메뉴 건너뛰기




Volumn 25, Issue 5-6, 2004, Pages 455-473

Carnitine: A nutritional, biosynthetic, and functional perspective

Author keywords

Biosynthesis; Carnitine; Carnitine palmitoyltransferase; Dietary; Malonyl CoA

Indexed keywords

ANION CHANNEL; CARNITINE; CARNITINE PALMITOYLTRANSFERASE; FATTY ACID; MALONYL COENZYME A;

EID: 4444315751     PISSN: 00982997     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mam.2004.06.006     Document Type: Article
Times cited : (354)

References (99)
  • 1
    • 0035970805 scopus 로고    scopus 로고
    • Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-CoA carboxylase 2
    • Abu-Elheiga L., Matzuk M.M., Abo_Hashema K., Wakil S.J. Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-CoA carboxylase 2. Science. 291:2001;2613-2616
    • (2001) Science , vol.291 , pp. 2613-2616
    • Abu-Elheiga, L.1    Matzuk, M.M.2    Abo Hashema, K.3    Wakil, S.J.4
  • 2
    • 0025302385 scopus 로고
    • Role of the liver in carnitine metabolism: The mechanism of development of carnitine-deficient status in guinea pigs
    • Alkonyi I., Cseko J., Sandor A. Role of the liver in carnitine metabolism: the mechanism of development of carnitine-deficient status in guinea pigs. J. Clin. Chem. Clin. Biochem. 28(5):1990;319-321
    • (1990) J. Clin. Chem. Clin. Biochem. , vol.28 , Issue.5 , pp. 319-321
    • Alkonyi, I.1    Cseko, J.2    Sandor, A.3
  • 3
    • 0033202059 scopus 로고    scopus 로고
    • Serum free carnitine levels in children with kwashiorkor
    • Aseo I., Tindimwebwa G., Agu E., Iputo J.E. Serum free carnitine levels in children with kwashiorkor. East Afr. Med. J. 76:1999;562-565
    • (1999) East Afr. Med. J. , vol.76 , pp. 562-565
    • Aseo, I.1    Tindimwebwa, G.2    Agu, E.3    Iputo, J.E.4
  • 4
    • 0842287450 scopus 로고    scopus 로고
    • Mitochondrial β-oxidation
    • Bartlett K., Eaton S. Mitochondrial β-oxidation. Eur. J. Biochem. 271:2004;462-469
    • (2004) Eur. J. Biochem. , vol.271 , pp. 462-469
    • Bartlett, K.1    Eaton, S.2
  • 5
    • 0024284216 scopus 로고
    • Inhibition of adenine nucleotide transport through the mitochondrial porin by a synthetic polyanion
    • Benz R., Wojtczak L., Bosch W., Brdiczka D. Inhibition of adenine nucleotide transport through the mitochondrial porin by a synthetic polyanion. FEBS Lett. 231:1988;75-80
    • (1988) FEBS Lett. , vol.231 , pp. 75-80
    • Benz, R.1    Wojtczak, L.2    Bosch, W.3    Brdiczka, D.4
  • 7
    • 0020371958 scopus 로고
    • Possible functions of short-chain and medium-chain carnitine acyltransferases
    • Bieber L.L., Emaus R., Valkner K., Farrell S. Possible functions of short-chain and medium-chain carnitine acyltransferases. Fed. Proc. 41:1982;2858-2862
    • (1982) Fed. Proc. , vol.41 , pp. 2858-2862
    • Bieber, L.L.1    Emaus, R.2    Valkner, K.3    Farrell, S.4
  • 8
    • 0025903652 scopus 로고
    • Inadequate iron availability as a possible cause of low serum carnitine concentrations in patients with phenylketonuria
    • Bohles H., Ullrich K., Endres W., Behbehani A.W., Wendel U. Inadequate iron availability as a possible cause of low serum carnitine concentrations in patients with phenylketonuria. Eur. J. Pediatr. 150:1991;425-428
    • (1991) Eur. J. Pediatr. , vol.150 , pp. 425-428
    • Bohles, H.1    Ullrich, K.2    Endres, W.3    Behbehani, A.W.4    Wendel, U.5
