acids in pancreatic B-cells
    • Flatt, P. and Lenzen, S., eds., Smith-Gordon, London
    • Yada, T. (1994) Action mechanisms of amino acids in pancreatic B-cells. In Frontiers of Insulin Secretion and Pancreatic β Cell Research (Flatt, P. and Lenzen, S., eds.), pp. 129-135, Smith-Gordon, London
    • (1994) Frontiers of Insulin Secretion and Pancreatic β Cell Research , pp. 129-135
    • Yada, T.1
  • 7
    • 0043169413 scopus 로고    scopus 로고
    • Amino acid ingestion strongly enhances insulin secretion in patients with long-term type 2 diabetes
    • van Loon, L. J., Kruijshoop, M., Menheere, P. P., Wagenmakers, A. J., Saris, W. H. and Keizer, H. A. (2003) Amino acid ingestion strongly enhances insulin secretion in patients with long-term type 2 diabetes. Diabetes Care 26, 625-630
    • (2003) Diabetes Care , vol.26 , pp. 625-630
    • Van Loon, L.J.1    Kruijshoop, M.2    Menheere, P.P.3    Wagenmakers, A.J.4    Saris, W.H.5    Keizer, H.A.6
  • 8
    • 0036263720 scopus 로고    scopus 로고
    • A nuclear magnetic resonance-based demonstration of substantial oxidative L-alanine metabolism and L-alanine-enhanced glucose metabolism in a clonal pancreatic β-cell line: Metabolism of L-alanine is important to the regulation of insulin secretion
    • Brennan, L., Shine, A., Hewage, C. et al. (2002) A nuclear magnetic resonance-based demonstration of substantial oxidative L-alanine metabolism and L-alanine-enhanced glucose metabolism in a clonal pancreatic β-cell line: metabolism of L-alanine is important to the regulation of insulin secretion. Diabetes 51, 1714-1721
    • (2002) Diabetes , vol.51 , pp. 1714-1721
    • Brennan, L.1    Shine, A.2    Hewage, C.3
  • 9
    • 0347287092 scopus 로고    scopus 로고
    • A comparative study of amino acid consumption by rat islet cells and the clonal β-cell line BRIN-BD11: The functional significance of L-alanine
    • Dixon, G., Nolan, J., McClenaghan, N., Flatt, P. R. and Newsholme, P. (2003) A comparative study of amino acid consumption by rat islet cells and the clonal β-cell line BRIN-BD11: the functional significance of L-alanine. J. Endocrinol. 179, 447-454
    • (2003) J. Endocrinol. , vol.179 , pp. 447-454
    • Dixon, G.1    Nolan, J.2    McClenaghan, N.3    Flatt, P.R.4    Newsholme, P.5
  • 10
    • 0019133275 scopus 로고
    • L-Leucine and a nonmetabolized analogue activate pancreatic islet glutamate dehydrogenase
    • Sener, A. and Malaisse, W. J. (1980) L-Leucine and a nonmetabolized analogue activate pancreatic islet glutamate dehydrogenase. Nature (London) 288, 187-189
    • (1980) Nature (London) , vol.288 , pp. 187-189
    • Sener, A.1    Malaisse, W.J.2
  • 11
  • 12
    • 0030891622 scopus 로고    scopus 로고
    • Regulation of pancreatic β-cell electrical activity and insulin release by physiological amino acid concentrations
    • Bolea, S., Pertusa, J. A., Martin, F., Sanchez-Andres, J. V. and Soria, B. (1997) Regulation of pancreatic β-cell electrical activity and insulin release by physiological amino acid concentrations. Pflügers Arch. 433, 699-704
    • (1997) Pflügers Arch. , vol.433 , pp. 699-704
    • Bolea, S.1    Pertusa, J.A.2    Martin, F.3    Sanchez-Andres, J.V.4    Soria, B.5
  • 14
    • 0029742094 scopus 로고    scopus 로고
    • Characterization of a novel glucose-responsive insulin-secreting cell line, BRIN-BD11, produced by electrofusion
    • McClenaghan, N. H., Barnett, C. R., Ah-Sing, E. et al. (1996) Characterization of a novel glucose-responsive insulin-secreting cell line, BRIN-BD11, produced by electrofusion. Diabetes 45, 1132-1140
    • (1996) Diabetes , vol.45 , pp. 1132-1140
    • McClenaghan, N.H.1    Barnett, C.R.2    Ah-Sing, E.3
  • 15
    • 0020317782 scopus 로고
    • The stimulus-secretion coupling of amino acid-induced insulin release. Influence of a nonmetabolized analog of leucine on the metabolism of glutamine in pancreatic islets
    • Malaisse-Lagae, F., Sener, A., Garcia-Morales, P., Valverde, I. and Malaisse, W. J. (1982) The stimulus-secretion coupling of amino acid-induced insulin release. Influence of a nonmetabolized analog of leucine on the metabolism of glutamine in pancreatic islets. J. Biol. Chem. 257, 3754-3758
    • (1982) J. Biol. Chem. , vol.257 , pp. 3754-3758
    • Malaisse-Lagae, F.1    Sener, A.2    Garcia-Morales, P.3    Valverde, I.4    Malaisse, W.J.5
  • 16
    • 0036865991 scopus 로고    scopus 로고
    • Mitochondria as the conductor of metabolic signals for insulin exocytosis in pancreatic β-cells
    • Maechler, P. (2002) Mitochondria as the conductor of metabolic signals for insulin exocytosis in pancreatic β-cells. Cell. Mol. Life Sci. 59, 1803-1818
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1803-1818
    • Maechler, P.1
  • 17
    • 0036311359 scopus 로고    scopus 로고
    • 2+, and metabolism for plasma insulin oscillations
    • 2+, and metabolism for plasma insulin oscillations. Diabetes 51 (Suppl. 1), S171-S176
    • (2002) Diabetes , vol.51 , Issue.1 SUPPL.
