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Volumn 1760, Issue 11, 2006, Pages 1741-1748

Pyrroloquinoline quinone nutritional status alters lysine metabolism and modulates mitochondrial DNA content in the mouse and rat

Author keywords

aminoadipic semialdehyde dehydrogenase; Lysine metabolism; Mitochondria; Pyrroloquinoline quinone

Indexed keywords

2 AMINOADIPIC ACID; ALDEHYDE DERIVATIVE; ALPHA AMINOADIPATE DELTA SEMIALDEHYDE DEHYDROGENASE; ALPHA AMINOADIPIC SEMIALDEHYDE; AMINO ACID; GLYCINE; LYSINE; MESSENGER RNA; MITOCHONDRIAL DNA; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; PYRROLOQUINOLINE QUINONE; QUINONE DERIVATIVE; SERINE; UNCLASSIFIED DRUG;

EID: 33750526669     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2006.07.009     Document Type: Article
Times cited : (41)

References (43)
  • 1
    • 0242668745 scopus 로고    scopus 로고
    • Nutritional biochemistry: a new redox-cofactor vitamin for mammals
    • Kasahara T., and Kato T. Nutritional biochemistry: a new redox-cofactor vitamin for mammals. Nature 422 (2003) 832
    • (2003) Nature , vol.422 , pp. 832
    • Kasahara, T.1    Kato, T.2
  • 2
    • 0035716604 scopus 로고    scopus 로고
    • Identification of the alpha-aminoadipic-delta-semialdehyde dehydrogenase-phosphopantetheinyl transferase gene, the human ortholog of the yeast LYS5 gene
    • Praphanphoj V., Sacksteder K.A., Gould S.J., Thomas G.H., and Geraghty M.T. Identification of the alpha-aminoadipic-delta-semialdehyde dehydrogenase-phosphopantetheinyl transferase gene, the human ortholog of the yeast LYS5 gene. Mol. Genet. Metab. 72 (2001) 336-342
    • (2001) Mol. Genet. Metab. , vol.72 , pp. 336-342
    • Praphanphoj, V.1    Sacksteder, K.A.2    Gould, S.J.3    Thomas, G.H.4    Geraghty, M.T.5
  • 3
    • 24744449999 scopus 로고    scopus 로고
    • Cloning and characterization of a novel human homolog of mouse U26, a putative PQQ-dependent AAS dehydrogenase
    • Wang L., Jil C., Xu Y., Xu J., Dai J., Wu Q., Wu M., Zou X., Sun L., Gu S., Xie Y., and Mao Y. Cloning and characterization of a novel human homolog of mouse U26, a putative PQQ-dependent AAS dehydrogenase. Mol. Biol. Rep. 32 (2005) 47-53
    • (2005) Mol. Biol. Rep. , vol.32 , pp. 47-53
    • Wang, L.1    Jil, C.2    Xu, Y.3    Xu, J.4    Dai, J.5    Wu, Q.6    Wu, M.7    Zou, X.8    Sun, L.9    Gu, S.10    Xie, Y.11    Mao, Y.12
  • 4
    • 0034103006 scopus 로고    scopus 로고
    • Physiological importance of quinoenzymes and the O-quinone family of cofactors
    • Stites T.E., Mitchell A.E., and Rucker R.B. Physiological importance of quinoenzymes and the O-quinone family of cofactors. J. Nutr. 130 (2000) 719-727
    • (2000) J. Nutr. , vol.130 , pp. 719-727
    • Stites, T.E.1    Mitchell, A.E.2    Rucker, R.B.3
  • 5
    • 0031819256 scopus 로고    scopus 로고
    • Newly discovered redox cofactors: possible nutritional, medical, and pharmacological relevance to higher animals
    • McIntire W.S. Newly discovered redox cofactors: possible nutritional, medical, and pharmacological relevance to higher animals. Annu. Rev. Nutr. 18 (1998) 145-177
    • (1998) Annu. Rev. Nutr. , vol.18 , pp. 145-177
    • McIntire, W.S.1
  • 6
    • 0035212690 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes
    • Anthony C. Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes. Antioxid. Redox Signal. 3 (2001) 757-774
    • (2001) Antioxid. Redox Signal. , vol.3 , pp. 757-774
    • Anthony, C.1
  • 7
    • 3042691747 scopus 로고    scopus 로고
    • The quinoprotein dehydrogenases for methanol and glucose
    • Anthony C. The quinoprotein dehydrogenases for methanol and glucose. Arch. Biochem. Biophys. 428 (2004) 2-9
    • (2004) Arch. Biochem. Biophys. , vol.428 , pp. 2-9
    • Anthony, C.1
  • 8
    • 84984754093 scopus 로고    scopus 로고
    • Biochemistry: role of PQQ as a mammalian enzyme cofactor?