  • 9
    • 0022382089 scopus 로고
    • Hepatic mitochondrial inner membrane properties and carnitine palmitoyltransferase a and B
    • Brady L.J., Silverstein L.J., Hoppel C.L., Brady P.S. Hepatic mitochondrial inner membrane properties and carnitine palmitoyltransferase A and B. Biochem. J. 232:1985;445-450
    • (1985) Biochem. J. , vol.232 , pp. 445-450
    • Brady, L.J.1    Silverstein, L.J.2    Hoppel, C.L.3    Brady, P.S.4
  • 10
    • 0029035063 scopus 로고
    • Pharmacokinetic considerations for the therapeutic use of carnitine in hemodialysis patients
    • Brass E.P. Pharmacokinetic considerations for the therapeutic use of carnitine in hemodialysis patients. Clin. Ther. 17:1995;176-185
    • (1995) Clin. Ther. , vol.17 , pp. 176-185
    • Brass, E.P.1
  • 11
    • 0037385524 scopus 로고    scopus 로고
    • Impact on carnitine homeostasis of short-term treatment with the pivalate prodrug cefditoren pivoxil
    • Brass E.P., Mayer M.D., Mulford D.J., Stickler T.K., Hoppel C.L. Impact on carnitine homeostasis of short-term treatment with the pivalate prodrug cefditoren pivoxil. Clin. Pharmacol. Ther. 73:2003;338-347
    • (2003) Clin. Pharmacol. Ther. , vol.73 , pp. 338-347
    • Brass, E.P.1    Mayer, M.D.2    Mulford, D.J.3    Stickler, T.K.4    Hoppel, C.L.5
  • 12
    • 0019798351 scopus 로고
    • The effect of fasting on the activity of liver carnitine palmitoyltransferase and its inhibition by malonyl-CoA
    • Bremer J. The effect of fasting on the activity of liver carnitine palmitoyltransferase and its inhibition by malonyl-CoA. Biochim. Biophys. Acta. 665:1981;628-631
    • (1981) Biochim. Biophys. Acta , vol.665 , pp. 628-631
    • Bremer, J.1
  • 13
    • 0021024932 scopus 로고
    • Carnitine-metabolism and function
    • Bremer J. Carnitine-metabolism and function. Physiol. Rev. 63:1983;1420-1480
    • (1983) Physiol. Rev. , vol.63 , pp. 1420-1480
    • Bremer, J.1
  • 14
    • 0023270488 scopus 로고
    • Effect of diet on plasma carnitine levels and urinary carnitine excretion in humans
    • Cederblad G. Effect of diet on plasma carnitine levels and urinary carnitine excretion in humans. Am. J. Clin. Nutr. 45:1987;725-729
    • (1987) Am. J. Clin. Nutr. , vol.45 , pp. 725-729
    • Cederblad, G.1
  • 15
    • 0015305639 scopus 로고
    • A method for the determination of carnitine in the picomole range
    • Cederblad G., Lindstedt S. A method for the determination of carnitine in the picomole range. Clin. Chim. Acta. 37:1972;235-243
    • (1972) Clin. Chim. Acta , vol.37 , pp. 235-243
    • Cederblad, G.1    Lindstedt, S.2
  • 16
    • 0021710439 scopus 로고
    • Urinary excretion of L-carnitine and acylcarnitines by patients with disorders of organic acid metabolism: Evidence for secondary insufficiency of L-carnitine
    • Chalmers R.A., Roe C.R., Stacey T.E., Hoppel C.L. Urinary excretion of L-carnitine and acylcarnitines by patients with disorders of organic acid metabolism: evidence for secondary insufficiency of L-carnitine. Pediatr. Res. 18:1984;1325-1328
    • (1984) Pediatr. Res. , vol.18 , pp. 1325-1328
    • Chalmers, R.A.1    Roe, C.R.2    Stacey, T.E.3    Hoppel, C.L.4
  • 17
    • 0031933339 scopus 로고    scopus 로고
    • Urinary, plasma, and erythrocyte carnitine concentrations during transition to a lactoovovegetarian diet with vitamin B-6 depletion and repletion in young adult women