    • Bergsten, P.1
  • 19
    • 0026733643 scopus 로고
    • Malonyl-CoA and long chain acyl-CoA esters as metabolic coupling factors in nutrient-induced insulin secretion
    • Prentki, M., Vischer, S., Glennon, M. C., Regazzi, R., Deeney, J. T. and Corkey, B. E. (1992) Malonyl-CoA and long chain acyl-CoA esters as metabolic coupling factors in nutrient-induced insulin secretion. J. Biol. Chem. 267, 5802-5810
    • (1992) J. Biol. Chem. , vol.267 , pp. 5802-5810
    • Prentki, M.1    Vischer, S.2    Glennon, M.C.3    Regazzi, R.4    Deeney, J.T.5    Corkey, B.E.6
  • 21
    • 0035406952 scopus 로고    scopus 로고
    • Activation of acetyl-CoA carboxylase by a glutamate- and magnesium-sensitive protein phosphatase in the islet β-cell
    • Kowluru, A., Chen, H. Q., Modrick, L. M. and Stefanelli, C. (2001) Activation of acetyl-CoA carboxylase by a glutamate- and magnesium-sensitive protein phosphatase in the islet β-cell. Diabetes 50, 1580-1587
    • (2001) Diabetes , vol.50 , pp. 1580-1587
    • Kowluru, A.1    Chen, H.Q.2    Modrick, L.M.3    Stefanelli, C.4
  • 22
    • 0033118649 scopus 로고    scopus 로고
    • Contributions of mitochondria to animal physiology: From homeostatic sensor to calcium signalling and cell death
    • Duchen, M. R. (1999) Contributions of mitochondria to animal physiology: from homeostatic sensor to calcium signalling and cell death. J. Physiol. 516, 1-17
    • (1999) J. Physiol. , vol.516 , pp. 1-17
    • Duchen, M.R.1
  • 23
    • 0033531951 scopus 로고    scopus 로고
    • Glucose generates sub-plasma membrane ATP microdomains in single islet β-cells. Potential role for strategically located mitochondria
    • Kennedy, H. J., Pouli, A. E., Ainscow, E. K., Jouaville, L. S., Rizzuto, R. and Rutter, G. A. (1999) Glucose generates sub-plasma membrane ATP microdomains in single islet β-cells. Potential role for strategically located mitochondria. J. Biol. Chem. 274, 13281-13291
    • (1999) J. Biol. Chem. , vol.274 , pp. 13281-13291
    • Kennedy, H.J.1    Pouli, A.E.2    Ainscow, E.K.3    Jouaville, L.S.4    Rizzuto, R.5    Rutter, G.A.6
  • 24
    • 0030926003 scopus 로고    scopus 로고
    • Mitochondrial activation directly triggers the exocytosis of insulin in permeabilized pancreatic β-cells
    • Maechler, P., Kennedy, E. D., Pozzan, T. and Wollheim, C. B. (1997) Mitochondrial activation directly triggers the exocytosis of insulin in permeabilized pancreatic β-cells. EMBO J. 16, 3833-3841
    • (1997) EMBO J. , vol.16 , pp. 3833-3841
    • Maechler, P.1    Kennedy, E.D.2    Pozzan, T.3    Wollheim, C.B.4
  • 25
    • 0036787462 scopus 로고    scopus 로고
    • Metabolic and autocrine regulation of the mammalian target of rapamycin by pancreatic β-cells
    • McDaniel, M. L., Marshall, C. A., Pappan, K. L. and Kwon, G. (2002) Metabolic and autocrine regulation of the mammalian target of rapamycin by pancreatic β-cells. Diabetes 51, 2877-2885
    • (2002) Diabetes , vol.51 , pp. 2877-2885
    • McDaniel, M.L.1    Marshall, C.A.2    Pappan, K.L.3    Kwon, G.4
  • 26
    • 0347627140 scopus 로고    scopus 로고
    • Amino acid signalling and the integration of metabolism
    • Meijer, A. J. and Dubbelhuis, P. F. (2004) Amino acid signalling and the integration of metabolism. Biochem. Biophys. Res. Commun. 313, 397-403
    • (2004) Biochem. Biophys. Res. Commun. , vol.313 , pp. 397-403
    • Meijer, A.J.1    Dubbelhuis, P.F.2
  • 27
    • 0033125406 scopus 로고    scopus 로고
    • Amino acid-dependent signal transduction and insulin sensitivity
    • Meijer, A. J. and Sauerwein, H. P. (1999) Amino acid-dependent signal transduction and insulin sensitivity. Curr. Opin. Clin. Nutr. Metab. Care 2, 207-211
    • (1999) Curr. Opin. Clin. Nutr. Metab. Care , vol.2 , pp. 207-211
    • Meijer, A.J.1    Sauerwein, H.P.2
  • 29
    • 0020064389 scopus 로고
    • The stimulus-secretion coupling of glucose-induced insulin release. Environmental influences on L-glutamine oxidation in pancreatic islets
