메뉴 건너뛰기




Volumn 287, Issue 51, 2012, Pages 42921-42935

A refined analysis of superoxide production by mitochondrial sn-glycerol 3-phosphate dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSOLIC; ELECTRON FLOW; ELECTRON TRANSPORT CHAIN; INNER MEMBRANES; MITOCHONDRIAL ELECTRON TRANSPORT CHAIN; REDUCTION STATE; REFINED ANALYSIS; SKELETAL MUSCLE; SUPEROXIDE GENERATION; SUPEROXIDE PRODUCTION; SUPEROXIDES; TISSUE SOURCES; UBIQUINONE;

EID: 84871139444     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.397828     Document Type: Article
Times cited : (138)

References (62)
  • 1
    • 0014764841 scopus 로고
    • Localization of the glycerol-phosphate dehydrogenase in the outer phase of the mitochondrial inner membrane
    • Klingenberg, M. (1970) Localization of the glycerol-phosphate dehydrogenase in the outer phase of the mitochondrial inner membrane. Eur. J. Biochem. 13, 247-252
    • (1970) Eur. J. Biochem. , vol.13 , pp. 247-252
    • Klingenberg, M.1
  • 2
    • 0019888328 scopus 로고
    • High content of mitochondrial glycerol-3-phosphate dehydrogenase in pancreatic islets and its inhibition by diazoxide
    • MacDonald, M. J. (1981) High content of mitochondrial glycerol-3-phosphate dehydrogenase in pancreatic islets and its inhibition by diazoxide. J. Biol. Chem. 256, 8287-8290
    • (1981) J. Biol. Chem. , vol.256 , pp. 8287-8290
    • MacDonald, M.J.1
  • 3
    • 0030471636 scopus 로고    scopus 로고
    • Sequence and tissue-dependent RNA expression of mouse FAD-linked glycerol-3-phosphate dehydrogenase
    • DOI 10.1006/abbi.1996.0536
    • Koza, R. A., Kozak, U. C., Brown, L. J., Leiter, E. H., MacDonald, M. J., and Kozak, L. P. (1996) Sequence- and tissue-dependent RNA expression of mouse FAD-linked glycerol-3-phosphate dehydrogenase. Arch. Biochem. Biophys. 336, 97-104 (Pubitemid 26423754)
    • (1996) Archives of Biochemistry and Biophysics , vol.336 , Issue.1 , pp. 97-104
    • Koza, R.A.1    Kozak, U.C.2    Brown, L.J.3    Leiter, E.H.4    MacDonald, M.J.5    Kozak, L.P.6
  • 4
    • 0030044236 scopus 로고    scopus 로고
    • Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied
    • DOI 10.1006/abbi.1996.0049
    • MacDonald, M. J., and Brown, L. J. (1996) Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied. Arch. Biochem. Biophys. 326, 79-84 (Pubitemid 26064579)
    • (1996) Archives of Biochemistry and Biophysics , vol.326 , Issue.1 , pp. 79-84
    • MacDonald, M.J.1    Brown, L.J.2
  • 5
    • 0014803307 scopus 로고
    • Thyroid hormone regulation of mitochondrial α-glycerophosphate dehydrogenase in liver and hepatoma
    • Hunt, S. M., Osnos, M., and Rivlin, R. S. (1970) Thyroid hormone regulation of mitochondrial α-glycerophosphate dehydrogenase in liver and hepatoma. Cancer Res. 30, 1764-1768
    • (1970) Cancer Res. , vol.30 , pp. 1764-1768
    • Hunt, S.M.1    Osnos, M.2    Rivlin, R.S.3
  • 6
    • 0029821947 scopus 로고    scopus 로고
    • Regulation of adenine nucleotide translocase and glycerol 3-phosphate dehydrogenase expression by thyroid hormones in different rat tissues
    • Dümmler, K., Müller, S., and Seitz, H. J. (1996) Regulation of adenine nucleotide translocase and glycerol 3-phosphate dehydrogenase expression by thyroid hormones in different rat tissues. Biochem. J. 317, 913-918 (Pubitemid 26308270)