    • Chen W., Huang Y.C., Shultz T.D., Mitchell M.E. Urinary, plasma, and erythrocyte carnitine concentrations during transition to a lactoovovegetarian diet with vitamin B-6 depletion and repletion in young adult women. Am. J. Clin. Nutr. 67:1998;221-230
    • (1998) Am. J. Clin. Nutr. , vol.67 , pp. 221-230
    • Chen, W.1    Huang, Y.C.2    Shultz, T.D.3    Mitchell, M.E.4
  • 18
    • 0025272599 scopus 로고
    • In vivo evidence for a vitamin B-6 requirement in carnitine synthesis
    • Cho Y.O., Leklem J.E. In vivo evidence for a vitamin B-6 requirement in carnitine synthesis. J. Nutr. 120:1990;258-265
    • (1990) J. Nutr. , vol.120 , pp. 258-265
    • Cho, Y.O.1    Leklem, J.E.2
  • 19
    • 0023513271 scopus 로고
    • The mitochondrial outer membrane channel, VDAC, is regulated by a synthetic polyanion
    • Colombini M., Yeung C.L., Tung J., Konig T. The mitochondrial outer membrane channel, VDAC, is regulated by a synthetic polyanion. Biochim. Biophys. Acta. 905:1987;279-286
    • (1987) Biochim. Biophys. Acta , vol.905 , pp. 279-286
    • Colombini, M.1    Yeung, C.L.2    Tung, J.3    Konig, T.4
  • 20
    • 0021758541 scopus 로고
    • Determination of free trimethyllysine in plasma and tissue speciemans by high-performance liquid chromotography
    • Davis A.T., Ingalls S.T., Hoppel C.L. Determination of free trimethyllysine in plasma and tissue speciemans by high-performance liquid chromotography. J. Chromatogr. 306:1984;79-87
    • (1984) J. Chromatogr. , vol.306 , pp. 79-87
    • Davis, A.T.1    Ingalls, S.T.2    Hoppel, C.L.3
  • 21
    • 0030965952 scopus 로고    scopus 로고
    • Functional characterization of mitochondrial carnitine palmitoyltransferase I and II expressed in the yeast Pichia pastoris
    • de Vries Y., Arvidson D.N., Waterham H.R., Cregg J.M., Woldegiorgis G. Functional characterization of mitochondrial carnitine palmitoyltransferase I and II expressed in the yeast Pichia pastoris. Biochemistry. 36:1997;5285-5292
    • (1997) Biochemistry , vol.36 , pp. 5285-5292
    • De Vries, Y.1    Arvidson, D.N.2    Waterham, H.R.3    Cregg, J.M.4    Woldegiorgis, G.5
  • 23
    • 0029803625 scopus 로고    scopus 로고
    • The effect of respiratory chain impairment of beta-oxidation in rat heart mitochondria
    • Eaton S., Purfarzam M., Bartlett K. The effect of respiratory chain impairment of beta-oxidation in rat heart mitochondria. Biochem. J. 319:1996;633-640
    • (1996) Biochem. J. , vol.319 , pp. 633-640
    • Eaton, S.1    Purfarzam, M.2    Bartlett, K.3
  • 24
    • 0029902428 scopus 로고    scopus 로고
    • Mammalian mitochondrial beta-oxidation
    • Eaton S., Bartlett K., Pourfarzam M. Mammalian mitochondrial beta-oxidation. Biochem. J. 320:1996;345-357
    • (1996) Biochem. J. , vol.320 , pp. 345-357
    • Eaton, S.1    Bartlett, K.2    Pourfarzam, M.3
  • 26
    • 0014773753 scopus 로고
    • Caarnitine and acetylcarnitine in the milk of normal and ketotic cows
    • Erfle J.D., Fisher L.J., Sauer F. Caarnitine and acetylcarnitine in the milk of normal and ketotic cows. J. Dairy Sci. 53:1970;486-489
    • (1970) J. Dairy Sci. , vol.53 , pp. 486-489
    • Erfle, J.D.1    Fisher, L.J.2    Sauer, F.3
  • 27
    • 0041806644 scopus 로고    scopus 로고
    • Quantification of non-protein nitrogen components of infant formulae and follow-up milks: Comparison with cows' and human milk