    • Sener, A., Malaisse-Lagae, F. and Malaisse, W.J. (1982) The stimulus-secretion coupling of glucose-induced insulin release. Environmental influences on L-glutamine oxidation in pancreatic islets. Biochem. J. 202, 309-316
    • (1982) Biochem. J. , vol.202 , pp. 309-316
    • Sener, A.1    Malaisse-Lagae, F.2    Malaisse, W.J.3
  • 30
    • 0032806183 scopus 로고    scopus 로고
    • Glucose regulation of glutaminolysis and its role in insulin secretion
    • Gao, Z. Y., Li, G., Najafi, H., Wolf, B. A. and Matschinsky, F. M. (1999) Glucose regulation of glutaminolysis and its role in insulin secretion. Diabetes 48, 1535-1542
    • (1999) Diabetes , vol.48 , pp. 1535-1542
    • Gao, Z.Y.1    Li, G.2    Najafi, H.3    Wolf, B.A.4    Matschinsky, F.M.5
  • 31
    • 0031438061 scopus 로고    scopus 로고
    • Nutrient regulation of γ-aminobutyric acid release from islet β cells
    • Smismans, A., Schuit, F. and Pipeleers, D. (1997) Nutrient regulation of γ-aminobutyric acid release from islet β cells. Diabetologia 40, 1411-1415
    • (1997) Diabetologia , vol.40 , pp. 1411-1415
    • Smismans, A.1    Schuit, F.2    Pipeleers, D.3
  • 32
    • 2642569300 scopus 로고    scopus 로고
    • Conversion into GABA (γ-aminobutyric acid) may reduce the capacity of L-glutamine as an insulin secretagogue
    • Fernandez-Pascual, S., Mukala-Nsengu-Tshibangu, A., Martin Del Rio, R. and Tamarit-Rodriguez, J. (2004) Conversion into GABA (γ-aminobutyric acid) may reduce the capacity of L-glutamine as an insulin secretagogue. Biochem J. 379, 721-729
    • (2004) Biochem J. , vol.379 , pp. 721-729
    • Fernandez-Pascual, S.1    Mukala-Nsengu-Tshibangu, A.2    Martin Del Rio, R.3    Tamarit-Rodriguez, J.4
  • 33
    • 0141987898 scopus 로고    scopus 로고
    • Glutamate-mediated signaling in the islets of Langerhans: A thread entangled
    • Moriyama, Y. and Hayashi, M. (2003) Glutamate-mediated signaling in the islets of Langerhans: a thread entangled. Trends Pharmacol. Sci. 24, 511-517
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 511-517
    • Moriyama, Y.1    Hayashi, M.2
  • 34
    • 0345548707 scopus 로고    scopus 로고
    • 13C NMR analysis reveals a link between L-glutamine metabolism, D-glucose metabolism and γ-glutamyl cycle activity in a clonal pancreatic β-cell line
    • 13C NMR analysis reveals a link between L-glutamine metabolism, D-glucose metabolism and γ-glutamyl cycle activity in a clonal pancreatic β-cell line. Diabetologia 46, 1512-1521
    • (2003) Diabetologia , vol.46 , pp. 1512-1521
    • Brennan, L.1    Corless, M.2    Hewage, C.3
  • 36
    • 11144354786 scopus 로고    scopus 로고
    • A signaling role of glutamine in insulin secretion
    • Li, C., Buettger, C., Kwagh, J. et al. (2004) A signaling role of glutamine in insulin secretion. J. Biol. Chem. 279, 13393-13401
    • (2004) J. Biol. Chem. , vol.279 , pp. 13393-13401
    • Li, C.1    Buettger, C.2    Kwagh, J.3
  • 37
    • 0033540037 scopus 로고    scopus 로고
    • Mitochondrial glutamate acts as a messenger in glucose-induced insulin exocytosis
    • Maechler, P. and Wollheim, C. B. (1999) Mitochondrial glutamate acts as a messenger in glucose-induced insulin exocytosis. Nature (London) 402, 685-689
    • (1999) Nature (London) , vol.402 , pp. 685-689
    • Maechler, P.1    Wollheim, C.B.2
  • 38
    • 0035965364 scopus 로고    scopus 로고
    • GAD65-mediated glutamate decarboxylation reduces glucose-stimulated insulin secretion in pancreatic β cells
    • Rubi, B., Ishihara, H., Hegardt, F. G., Wollheim, C. B. and Maechler, P. (2001) GAD65-mediated glutamate decarboxylation reduces glucose-stimulated insulin secretion in pancreatic β cells. J. Biol. Chem. 276, 36391-36396
    • (2001) J. Biol. Chem. , vol.276 , pp. 36391-36396
    • Rubi, B.1    Ishihara, H.2    Hegardt, F.G.3    Wollheim, C.B.4    Maechler, P.5
  • 39
    • 0037031896 scopus 로고    scopus 로고
    • The elevation of glutamate content and the amplification of insulin secretion in glucose-stimulated pancreatic islets are not causally related