    • (1996) Biochemical Journal , vol.317 , Issue.3 , pp. 913-918
    • Dummler, K.1    Muller, S.2    Seitz, H.J.3
  • 7
    • 0034836498 scopus 로고    scopus 로고
    • Hormonal regulation of multiple promoters of the rat mitochondrial glycerol-3-phosphate dehydrogenase gene: Identification of a complex hormone-response element in the ubiquitous promoter B
    • DOI 10.1046/j.1432-1327.2001.02332.x
    • Weitzel, J. M., Kutz, S., Radtke, C., Grott, S., and Seitz, H. J. (2001) Hormonal regulation of multiple promoters of the rat mitochondrial glycerol-3-phosphate dehydrogenase gene. Identification of a complex hormoneresponse element in the ubiquitous promoter B. Eur. J. Biochem. 268, 4095-4103 (Pubitemid 32868623)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.14 , pp. 4095-4103
    • Weitzel, J.M.1    Kutz, S.2    Radtke, C.3    Grott, S.4    Seitz, H.J.5
  • 8
    • 0035715706 scopus 로고    scopus 로고
    • A sequence variation in the mitochondrial glycerol-3-phosphate dehydrogenase gene is associated with increased plasma glycerol and free fatty acid concentrations among French Canadians
    • DOI 10.1006/mgme.2000.3144
    • St-Pierre, J., Vohl, M. C., Brisson, D., Perron, P., Després, J. P., Hudson, T. J., and Gaudet, D. (2001) A sequence variation in the mitochondrial glycerol-3-phosphate dehydrogenase gene is associated with increased plasma glycerol and free fatty acid concentrations among French Canadians. Mol. Genet. Metab. 72, 209-217 (Pubitemid 34171437)
    • (2001) Molecular Genetics and Metabolism , vol.72 , Issue.3 , pp. 209-217
    • St-Pierre, J.1    Vohl, M.-C.2    Brisson, D.3    Perron, P.4    Despres, J.-P.5    Hudson, T.J.6    Gaudet, D.7
  • 10
    • 0016295886 scopus 로고
    • Studies on respiration and 11 β-hydroxylation of deoxycorticosterone in mitochondria and intact cells isolated from the Snell adrenocortical carcinoma 494
    • Péron, F. G., Haksar, A., Lin, M., Kupfer, D., Robidoux, W., Jr., Kimmel, G., and Bedigian, E. (1974) Studies on respiration and 11 β-hydroxylation of deoxycorticosterone in mitochondria and intact cells isolated from the Snell adrenocortical carcinoma 494. Cancer Res. 34, 2711-2719
    • (1974) Cancer Res. , vol.34 , pp. 2711-2719
    • Péron, F.G.1    Haksar, A.2    Lin, M.3    Kupfer, D.4    Robidoux Jr., W.5    Kimmel, G.6    Bedigian, E.7
  • 11
    • 34748881883 scopus 로고    scopus 로고
    • Increased expression of mitochondrial glycerophosphate dehydrogenase and antioxidant enzymes in prostate cancer cell lines/cancer
    • DOI 10.1080/10715760701579314, PII 782132579
    • Chowdhury, S. K., Raha, S., Tarnopolsky, M. A., and Singh, G. (2007) Increased expression of mitochondrial glycerophosphate dehydrogenase and antioxidant enzymes in prostate cancer cell lines/cancer. Free Radic. Res. 41, 1116-1124 (Pubitemid 47470849)
    • (2007) Free Radical Research , vol.41 , Issue.10 , pp. 1116-1124
    • Roy, C.S.K.1    Raha, S.2    Tarnopolsky, M.A.3    Singh, G.4
  • 12
    • 0025202143 scopus 로고
    • High activity of mitochondrial glycerol phosphate dehydrogenase in insulinomas and carcinoid and other tumors of the amine precursor uptake decarboxylation system