    • Felton L.M., and Anthony C. Biochemistry: role of PQQ as a mammalian enzyme cofactor?. Nature 433 (2005) E10
    • (2005) Nature , vol.433
    • Felton, L.M.1    Anthony, C.2
  • 10
    • 0028246229 scopus 로고
    • Dietary pyrroloquinoline quinone: growth and immune response in BALB/c mice
    • Steinberg F.M., Gershwin E., and Rucker R.B. Dietary pyrroloquinoline quinone: growth and immune response in BALB/c mice. J. Nutr. 124 (1994) 744-753
    • (1994) J. Nutr. , vol.124 , pp. 744-753
    • Steinberg, F.M.1    Gershwin, E.2    Rucker, R.B.3
  • 11
    • 0037313822 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone improves growth and reproductive performance in mice fed chemically defined diets
    • Steinberg F., Stites T., Anderson P., Storms D., Chan I., Eghbali S., and Rucker R.B. Pyrroloquinoline quinone improves growth and reproductive performance in mice fed chemically defined diets. Exp. Biol. Med. 228 (2003) 116-160
    • (2003) Exp. Biol. Med. , vol.228 , pp. 116-160
    • Steinberg, F.1    Stites, T.2    Anderson, P.3    Storms, D.4    Chan, I.5    Eghbali, S.6    Rucker, R.B.7
  • 14
    • 0014027007 scopus 로고
    • Metabolism of pipecolic acid in a Pseudomonas species. 3. l-alpha-aminoadipate-delta-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase
    • Calvert A.F., and Rodwell V.W. Metabolism of pipecolic acid in a Pseudomonas species. 3. l-alpha-aminoadipate-delta-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase. J. Biol. Chem. 241 (1966) 409-414
    • (1966) J. Biol. Chem. , vol.241 , pp. 409-414
    • Calvert, A.F.1    Rodwell, V.W.2
  • 15
    • 73049169750 scopus 로고
    • 1-Piperideine-6-carboxylic acid and α-aminoadipic acid-δ-semialdehyde
    • 1-Piperideine-6-carboxylic acid and α-aminoadipic acid-δ-semialdehyde. J. Biol. Chem. 237 (1962) 2239-2245
    • (1962) J. Biol. Chem. , vol.237 , pp. 2239-2245
    • Basso, L.V.1    Rao, D.R.2    Rodwell, V.W.3
  • 16
    • 0034672799 scopus 로고    scopus 로고
    • 14C]pyrroloquinoline quinone (PQQ) in E. coli using genes for PQQ synthesis from K. pneumoniae
    • 14C]pyrroloquinoline quinone (PQQ) in E. coli using genes for PQQ synthesis from K. pneumoniae. Biochim. Biophys. Acta 1524 (2002) 247-252
    • (2002) Biochim. Biophys. Acta , vol.1524 , pp. 247-252
    • Stites, T.E.1    Sih, T.2    Rucker, R.B.3
  • 18
    • 0036676346 scopus 로고    scopus 로고
    • Plasma amino acid concentrations in 36 dogs with histologically confirmed superficial necrolytic dermatitis
    • Outerbridge C.A., Marks S.L., and Rogers Q.R. Plasma amino acid concentrations in 36 dogs with histologically confirmed superficial necrolytic dermatitis. Vet. Dermatol. 13 (2002) 177-186
    • (2002) Vet. Dermatol. , vol.13 , pp. 177-186
    • Outerbridge, C.A.1    Marks, S.L.2    Rogers, Q.R.3
  • 19
    • 0032615941 scopus 로고    scopus 로고
    • Plasma amino acid profiles in cats with naturally acquired chronic renal failure
    • Goldstein R.E., Marks S.L., Cowgill L.D., Kass P.H., and Rogers Q.R. Plasma amino acid profiles in cats with naturally acquired chronic renal failure. Am. J. Vet. Res. 60 (1999) 109-113
    • (1999) Am. J. Vet. Res. , vol.60 , pp. 109-113
    • Goldstein, R.E.1    Marks, S.L.2    Cowgill, L.D.3    Kass, P.H.4    Rogers, Q.R.5
  • 20
    • 0025264451 scopus 로고