    • Bertrand, G., Ishiyama, N., Nenquin, M., Ravier, M. A. and Henquin, J. C. (2002) The elevation of glutamate content and the amplification of insulin secretion in glucose-stimulated pancreatic islets are not causally related. J. Biol. Chem. 277, 32883-32891
    • (2002) J. Biol. Chem. , vol.277 , pp. 32883-32891
    • Bertrand, G.1    Ishiyama, N.2    Nenquin, M.3    Ravier, M.A.4    Henquin, J.C.5
  • 40
    • 0038540613 scopus 로고    scopus 로고
    • Mitochondria-derived glutamate at the interplay between branched-chain amino acid and glucose-induced insulin secretion
    • Broca, C., Brennan, L., Petit, P., Newsholme, P. and Maechler, P. (2003) Mitochondria-derived glutamate at the interplay between branched-chain amino acid and glucose-induced insulin secretion. FEBS Lett. 545, 167-172
    • (2003) FEBS Lett. , vol.545 , pp. 167-172
    • Broca, C.1    Brennan, L.2    Petit, P.3    Newsholme, P.4    Maechler, P.5
  • 41
    • 0014725720 scopus 로고
    • Levels of α-ketoglutarate and glutamate in stimulated pancreatic β-cells
    • Danielsson, A., Hellman, B. and Idahl, L. A. (1970) Levels of α-ketoglutarate and glutamate in stimulated pancreatic β-cells. Horm. Metab. Res. 2, 28-31
    • (1970) Horm. Metab. Res. , vol.2 , pp. 28-31
    • Danielsson, A.1    Hellman, B.2    Idahl, L.A.3
  • 42
    • 0034602141 scopus 로고    scopus 로고
    • Glutamate is not a messenger in insulin secretion
    • MacDonald, M. J. and Fahien, L. A. (2000) Glutamate is not a messenger in insulin secretion. J. Biol. Chem. 275, 34025-34027
    • (2000) J. Biol. Chem. , vol.275 , pp. 34025-34027
    • MacDonald, M.J.1    Fahien, L.A.2
  • 43
    • 0037032447 scopus 로고    scopus 로고
    • Increase in cellular glutamate levels stimulates exocytosis in pancreatic β-cells
    • Hoy, M., Maechler, P., Efanov, A. M., Wollheim, C. B., Berggren, P. O. and Gromada, J. (2002) Increase in cellular glutamate levels stimulates exocytosis in pancreatic β-cells. FEBS Lett. 531, 199-203
    • (2002) FEBS Lett. , vol.531 , pp. 199-203
    • Hoy, M.1    Maechler, P.2    Efanov, A.M.3    Wollheim, C.B.4    Berggren, P.O.5    Gromada, J.6
  • 44
    • 0035965207 scopus 로고    scopus 로고
    • Molecular and functional analysis of a novel neuronal vesicular glutamate transporter
    • Bai, L., Xu, H., Collins, J. F. and Ghishan, F. K. (2001) Molecular and functional analysis of a novel neuronal vesicular glutamate transporter. J. Biol. Chem. 276, 36764-36769
    • (2001) J. Biol. Chem. , vol.276 , pp. 36764-36769
    • Bai, L.1    Xu, H.2    Collins, J.F.3    Ghishan, F.K.4
  • 45
    • 0041802735 scopus 로고    scopus 로고
    • Glucose metabolism and glutamate analog acutely alkalinize pH of insulin secretory vesicles of pancreatic β-cells
    • Eto, K., Yamashita, T., Hirose, K. et al. (2003) Glucose metabolism and glutamate analog acutely alkalinize pH of insulin secretory vesicles of pancreatic β-cells. Am. J. Physiol. Endocrinol. Metab. 285, E262-E271
    • (2003) Am. J. Physiol. Endocrinol. Metab. , vol.285
    • Eto, K.1    Yamashita, T.2    Hirose, K.3
  • 46
    • 0015181366 scopus 로고
    • Uptake of alanine, arginine and leucine by mammalian pancreatic β-cells
    • Hellman, B., Sehlin, J. and Taljedal, I. (1971) Uptake of alanine, arginine and leucine by mammalian pancreatic β-cells. Endocrinology 89, 1432-1439
    • (1971) Endocrinology , vol.89 , pp. 1432-1439
    • Hellman, B.1    Sehlin, J.2    Taljedal, I.3
  • 48
    • 0032547303 scopus 로고    scopus 로고
    • + cotransport by metabolizable and nonmetabolizable amino acids stimulates a glucose-regulated insulin-secretory response
    • + cotransport by metabolizable and nonmetabolizable amino acids stimulates a glucose-regulated insulin-secretory response. Biochem. Biophys. Res. Commun. 249, 299-303
    • (1998) Biochem. Biophys. Res. Commun. , vol.249 , pp. 299-303
    • McClenaghan, N.H.1    Barnett, C.R.2    Flatt, P.R.3
  • 49
    • 0037057822 scopus 로고    scopus 로고
    • The stimulus-secretion coupling of amino acid-induced insulin release. Insulinotropic action of L-alanine