    • MacDonald, M. J., Warner, T. F., and Mertz, R. J. (1990) High activity of mitochondrial glycerol phosphate dehydrogenase in insulinomas and carcinoid and other tumors of the amine precursor uptake decarboxylation system. Cancer Res. 50, 7203-7205
    • (1990) Cancer Res. , vol.50 , pp. 7203-7205
    • MacDonald, M.J.1    Warner, T.F.2    Mertz, R.J.3
  • 13
    • 0031584809 scopus 로고    scopus 로고
    • Mutation in the calcium-binding domain of the mitochondrial glycerophosphate dehydrogenase gene in a family of diabetic subjects
    • DOI 10.1006/bbrc.1997.6147
    • Novials, A., Vidal, J., Franco, C., Ribera, F., Sener, A., Malaisse, W. J., and Gomis, R. (1997) Mutation in the calcium-binding domain of the mitochondrial glycerophosphate dehydrogenase gene in a family of diabetic subjects. Biochem. Biophys. Res. Commun. 231, 570-572 (Pubitemid 27217554)
    • (1997) Biochemical and Biophysical Research Communications , vol.231 , Issue.3 , pp. 570-572
    • Novials, A.1    Vidal, J.2    Franco, C.3    Ribera, F.4    Sener, A.5    Malaisse, W.J.6    Gomis, R.7
  • 14
    • 0035663548 scopus 로고    scopus 로고
    • Identification and functional analysis of mutations in FAD-binding domain of mitochondrial glycerophosphate dehydrogenase in Caucasian patients with type 2 diabetes mellitus
    • DOI 10.1385/ENDO:16:1:39
    • Gudayol, M., Vidal, J., Usac, E. F., Morales, A., Fabregat, M. E., Fernández-Checa, J. C., Novials, A., and Gomis, R. (2001) Identification and functional analysis of mutations in FAD-binding domain of mitochondrial glycerophosphate dehydrogenase in caucasian patients with type 2 diabetes mellitus. Endocrine 16, 39-42 (Pubitemid 34017051)
    • (2001) Endocrine , vol.16 , Issue.1 , pp. 39-42
    • Gudayol, M.1    Vidal, J.2    Usac, E.F.3    Morales, A.4    Fabregat, M.E.5    Fernandez-Checa, J.C.6    Novials, A.7    Gomis, R.8
  • 15
    • 0018265597 scopus 로고
    • Isolation and characterization of flavin-linked glycerol-3-phosphate dehydrogenase from rabbit skeletal muscle mitochondria and comparison with the enzyme from rabbit brain
    • Cole, E. S., Lepp, C. A., Holohan, P. D., and Fondy, T. P. (1978) Isolation and characterization of flavin-linked glycerol-3-phosphate dehydrogenase from rabbit skeletal muscle mitochondria and comparison with the enzyme from rabbit brain. J. Biol. Chem. 253, 7952-7959
    • (1978) J. Biol. Chem. , vol.253 , pp. 7952-7959
    • Cole, E.S.1    Lepp, C.A.2    Holohan, P.D.3    Fondy, T.P.4
  • 16
    • 42149117451 scopus 로고    scopus 로고
    • Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism
    • DOI 10.1073/pnas.0712331105
    • Yeh, J. I., Chinte, U., and Du, S. (2008) Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism. Proc. Natl. Acad. Sci. U.S.A. 105, 3280-3285 (Pubitemid 351723544)
    • (2008) Proceedings of the National Academy of Sciences of the United States of America , vol.105 , Issue.9 , pp. 3280-3285
    • Yeh, J.I.1    Chinte, U.2    Du, S.3
  • 17
    • 0019888718 scopus 로고
    • 2+ stimulation of rat liver mitochondrial glycerophosphate dehydrogenase
    • 2+ stimulation of rat liver mitochondrial glycerophosphate dehydrogenase. J. Biol. Chem. 256, 12767-12771
    • (1981) J. Biol. Chem. , vol.256 , pp. 12767-12771
    • Wernette, M.E.1    Ochs, R.S.2    Lardy, H.A.3
  • 18
    • 0028232768 scopus 로고