    • l-Pipecolic acid metabolism in human liver: l-α-aminoadipate δ-semialdehyde oxidoreductase
    • Chang Y.-F., Ghosh P., and Rao V.V. l-Pipecolic acid metabolism in human liver: l-α-aminoadipate δ-semialdehyde oxidoreductase. Biochim. Biophys. Acta 1038 (1990) 300-305
    • (1990) Biochim. Biophys. Acta , vol.1038 , pp. 300-305
    • Chang, Y.-F.1    Ghosh, P.2    Rao, V.V.3
  • 21
    • 0025262320 scopus 로고
    • l-pipecolic acid metabolism in human liver: detection of l-pipecolate oxidase and identification of its reaction product
    • Rao V.V., and Chang Y.-F. l-pipecolic acid metabolism in human liver: detection of l-pipecolate oxidase and identification of its reaction product. Biochim. Biophys. Acta 1038 (1990) 295-299
    • (1990) Biochim. Biophys. Acta , vol.1038 , pp. 295-299
    • Rao, V.V.1    Chang, Y.-F.2
  • 22
    • 0023188132 scopus 로고
    • Adaptation of the Bradford protein assay to membrane-bound proteins by solubilizing in glucopyranoside detergents
    • Fanger B.O. Adaptation of the Bradford protein assay to membrane-bound proteins by solubilizing in glucopyranoside detergents. Anal. Biochem. 167 (1989) 11-17
    • (1989) Anal. Biochem. , vol.167 , pp. 11-17
    • Fanger, B.O.1
  • 23
    • 0018079559 scopus 로고
    • Rapid purification and properties of potassium-activated aldehyde dehydrogenase from Saccharomyces cerevisiae
    • Bostian K.A., and Betts G.F. Rapid purification and properties of potassium-activated aldehyde dehydrogenase from Saccharomyces cerevisiae. Biochem. J. 173 (1978) 773-786
    • (1978) Biochem. J. , vol.173 , pp. 773-786
    • Bostian, K.A.1    Betts, G.F.2
  • 24
    • 0025909204 scopus 로고
    • Correlations between a nuclear and a mitochondrial mRNA of cytochrome c oxidase subunits, enzymatic activity and total mRNA content, in rat tissues
    • Gagnon J., Kurowski T.T., Wiesner R.J., and Zak R. Correlations between a nuclear and a mitochondrial mRNA of cytochrome c oxidase subunits, enzymatic activity and total mRNA content, in rat tissues. Mol. Cell. Biochem. 107 (1991) 21-29
    • (1991) Mol. Cell. Biochem. , vol.107 , pp. 21-29
    • Gagnon, J.1    Kurowski, T.T.2    Wiesner, R.J.3    Zak, R.4
  • 25
    • 0036435533 scopus 로고    scopus 로고
    • High-throughput measurement of mitochondrial membrane potential in a neural cell line using a fluorescence plate reader
    • Wong A., and Cortopassi G.A. High-throughput measurement of mitochondrial membrane potential in a neural cell line using a fluorescence plate reader. Biochem. Biophys. Res. Commun. 298 (2002) 750-754
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 750-754
    • Wong, A.1    Cortopassi, G.A.2
  • 26
    • 23944516267 scopus 로고    scopus 로고
    • Effect of calcitonin gene-related peptide on gonadotrophin releasing hormone mRNA expression in GT1-7 cells
    • Kinsey-Jones J.S., Li X.F., Bowe J.E., Brain S.D., Lightman S.L., and O'Byrne K.T. Effect of calcitonin gene-related peptide on gonadotrophin releasing hormone mRNA expression in GT1-7 cells. J. Neuroendocrinol. 17 (2005) 541-544
    • (2005) J. Neuroendocrinol. , vol.17 , pp. 541-544
    • Kinsey-Jones, J.S.1    Li, X.F.2    Bowe, J.E.3    Brain, S.D.4    Lightman, S.L.5    O'Byrne, K.T.6
  • 27
    • 0034609681 scopus 로고    scopus 로고
    • Retinal VEGF mRNA measured by SYBR Green I fluorescence: a versatile approach to quantitative PCR