    • Sener, A. and Malaisse, W. J. (2002) The stimulus-secretion coupling of amino acid-induced insulin release. Insulinotropic action of L-alanine. Biochim. Biophys. Acta. 1573, 100-104
    • (2002) Biochim. Biophys. Acta. , vol.1573 , pp. 100-104
    • Sener, A.1    Malaisse, W.J.2
  • 50
    • 0017144760 scopus 로고
    • Comparison of the effects of leucines, non-metabolizable leucine analogues and other insulin secretagogues on the activity of glutamate dehydrogenase
    • Gylfe, E. (1976) Comparison of the effects of leucines, non-metabolizable leucine analogues and other insulin secretagogues on the activity of glutamate dehydrogenase. Acta Diabetol. Lat. 13, 20-24
    • (1976) Acta Diabetol. Lat. , vol.13 , pp. 20-24
    • Gylfe, E.1
  • 51
    • 0009555101 scopus 로고
    • Effects of L-leucine and α-ketoisocaproic acid upon insulin secretion and metabolism of isolated pancreatic islets
    • Panten, U., Kriegstein, E., Poser, W., Schonborn, J. and Hasselblatt, A. (1972) Effects of L-leucine and α-ketoisocaproic acid upon insulin secretion and metabolism of isolated pancreatic islets. FEBS Lett. 20, 225-228
    • (1972) FEBS Lett. , vol.20 , pp. 225-228
    • Panten, U.1    Kriegstein, E.2    Poser, W.3    Schonborn, J.4    Hasselblatt, A.5
  • 52
    • 0025967980 scopus 로고
    • Glucose regulates leucine-induced insulin release and the expression of the branched chain ketoacid dehydrogenase E1α subunit gene in pancreatic islets
    • MacDonald, M. J., McKenzie, D. I., Kaysen, J. H. et al. (1991) Glucose regulates leucine-induced insulin release and the expression of the branched chain ketoacid dehydrogenase E1α subunit gene in pancreatic islets. J. Biol. Chem. 266, 1335-1340
    • (1991) J. Biol. Chem. , vol.266 , pp. 1335-1340
    • MacDonald, M.J.1    McKenzie, D.I.2    Kaysen, J.H.3
  • 53
    • 0035091975 scopus 로고    scopus 로고
    • Protein-sensitive and fasting hypoglycemia in children with the hyperinsulinism/hyperammonemia syndrome
    • Hsu, B. Y., Kelly, A., Thornton, P. S., Greenberg, C. R., Dilling, L. A. and Stanley, C. A. (2001) Protein-sensitive and fasting hypoglycemia in children with the hyperinsulinism/hyperammonemia syndrome. J. Pediatr. 138, 383-389
    • (2001) J. Pediatr. , vol.138 , pp. 383-389
    • Hsu, B.Y.1    Kelly, A.2    Thornton, P.S.3    Greenberg, C.R.4    Dilling, L.A.5    Stanley, C.A.6
  • 54
    • 0032493123 scopus 로고    scopus 로고
    • Hyperinsulinism and hyperammonemia in infants with regulatory mutations of the glutamate dehydrogenase gene
    • Stanley, C. A., Lieu, Y. K., Hsu, B. Y. et al. (1998) Hyperinsulinism and hyperammonemia in infants with regulatory mutations of the glutamate dehydrogenase gene. N. Engl. J. Med. 338, 1352-1357
    • (1998) N. Engl. J. Med. , vol.338 , pp. 1352-1357
    • Stanley, C.A.1    Lieu, Y.K.2    Hsu, B.Y.3
  • 55
    • 0038071524 scopus 로고    scopus 로고
    • Distinguishing features of leucine and α-ketoisocaproate sensing in pancreatic β-cells
    • Gao, Z., Young, R. A., Li, G. et al. (2003) Distinguishing features of leucine and α-ketoisocaproate sensing in pancreatic β-cells. Endocrinology 144, 1949-1957
    • (2003) Endocrinology , vol.144 , pp. 1949-1957
    • Gao, Z.1    Young, R.A.2    Li, G.3
  • 56
    • 0030866101 scopus 로고    scopus 로고
    • PHAS proteins as mediators of the actions of insulin, growth factors and cAMP on protein synthesis and cell proliferation
    • Lawrence, Jr, J. C., Fadden, P., Haystead, T. A. and Lin, T. A. (1997) PHAS proteins as mediators of the actions of insulin, growth factors and cAMP on protein synthesis and cell proliferation. Adv. Enzyme. Regul. 37, 239-267
    • (1997) Adv. Enzyme. Regul. , vol.37 , pp. 239-267
    • Lawrence Jr., J.C.1    Fadden, P.2    Haystead, T.A.3    Lin, T.A.4
  • 57
    • 0033429554 scopus 로고    scopus 로고
    • Mammalian target of rapamycin is a direct target for protein kinase B: Identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation
    • Nave, B. T., Ouwens, M., Withers, D. J., Alessi, D. R. and Shepherd, P. R. (1999) Mammalian target of rapamycin is a direct target for protein kinase B: identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation. Biochem. J. 344, 427-431