    • Sequence of rat mitochondrial glycerol-3-phosphate dehydrogenase cDNA. Evidence for EF-hand calcium-binding domains
    • Brown, L. J., MacDonald, M. J., Lehn, D. A., and Moran, S. M. (1994) Sequence of rat mitochondrial glycerol-3-phosphate dehydrogenase cDNA. Evidence for EF-hand calcium-binding domains. J. Biol. Chem. 269, 14363-14366
    • (1994) J. Biol. Chem. , vol.269 , pp. 14363-14366
    • Brown, L.J.1    MacDonald, M.J.2    Lehn, D.A.3    Moran, S.M.4
  • 20
    • 0141526414 scopus 로고    scopus 로고
    • Superoxide and hydrogen peroxide production by Drosophila mitochondria
    • DOI 10.1016/S0891-5849(03)00464-7
    • Miwa, S., St-Pierre, J., Partridge, L., and Brand, M. D. (2003) Superoxide and hydrogen peroxide production by Drosophila mitochondria. Free Radic. Biol. Med. 35, 938-948 (Pubitemid 37211448)
    • (2003) Free Radical Biology and Medicine , vol.35 , Issue.8 , pp. 938-948
    • Miwa, S.1    St-Pierre, J.2    Partridge, L.3    Brand, M.D.4
  • 21
    • 24344508510 scopus 로고    scopus 로고
    • The topology of superoxide production by complex III and glycerol 3-phosphate dehydrogenase in Drosophila mitochondria
    • DOI 10.1016/j.bbabio.2005.08.003, PII S0005272805001921
    • Miwa, S., and Brand, M. D. (2005) The topology of superoxide production by complex III and glycerol 3-phosphate dehydrogenase in Drosophila mitochondria. Biochim. Biophys. Acta 1709, 214-219 (Pubitemid 41254214)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1709 , Issue.3 , pp. 214-219
    • Miwa, S.1    Brand, M.D.2
  • 24
    • 57449106484 scopus 로고    scopus 로고
    • High efficiency of ROS production by glycerophosphate dehydrogenase in mammalian mitochondria
    • Mrácek, T., Pecinová, A., Vrbacký, M., Drahota, Z., and Houstek, J. (2009) High efficiency of ROS production by glycerophosphate dehydrogenase in mammalian mitochondria. Arch. Biochem. Biophys. 481, 30-36
    • (2009) Arch. Biochem. Biophys. , vol.481 , pp. 30-36
    • Mrácek, T.1    Pecinová, A.2    Vrbacký, M.3    Drahota, Z.4    Houstek, J.5
  • 25
    • 77954606816 scopus 로고    scopus 로고
    • Uncoupling protein 1 decreases superoxide production in brown adipose tissue mitochondria
    • Oelkrug, R., Kutschke, M., Meyer, C. W., Heldmaier, G., and Jastroch, M. (2010) Uncoupling protein 1 decreases superoxide production in brown adipose tissue mitochondria. J. Biol. Chem. 285, 21961-21968
    • (2010) J. Biol. Chem. , vol.285 , pp. 21961-21968
    • Oelkrug, R.1    Kutschke, M.2    Meyer, C.W.3    Heldmaier, G.4    Jastroch, M.5
  • 26
    • 77952541558 scopus 로고    scopus 로고
    • The sites and topology of mitochondrial superoxide production
    • Brand, M. D. (2010) The sites and topology of mitochondrial superoxide production. Exp. Gerontol. 45, 466-472
    • (2010) Exp. Gerontol. , vol.45 , pp. 466-472
    • Brand, M.D.1
  • 27
    • 0019155664 scopus 로고
    • Purification and properties of L-3-glycerophosphate dehydrogenase from pig brain mitochondria
    • Cottingham, I. R., and Ragan, C. I. (1980) Purification and properties of L-3-glycerophosphate dehydrogenase from pig brain mitochondria. Biochem. J. 192, 9-18 (Pubitemid 11207908)
    • (1980) Biochemical Journal , vol.192 , Issue.1 , pp. 9-18
    • Cottingham, I.R.1    Ragan, C.I.2
  • 28