    • Simpson D.A.C., Feeney S., Boyle C., and Stitt A.W. Retinal VEGF mRNA measured by SYBR Green I fluorescence: a versatile approach to quantitative PCR. Mol. Vision 6 (2000) 178-183
    • (2000) Mol. Vision , vol.6 , pp. 178-183
    • Simpson, D.A.C.1    Feeney, S.2    Boyle, C.3    Stitt, A.W.4
  • 29
    • 0032411663 scopus 로고    scopus 로고
    • Mitochondrial lysine uptake limits hepatic lysine oxidation in rats fed diets containing 5, 20 or 60% casein
    • Blemings K.P., Crenshaw T.D., and Benevenga N.J. Mitochondrial lysine uptake limits hepatic lysine oxidation in rats fed diets containing 5, 20 or 60% casein. J. Nutr. 128 (1999) 2427-2434
    • (1999) J. Nutr. , vol.128 , pp. 2427-2434
    • Blemings, K.P.1    Crenshaw, T.D.2    Benevenga, N.J.3
  • 30
    • 0031658297 scopus 로고    scopus 로고
    • Rates of lysine catabolism are inversely related to rates of protein synthesis when measured concurrently in adult female rats induced to grow at different rates
    • Gahl M.J., Benevenga N.J., and Crenshaw T.D. Rates of lysine catabolism are inversely related to rates of protein synthesis when measured concurrently in adult female rats induced to grow at different rates. J. Nutr. 128 (1998) 1503-1511
    • (1998) J. Nutr. , vol.128 , pp. 1503-1511
    • Gahl, M.J.1    Benevenga, N.J.2    Crenshaw, T.D.3
  • 31
    • 0028170488 scopus 로고
    • Lysine-alpha-ketoglutarate reductase and saccharopine dehydrogenase are located only in the mitochondrial matrix in rat liver
    • Blemings K.P., Crenshaw T.D., Swick R.W., and Benevenga N.J. Lysine-alpha-ketoglutarate reductase and saccharopine dehydrogenase are located only in the mitochondrial matrix in rat liver. J. Nutr. 124 (1994) 1215-1221
    • (1994) J. Nutr. , vol.124 , pp. 1215-1221
    • Blemings, K.P.1    Crenshaw, T.D.2    Swick, R.W.3    Benevenga, N.J.4
  • 32
    • 0021115333 scopus 로고
    • Purification, characterization and identification of rat liver mitochondrial kynurenine aminotransferase with alpha-aminoadipate aminotransferase
    • Takeuchi F., Otsuka H., and Shibata Y. Purification, characterization and identification of rat liver mitochondrial kynurenine aminotransferase with alpha-aminoadipate aminotransferase. Biochim. Biophys. Acta 743 (1983) 323-330
    • (1983) Biochim. Biophys. Acta , vol.743 , pp. 323-330
    • Takeuchi, F.1    Otsuka, H.2    Shibata, Y.3
  • 33
    • 0346100521 scopus 로고    scopus 로고
    • Recent advances in the analysis of oxidized proteins
    • Requena J.R., Levine R.L., and Stadtman E.R. Recent advances in the analysis of oxidized proteins. Amino Acids 25 (2003) 221-226
    • (2003) Amino Acids , vol.25 , pp. 221-226
    • Requena, J.R.1    Levine, R.L.2    Stadtman, E.R.3
  • 34
    • 0026643352 scopus 로고
    • The enzymatic and non-enzymatic crosslinking of collagen and elastin
    • Reiser K., McCormick R.J., and Rucker R.B. The enzymatic and non-enzymatic crosslinking of collagen and elastin. FASEB J. 6 (1992) 2439-2449
    • (1992) FASEB J. , vol.6 , pp. 2439-2449
    • Reiser, K.1    McCormick, R.J.2    Rucker, R.B.3
  • 35
    • 0026101107 scopus 로고
    • Species variation in organellar location and activity of l-pipecolic acid oxidation in mammals
    • Mihalik S.J., and Rhead W.J. Species variation in organellar location and activity of l-pipecolic acid oxidation in mammals. J. Comp. Physiol., B 160 (1991) 671-676