    • (1999) Biochem. J. , vol.344 , pp. 427-431
    • Nave, B.T.1    Ouwens, M.2    Withers, D.J.3    Alessi, D.R.4    Shepherd, P.R.5
  • 58
    • 0035145602 scopus 로고    scopus 로고
    • Metabolic regulation by leucine of translation initiation through the mTOR-signaling pathway by pancreatic β-cells
    • Xu, G., Kwon, G., Cruz, W. S., Marshall, C. A. and McDaniel, M. L. (2001) Metabolic regulation by leucine of translation initiation through the mTOR-signaling pathway by pancreatic β-cells. Diabetes 50, 353-360
    • (2001) Diabetes , vol.50 , pp. 353-360
    • Xu, G.1    Kwon, G.2    Cruz, W.S.3    Marshall, C.A.4    McDaniel, M.L.5
  • 61
    • 0034485703 scopus 로고    scopus 로고
    • Stimulus-secretion coupling of arginine-induced insulin release: Comparison between the cationic amino acid and its methyl ester
    • Sener, A., Best, L. C., Yates, A. P. et al. (2000) Stimulus-secretion coupling of arginine-induced insulin release: comparison between the cationic amino acid and its methyl ester. Endocrine 13, 329-340
    • (2000) Endocrine , vol.13 , pp. 329-340
    • Sener, A.1    Best, L.C.2    Yates, A.P.3
  • 62
    • 0042821884 scopus 로고    scopus 로고
    • Widespread expression of arginase I in mouse tissues. Biochemical and physiological implications
    • Yu, H., Yoo, P. K., Aguirre, C. C. et al. (2003) Widespread expression of arginase I in mouse tissues. Biochemical and physiological implications. J. Histochem. Cytochem. 51, 1151-1160
    • (2003) J. Histochem. Cytochem. , vol.51 , pp. 1151-1160
    • Yu, H.1    Yoo, P.K.2    Aguirre, C.C.3
  • 63
    • 0038050529 scopus 로고    scopus 로고
    • Interorgan amino acid transport and its regulation
    • Brosnan, J. T. (2003) Interorgan amino acid transport and its regulation. J. Nutr. 133, 2068S-2072S
    • (2003) J. Nutr. , vol.133
    • Brosnan, J.T.1
  • 64
    • 0032533159 scopus 로고    scopus 로고
    • Arginine metabolism: Nitric oxide and beyond
    • Wu, G. and Morris, Jr, S. M. (1998) Arginine metabolism: nitric oxide and beyond. Biochem. J. 336, 1-17
    • (1998) Biochem. J. , vol.336 , pp. 1-17
    • Wu, G.1    Morris Jr., S.M.2
  • 65
    • 0032483516 scopus 로고    scopus 로고
    • Molecular cloning of Aralar, a new member of the mitochondrial carrier superfamily that binds calcium and is present in human muscle and brain
    • del Arco, A. and Satrustegui, J. (1998) Molecular cloning of Aralar, a new member of the mitochondrial carrier superfamily that binds calcium and is present in human muscle and brain. J. Biol. Chem. 273, 23327-23334
    • (1998) J. Biol. Chem. , vol.273 , pp. 23327-23334
    • Del Arco, A.1    Satrustegui, J.2
  • 66
    • 0034141637 scopus 로고    scopus 로고
    • Characterization of a second member of the subfamily of calcium-binding mitochondrial carriers expressed in human non-excitable tissues
    • del Arco, A., Agudo, M. and Satrustegui, J. (2000) Characterization of a second member of the subfamily of calcium-binding mitochondrial carriers expressed in human non-excitable tissues. Biochem. J. 345, 725-732
    • (2000) Biochem. J. , vol.345 , pp. 725-732
    • Del Arco, A.1    Agudo, M.2    Satrustegui, J.3
  • 67
    • 0036306987 scopus 로고    scopus 로고
    • Expression of the aspartate/glutamate mitochondrial carriers aralar1 and citrin during development and in adult rat tissues
    • del Arco, A., Morcillo, J., Martinez-Morales, J. R. et al. (2002) Expression of the aspartate/glutamate mitochondrial carriers aralar1 and citrin during development and in adult rat tissues. Eur. J. Biochem. 269, 3313-3320
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3313-3320
    • Del Arco, A.1    Morcillo, J.2    Martinez-Morales, J.R.3
  • 68
    • 17944378173 scopus 로고    scopus 로고
    • 2+-stimulated aspartate/glutamate transporters in mitochondria
    • 2+-stimulated aspartate/glutamate transporters in mitochondria. EMBO J. 20, 5060-5069