    • 0022979469 scopus 로고
    • Purification and characterization of glycerol-3-phosphate dehydrogenase (flavin-linked) from rat liver mitochondria
    • Garrib, A., and McMurray, W. C. (1986) Purification and characterization of glycerol-3-phosphate dehydrogenase (flavin-linked) from rat liver mitochondria. J. Biol. Chem. 261, 8042-8048 (Pubitemid 17208741)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.17 , pp. 8042-8048
    • Garrib, A.1    McMurray, W.C.2
  • 29
    • 82355183887 scopus 로고    scopus 로고
    • Measurement of proton leak and electron leak in isolated mitochondria
    • Affourtit, C., Quinlan, C. L., and Brand, M. D. (2012) Measurement of proton leak and electron leak in isolated mitochondria. Methods Mol. Biol. 810, 165-182
    • (2012) Methods Mol. Biol. , vol.810 , pp. 165-182
    • Affourtit, C.1    Quinlan, C.L.2    Brand, M.D.3
  • 30
    • 80052710701 scopus 로고    scopus 로고
    • Characteristics of the turnover of uncoupling protein 3 by the ubiquitin proteasome system in isolated mitochondria
    • Mookerjee, S. A., and Brand, M. D. (2011) Characteristics of the turnover of uncoupling protein 3 by the ubiquitin proteasome system in isolated mitochondria. Biochim. Biophys. Acta 1807, 1474-1481
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 1474-1481
    • Mookerjee, S.A.1    Brand, M.D.2
  • 33
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • DOI 10.1074/jbc.M207217200
    • St-Pierre, J., Buckingham, J. A., Roebuck, S. J., and Brand, M. D. (2002) Topology of superoxide production from different sites in the mitochondrial electron transport chain. J. Biol. Chem. 277, 44784-44790 (Pubitemid 36159072)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.47 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 34
    • 80052419584 scopus 로고    scopus 로고
    • The mechanism of superoxide production by the antimycin-inhibited mitochondrial Q-cycle
    • Quinlan, C. L., Gerencser, A. A., Treberg, J. R., and Brand, M. D. (2011) The mechanism of superoxide production by the antimycin-inhibited mitochondrial Q-cycle. J. Biol. Chem. 286, 31361-31372
    • (2011) J. Biol. Chem. , vol.286 , pp. 31361-31372
    • Quinlan, C.L.1    Gerencser, A.A.2    Treberg, J.R.3    Brand, M.D.4
  • 35
    • 77953565915 scopus 로고    scopus 로고
    • Hydrogen peroxide efflux from muscle mitochondria underestimates matrix superoxide production. A correction using glutathione depletion
    • Treberg, J. R., Quinlan, C. L., and Brand, M. D. (2010) Hydrogen peroxide efflux from muscle mitochondria underestimates matrix superoxide production. A correction using glutathione depletion. FEBS J. 277, 2766-2778
    • (2010) FEBS J. , vol.277 , pp. 2766-2778
    • Treberg, J.R.1    Quinlan, C.L.2    Brand, M.D.3
  • 36
    • 79961008706 scopus 로고    scopus 로고
    • Evidence for two sites of superoxide production by mitochondrial NADH-ubiquinone oxidoreductase (complex I)
    • Treberg, J. R., Quinlan, C. L., and Brand, M. D. (2011) Evidence for two sites of superoxide production by mitochondrial NADH-ubiquinone oxidoreductase (complex I). J. Biol. Chem. 286, 27103-27110
    • (2011) J. Biol. Chem. , vol.286 , pp. 27103-27110
    • Treberg, J.R.1    Quinlan, C.L.2    Brand, M.D.3
  • 37