    • (1991) J. Comp. Physiol., B , vol.160 , pp. 671-676
    • Mihalik, S.J.1    Rhead, W.J.2
  • 36
    • 0020443011 scopus 로고
    • Comparative rates of metabolism of pipecolic acid in several animal species
    • Dancis J., and Hutzler J. Comparative rates of metabolism of pipecolic acid in several animal species. Comp. Biochem. Physiol., B 73 (1982) 1011-1012
    • (1982) Comp. Biochem. Physiol., B , vol.73 , pp. 1011-1012
    • Dancis, J.1    Hutzler, J.2
  • 37
    • 0019990190 scopus 로고
    • Accumulation, elimination, release and metabolism of pipecolic acid in the mouse brain following intraventricular injection
    • Nishio H., Giacobini E., and Ortiz J. Accumulation, elimination, release and metabolism of pipecolic acid in the mouse brain following intraventricular injection. Neurochem. Res. 7 (1982) 373-385
    • (1982) Neurochem. Res. , vol.7 , pp. 373-385
    • Nishio, H.1    Giacobini, E.2    Ortiz, J.3
  • 38
    • 0024326912 scopus 로고
    • Butyrobetaine availability in liver is a regulatory factor for carnitine biosynthesis in rat: flux through butyrobetaine hydroxylase in the fasting state
    • Sandor A., and Hoppel C.L. Butyrobetaine availability in liver is a regulatory factor for carnitine biosynthesis in rat: flux through butyrobetaine hydroxylase in the fasting state. Eur. J. Biochem. 185 (1989) 671-675
    • (1989) Eur. J. Biochem. , vol.185 , pp. 671-675
    • Sandor, A.1    Hoppel, C.L.2
  • 39
    • 0033993778 scopus 로고    scopus 로고
    • Improved cholecalciferol nutrition in rats is noncalcemic, suppresses parathyroid hormone and increases responsiveness to 1,25-dihydroxycholecalciferol
    • Vieth R., Milojevic S., and Peltekova V. Improved cholecalciferol nutrition in rats is noncalcemic, suppresses parathyroid hormone and increases responsiveness to 1,25-dihydroxycholecalciferol. J. Nutr. 130 (2000) 578-584
    • (2000) J. Nutr. , vol.130 , pp. 578-584
    • Vieth, R.1    Milojevic, S.2    Peltekova, V.3
  • 40
    • 0034570245 scopus 로고    scopus 로고
    • Peroxisomal and mitochondrial targeting of serine:pyruvate/alanine:glyoxylate aminotransferase in rat liver
    • Oda T., Mizuno T., Ito K., Funai T., Ichiyama A., and Miura S. Peroxisomal and mitochondrial targeting of serine:pyruvate/alanine:glyoxylate aminotransferase in rat liver. Cell Biochem. Biophys. 32 (2000) 277-281
    • (2000) Cell Biochem. Biophys. , vol.32 , pp. 277-281
    • Oda, T.1    Mizuno, T.2    Ito, K.3    Funai, T.4    Ichiyama, A.5    Miura, S.6
  • 41
    • 0033523088 scopus 로고    scopus 로고
    • Flux of the l-serine metabolism in rabbit, human, and dog livers
    • Xue H., Sakaguchi T., Fujie M., Ogawa H., and Ichiyama A. Flux of the l-serine metabolism in rabbit, human, and dog livers. J. Biol. Chem. 274 (1999) 16028-16033
    • (1999) J. Biol. Chem. , vol.274 , pp. 16028-16033
    • Xue, H.1    Sakaguchi, T.2    Fujie, M.3    Ogawa, H.4    Ichiyama, A.5
  • 43
    • 0036402941 scopus 로고    scopus 로고
    • Regulation of enzymes of the urea cycle and arginine metabolism
    • Morris M.M. Regulation of enzymes of the urea cycle and arginine metabolism. Annu. Rev. Nutr. 22 (2002) 87-105
    • (2002) Annu. Rev. Nutr. , vol.22 , pp. 87-105
    • Morris, M.M.1


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