    • (2001) EMBO J. , vol.20 , pp. 5060-5069
    • Palmieri, L.1    Pardo, B.2    Lasorsa, F.M.3
  • 69
    • 0020093110 scopus 로고
    • Evidence for the malate aspartate shuttle in pancreatic islets
    • MacDonald, M. J. (1982) Evidence for the malate aspartate shuttle in pancreatic islets. Arch. Biochem. Biophys. 213, 643-649
    • (1982) Arch. Biochem. Biophys. , vol.213 , pp. 643-649
    • MacDonald, M.J.1
  • 70
    • 9544249496 scopus 로고    scopus 로고
    • Effect of mitochondrial and/or cytosolic glycerol 3-phosphate dehydrogenase overexpression on glucose-stimulated insulin secretion from MIN6 and HIT cells
    • Ishihara, H., Nakazaki, M., Kanegae, Y. et al. (1996) Effect of mitochondrial and/or cytosolic glycerol 3-phosphate dehydrogenase overexpression on glucose-stimulated insulin secretion from MIN6 and HIT cells. Diabetes 45, 1238-1244
    • (1996) Diabetes , vol.45 , pp. 1238-1244
    • Ishihara, H.1    Nakazaki, M.2    Kanegae, Y.3
  • 71
    • 0034544579 scopus 로고    scopus 로고
    • +-linked glycerol phosphate dehydrogenase has normal pancreatic β cell function but abnormal metabolite pattern in skeletal muscle
    • +-linked glycerol phosphate dehydrogenase has normal pancreatic β cell function but abnormal metabolite pattern in skeletal muscle. Arch. Biochem. Biophys. 384, 143-153
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 143-153
    • MacDonald, M.J.1    Marshall, L.K.2
  • 72
    • 0019904523 scopus 로고
    • The stimulus-secretion coupling of amino acid-induced insulin release. Metabolic response of pancreatic islets of L-glutamine and L-leucine
    • Malaisse, W. J., Sener, A., Malaisse-Lagae, F. et al. (1982) The stimulus-secretion coupling of amino acid-induced insulin release. Metabolic response of pancreatic islets of L-glutamine and L-leucine. J. Biol. Chem. 257, 8731-8737
    • (1982) J. Biol. Chem. , vol.257 , pp. 8731-8737
    • Malaisse, W.J.1    Sener, A.2    Malaisse-Lagae, F.3
  • 73
    • 0032143925 scopus 로고    scopus 로고
    • Malate-aspartate shuttle, cytoplasmic NADH redox potential and energetics in vascular smooth muscle
    • Barron, J. T., Gu, L. and Parrillo, J. E. (1998) Malate-aspartate shuttle, cytoplasmic NADH redox potential and energetics in vascular smooth muscle. J. Mol. Cell. Cardiol. 30, 1571-1579
    • (1998) J. Mol. Cell. Cardiol. , vol.30 , pp. 1571-1579
    • Barron, J.T.1    Gu, L.2    Parrillo, J.E.3
  • 74
    • 0028301431 scopus 로고
    • Dependence on NADH produced during glycolysis for β-cell glucose signaling
    • Dukes, I. D., McIntyre, M. S., Mertz, R. J. et al. (1994) Dependence on NADH produced during glycolysis for β-cell glucose signaling. J. Biol. Chem. 269, 10979-10982
    • (1994) J. Biol. Chem. , vol.269 , pp. 10979-10982
    • Dukes, I.D.1    McIntyre, M.S.2    Mertz, R.J.3
  • 75
    • 0034072556 scopus 로고    scopus 로고
    • Glucose-regulated anaplerosis and cataplerosis in pancreatic β-cells: Possible implication of a pyruvate/citrate shuttle in insulin secretion
    • Farfari, S., Schulz, V., Corkey, B. and Prentki, M. (2000) Glucose-regulated anaplerosis and cataplerosis in pancreatic β-cells: possible implication of a pyruvate/citrate shuttle in insulin secretion. Diabetes 49, 718-726
    • (2000) Diabetes , vol.49 , pp. 718-726
    • Farfari, S.1    Schulz, V.2    Corkey, B.3    Prentki, M.4
  • 76
    • 0023653356 scopus 로고
    • Aminooxyacetic acid inhibits the malate-aspartate shuttle in isolated nerve terminals and prevents the mitochondria from utilizing glycolytic substrates
    • Kauppinen, R. A., Sihra, T. S. and Nicholls, D. G. (1987) Aminooxyacetic acid inhibits the malate-aspartate shuttle in isolated nerve terminals and prevents the mitochondria from utilizing glycolytic substrates. Biochim. Biophys. Acta. 930, 173-178
    • (1987) Biochim. Biophys. Acta. , vol.930 , pp. 173-178
    • Kauppinen, R.A.1    Sihra, T.S.2    Nicholls, D.G.3
  • 77
    • 0036829678 scopus 로고    scopus 로고
    • Switch to anaerobic glucose metabolism with NADH accumulation in the β-cell model of mitochondrial diabetes. Characteristics of βHC9 cells deficient in mitochondrial DNA transcription