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • DOI 10.1074/jbc.M407715200
    • Muller, F. L., Liu, Y., and Van Remmen, H. (2004) Complex III releases superoxide to both sides of the inner mitochondrial membrane. J. Biol. Chem. 279, 49064-49073 (Pubitemid 39625788)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.47 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    Van Remmen, H.3
  • 38
    • 84867401800 scopus 로고    scopus 로고
    • Native rates of superoxide production from multiple sites in isolated mitochondria measured using endogenous reporters
    • Quinlan, C. L., Treberg, J. R., Perevoshchikova, I. V., Orr, A. L., and Brand, M. D. (2012) Native rates of superoxide production from multiple sites in isolated mitochondria measured using endogenous reporters. Free Radic. Biol. Med. 53, 1807-1817
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 1807-1817
    • Quinlan, C.L.1    Treberg, J.R.2    Perevoshchikova, I.V.3    Orr, A.L.4    Brand, M.D.5
  • 39
    • 0001104662 scopus 로고
    • The role of cytochrome b-566 in the electron-transfer chain of Rhodopseudomonas sphaeroides
    • Meinhardt, S. W., and Crofts, A. R. (1983) The role of cytochrome b-566 in the electron-transfer chain of Rhodopseudomonas sphaeroides. Biochim. Biophys. Acta 723, 219-230
    • (1983) Biochim. Biophys. Acta , vol.723 , pp. 219-230
    • Meinhardt, S.W.1    Crofts, A.R.2
  • 40
    • 0014545728 scopus 로고
    • On the redox potentials of ubiquinone and cytochrome b in the respiratory chain
    • Urban, P. F., and Klingenberg, M. (1969) On the redox potentials of ubiquinone and cytochrome b in the respiratory chain. Eur. J. Biochem. 9, 519-525
    • (1969) Eur. J. Biochem. , vol.9 , pp. 519-525
    • Urban, P.F.1    Klingenberg, M.2
  • 41
    • 43049141441 scopus 로고    scopus 로고
    • Diphenyleneiodonium acutely inhibits reactive oxygen species production by mitochondrial complex i during reverse, but not forward electron transport
    • Lambert, A. J., Buckingham, J. A., Boysen, H. M., and Brand, M. D. (2008) Diphenyleneiodonium acutely inhibits reactive oxygen species production by mitochondrial complex I during reverse, but not forward electron transport. Biochim. Biophys. Acta 1777, 397-403
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 397-403
    • Lambert, A.J.1    Buckingham, J.A.2    Boysen, H.M.3    Brand, M.D.4
  • 42
    • 0014443466 scopus 로고
    • Preparation and some properties of L-3-glycerophosphate dehydrogenase from pig brain mitochondria
    • Dawson, A. P., and Thorne, C. J. (1969) Preparation and some properties of L-3-glycerophosphate dehydrogenase from pig brain mitochondria. Biochem. J. 111, 27-34
    • (1969) Biochem. J. , vol.111 , pp. 27-34
    • Dawson, A.P.1    Thorne, C.J.2
  • 43
    • 84864540083 scopus 로고    scopus 로고
    • Mitochondrial complex II can generate reactive oxygen species at high rates in both the forward and reverse reactions
    • Quinlan, C. L., Orr, A. L., Perevoshchikova, I. V., Treberg, J. R., Ackrell, B. A., and Brand, M. D. (2012) Mitochondrial complex II can generate reactive oxygen species at high rates in both the forward and reverse reactions. J. Biol. Chem. 287, 27255-27264
    • (2012) J. Biol. Chem. , vol.287 , pp. 27255-27264
    • Quinlan, C.L.1    Orr, A.L.2    Perevoshchikova, I.V.3    Treberg, J.R.4    Ackrell, B.A.5    Brand, M.D.6
  • 46
    • 0029064257 scopus 로고
    • Superoxide radical and iron modulate aconitase activity in mammalian cells
    • Gardner, P. R., Raineri, I., Epstein, L. B., and White, C. W. (1995) Superoxide radical and iron modulate aconitase activity in mammalian cells. J. Biol. Chem. 270, 13399-13405
    • (1995) J. Biol. Chem. , vol.270 , pp. 13399-13405
    • Gardner, P.R.1    Raineri, I.2    Epstein, L.B.3    White, C.W.4
  • 47
    • 0033847221 scopus 로고    scopus 로고
    • Multiple promoters direct the tissue-specific expression of rat mitochondrial glycerol-3-phosphate dehydrogenase
    • Weitzel, J. M., Grott, S., Radtke, C., Kutz, S., and Seitz, H. J. (2000) Multiple promoters direct the tissue-specific expression of rat mitochondrial glycerol-3-phosphate dehydrogenase. Biol. Chem. 381, 611-614 (Pubitemid 30657883)
    • (2000) Biological Chemistry , vol.381 , Issue.7 , pp. 611-614
    • Weitzel, J.M.1    Grott, S.2    Radtke, C.3    Kutz, S.4    Seitz, H.J.5
  • 48
    • 0037307356 scopus 로고    scopus 로고
    • Testis-specific expression of rat mitochondrial glycerol-3-phosphate dehydrogenase in haploid male germ cells
    • DOI 10.1095/biolreprod.102.008540
    • Weitzel, J. M., Shiryaeva, N. B., Middendorff, R., Balvers, M., Radtke, C., Ivell, R., and Seitz, H. J. (2003) Testis-specific expression of rat mitochondrial glycerol-3-phosphate dehydrogenase in haploid male germ cells. Biol. Reprod. 68, 699-707 (Pubitemid 36139339)
    • (2003) Biology of Reproduction , vol.68 , Issue.2 , pp. 699-707
    • Weitzel, J.M.1    Shiryaeva, N.B.2    Middendorff, R.3    Balvers, M.4    Radtke, C.5    Ivell, R.6    Seitz, H.J.7
  • 49
    • 77955672171 scopus 로고    scopus 로고
    • Oxidation of hydrogen sulfide remains a priority in mammalian cells and causes reverse electron transfer in colonocytes
    • Lagoutte, E., Mimoun, S., Andriamihaja, M., Chaumontet, C., Blachier, F., and Bouillaud, F. (2010) Oxidation of hydrogen sulfide remains a priority in mammalian cells and causes reverse electron transfer in colonocytes. Biochim. Biophys. Acta 1797, 1500-1511
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1500-1511
    • Lagoutte, E.1    Mimoun, S.2    Andriamihaja, M.3    Chaumontet, C.4    Blachier, F.5    Bouillaud, F.6
  • 50
    • 84858195283 scopus 로고    scopus 로고
    • Sulphide quinone reductase contributes to hydrogen sulphide metabolism in murine peripheral tissues but not in the CNS
    • Linden, D. R., Furne, J., Stoltz, G. J., Abdel-Rehim, M. S., Levitt, M. D., and Szurszewski, J. H. (2012) Sulphide quinone reductase contributes to hydrogen sulphide metabolism in murine peripheral tissues but not in the CNS. Br. J. Pharmacol. 165, 2178-2190
    • (2012) Br. J. Pharmacol. , vol.165 , pp. 2178-2190
    • Linden, D.R.1    Furne, J.2    Stoltz, G.J.3    Abdel-Rehim, M.S.4    Levitt, M.D.5    Szurszewski, J.H.6
  • 55
    • 0021324783 scopus 로고
    • Mitochondrial oxidative enzyme activity in individual fibre types in hypo- and hyperthyroid rat skeletal muscles
    • Johnson, M. A., and Turnbull, D. M. (1984) Mitochondrial oxidative enzyme activity in individual fibre types in hypo- and hyperthyroid rat skeletal muscles. Q. J. Exp. Physiol. 69, 257-270 (Pubitemid 14138556)