    • Noda, M., Yamashita, S., Takahashi, N. et al. (2002) Switch to anaerobic glucose metabolism with NADH accumulation in the β-cell model of mitochondrial diabetes. Characteristics of βHC9 cells deficient in mitochondrial DNA transcription. J. Biol. Chem. 277, 41817-41826
    • (2002) J. Biol. Chem. , vol.277 , pp. 41817-41826
    • Noda, M.1    Yamashita, S.2    Takahashi, N.3
  • 78
    • 0020524190 scopus 로고
    • Evidence of an age-related decline in mitochondrial glycerophosphate dehydrogenase activity of isolated rat islets
    • Azhar, S., Ho, H., Reaven, E. P. and Reaven, G. M. (1983) Evidence of an age-related decline in mitochondrial glycerophosphate dehydrogenase activity of isolated rat islets. Metab. Clin. Exp. 32, 1019-1021
    • (1983) Metab. Clin. Exp. , vol.32 , pp. 1019-1021
    • Azhar, S.1    Ho, H.2    Reaven, E.P.3    Reaven, G.M.4
  • 79
    • 0023730821 scopus 로고
    • Evidence for age-related changes in pyridine nucleotide content of isolated rat islets
    • Azhar, S., Ho, H. Y., Reaven, E. and Reaven, G. M. (1988) Evidence for age-related changes in pyridine nucleotide content of isolated rat islets. Horm. Metab. Res. 20, 559-561
    • (1988) Horm. Metab. Res. , vol.20 , pp. 559-561
    • Azhar, S.1    Ho, H.Y.2    Reaven, E.3    Reaven, G.M.4
  • 81
    • 0037023692 scopus 로고    scopus 로고
    • Mitochondrial metabolism sets the maximal limit of fuel-stimulated insulin secretion in a model pancreatic β cell: A survey of four fuel secretagogues
    • Antinozzi, P. A., Ishihara, H., Newgard, C. B. and Wollheim, C. B. (2002) Mitochondrial metabolism sets the maximal limit of fuel-stimulated insulin secretion in a model pancreatic β cell: a survey of four fuel secretagogues. J. Biol. Chem. 277, 11746-11755
    • (2002) J. Biol. Chem. , vol.277 , pp. 11746-11755
    • Antinozzi, P.A.1    Ishihara, H.2    Newgard, C.B.3    Wollheim, C.B.4
  • 82
    • 11244318158 scopus 로고    scopus 로고
    • The malate-aspartate NADH shuttle member aralar1 determines glucose metabolic fate, mitochondrial activity, and insulin secretion in β cells
    • Rubi, B., del Arco, A., Bartley, C., Satrustegui, J. and Maechler, P. (2004) The malate-aspartate NADH shuttle member aralar1 determines glucose metabolic fate, mitochondrial activity, and insulin secretion in β cells J. Biol. Chem. 279, 55659-55666
    • (2004) J. Biol. Chem. , vol.279 , pp. 55659-55666
    • Rubi, B.1    Del Arco, A.2    Bartley, C.3    Satrustegui, J.4    Maechler, P.5
  • 83
    • 0020049718 scopus 로고
    • The diabetic syndrome of the 'BB' Wistar rat: Possible relevance to type 1 (insulin-dependent) diabetes in man
    • Marliss, E. B., Nakhooda, A. F., Poussier, P. and Sima, A. A. (1982) The diabetic syndrome of the 'BB' Wistar rat: possible relevance to type 1 (insulin-dependent) diabetes in man. Diabetologia 22, 225-232
    • (1982) Diabetologia , vol.22 , pp. 225-232
    • Marliss, E.B.1    Nakhooda, A.F.2    Poussier, P.3    Sima, A.A.4
  • 84
    • 0035145602 scopus 로고    scopus 로고
    • Metabolic regulation by leucine of translation initiation through the mTOR signalling pathway by pancreatic β cells
    • Xu, G., Kwon, G., Cruz, W. S., Marshall, C. A. and McDaniel, M. L. (2001) Metabolic regulation by leucine of translation initiation through the mTOR signalling pathway by pancreatic β cells. Diabetes 50 353-360
    • (2001) Diabetes , vol.50 , pp. 353-360
    • Xu, G.1    Kwon, G.2    Cruz, W.S.3    Marshall, C.A.4    McDaniel, M.L.5
  • 85
    • 0034700456 scopus 로고    scopus 로고
    • Hypoinsulinaemia, glucose intolerance and diminished β-cell size in S6K1-deficient mice
    • Pende, M., Kozma, S. C., Jaquet, M. et al. (2000) Hypoinsulinaemia, glucose intolerance and diminished β-cell size in S6K1-deficient mice. Nature (London) 408 994-997
    • (2000) Nature (London) , vol.408 , pp. 994-997
    • Pende, M.1    Kozma, S.C.2    Jaquet, M.3


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