    • (1984) Quarterly Journal of Experimental Physiology , vol.69 , Issue.2 , pp. 257-270
    • Johnson, M.A.1    Turnbull, D.M.2
  • 56
    • 0029880902 scopus 로고    scopus 로고
    • Characteristics of mitochondria isolated from type i and type IIb skeletal muscle
    • Jackman, M. R., and Willis, W. T. (1996) Characteristics of mitochondria isolated from type I and type IIb skeletal muscle. Am. J. Physiol. 270, C673-C678
    • (1996) Am. J. Physiol. , vol.270
    • Jackman, M.R.1    Willis, W.T.2
  • 57
    • 0015826334 scopus 로고
    • Metabolic changes induced by ethanol in muscle and liver tissue of the rat in vivo
    • Fellenius, E., Björkroth, U., Kiessling, K. H. (1973) Metabolic changes induced by ethanol in muscle and liver tissue of the rat in vivo. Acta Chem. Scand. 27, 2361-2366
    • (1973) Acta Chem. Scand. , vol.27 , pp. 2361-2366
    • Fellenius, E.1    Björkroth, U.2    Kiessling, K.H.3
  • 58
    • 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
  • 59
    • 0033939421 scopus 로고    scopus 로고
    • Calcium ion in skeletal muscle: Its crucial role for muscle function, plasticity, and disease
    • Berchtold, M. W., Brinkmeier, H., and Müntener, M. (2000) Calcium ion in skeletal muscle. Its crucial role for muscle function, plasticity, and disease. Physiol. Rev. 80, 1215-1265 (Pubitemid 30452014)
    • (2000) Physiological Reviews , vol.80 , Issue.3 , pp. 1215-1265
    • Berchtold, M.W.1    Brinkmeier, H.2    Muntener, M.3
  • 60
    • 79952409731 scopus 로고    scopus 로고
    • Calcium dysregulation and homeostasis of neural calcium in the molecular mechanisms of neurodegenerative diseases provide multiple targets for neuroprotection
    • Zündorf, G., and Reiser, G. (2011) Calcium dysregulation and homeostasis of neural calcium in the molecular mechanisms of neurodegenerative diseases provide multiple targets for neuroprotection. Antioxid. Redox Signal. 14, 1275-1288
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 1275-1288
    • Zündorf, G.1    Reiser, G.2
  • 61
    • 0021710580 scopus 로고
    • P-31 nuclear magnetic resonance analysis of brain: II. Effects of oxygen deprivation on isolated perfused and nonperfused rat brain
    • DOI 10.1111/j.1471-4159.1984.tb06100.x
    • Kopp, S. J., Krieglstein, J., Freidank, A., Rachman, A., Seibert, A., and Cohen, M. M. (1984) P-31 nuclear magnetic resonance analysis of brain. II. Effects of oxygen deprivation on isolated perfused and nonperfused rat brain. J. Neurochem. 43, 1716-1731 (Pubitemid 15212091)
    • (1984) Journal of Neurochemistry , vol.43 , Issue.6 , pp. 1716-1731
    • Kopp, S.J.1    Krieglstein, J.2    Freidank, A.3
  • 62
    • 34249814001 scopus 로고    scopus 로고
    • Formation of glycerol from glucose in rat brain and cultured brain cells. Augmentation with kainate or ischemia
    • DOI 10.1111/j.1471-4159.2006.04433.x
    • Nguyen, N. H., Gonzalez, S. V., and Hassel, B. (2007) Formation of glycerol from glucose in rat brain and cultured brain cells. Augmentation with kainate or ischemia. J. Neurochem. 101, 1694-1700 (Pubitemid 46848840)
    • (2007) Journal of Neurochemistry , vol.101 , Issue.6 , pp. 1694-1700
    • Nguyen, N.H.T.1    Gonzalez, S.V.2    Hassel, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.