    • Ferreira I.M. Quantification of non-protein nitrogen components of infant formulae and follow-up milks: comparison with cows' and human milk. Br. J. Nutr. 90:2003;127-133
    • (2003) Br. J. Nutr. , vol.90 , pp. 127-133
    • Ferreira, I.M.1
  • 28
    • 0031449295 scopus 로고    scopus 로고
    • Enzymic flow injection determination of free L-carnitine in infant formulae
    • Ferreira I.M., Macedo M.N., Ferreira M.A. Enzymic flow injection determination of free L-carnitine in infant formulae. Analyst. 122:1997;1539-1541
    • (1997) Analyst , vol.122 , pp. 1539-1541
    • Ferreira, I.M.1    MacEdo, M.N.2    Ferreira, M.A.3
  • 29
    • 0033032120 scopus 로고    scopus 로고
    • Submitochondrial and subcellular distributions of the carnitine-acylcarnitine carrier
    • Fraser F., Zammit V.A. Submitochondrial and subcellular distributions of the carnitine-acylcarnitine carrier. FEBS Lett. 445:1999;41-44
    • (1999) FEBS Lett. , vol.445 , pp. 41-44
    • Fraser, F.1    Zammit, V.A.2
  • 30
    • 0031006933 scopus 로고    scopus 로고
    • Topology of carnitine palmitoyltransferase I in the mitochondrial outer membrane
    • Fraser F., Corstorphine C.G., Zammit V.A. Topology of carnitine palmitoyltransferase I in the mitochondrial outer membrane. Biochem. J. 323:1997;711-718
    • (1997) Biochem. J. , vol.323 , pp. 711-718
    • Fraser, F.1    Corstorphine, C.G.2    Zammit, V.A.3
  • 31
    • 0026707744 scopus 로고
    • Activity of carnitine palmitoyltransferase in mitochondrial outer membranes and peroxisomes in digitonin-permeabilized hepatocytes. Selective modulation of mitochondrial enzyme activity by okadaic acid
    • Guzman M., Geelen M.J.H. Activity of carnitine palmitoyltransferase in mitochondrial outer membranes and peroxisomes in digitonin-permeabilized hepatocytes. Selective modulation of mitochondrial enzyme activity by okadaic acid. Biochem. J. 287:1992;487-492
    • (1992) Biochem. J. , vol.287 , pp. 487-492
    • Guzman, M.1    Geelen, M.J.H.2
  • 32
    • 0028333843 scopus 로고
    • Evidence against direct involvement of phosphorylation in the activation of carnitine palmitoyltransferase by okadaic acid in rat hepatocytes
    • Guzman M., Kolodziej M.P., Caldwell A., Corstorphine C.G., Zammit V.A. Evidence against direct involvement of phosphorylation in the activation of carnitine palmitoyltransferase by okadaic acid in rat hepatocytes. Biochem. J. 300:1994;693-699
    • (1994) Biochem. J. , vol.300 , pp. 693-699
    • Guzman, M.1    Kolodziej, M.P.2    Caldwell, A.3    Corstorphine, C.G.4    Zammit, V.A.5
  • 33
    • 0023756726 scopus 로고
    • Pharmacokinetics of intravenous and oral bolus doses of L-carnitine in healthy subjects
    • Harper P., Elwin C.E., Cederblad G. Pharmacokinetics of intravenous and oral bolus doses of L-carnitine in healthy subjects. Eur. J. Clin. Pharmacol. 35:1988;555-562
    • (1988) Eur. J. Clin. Pharmacol. , vol.35 , pp. 555-562
    • Harper, P.1    Elwin, C.E.2    Cederblad, G.3
  • 36
    • 0037623016 scopus 로고
    • Carnitine palmitoyltransferase and transport of fatty acids
    • Martonosi A. New York: Plenum
    • Hoppel C.L. Carnitine palmitoyltransferase and transport of fatty acids. Martonosi A. The Enzymes of Biological Membranes. vol. 2:1976;119-143 Plenum, New York
    • (1976) The Enzymes of Biological Membranes , vol.2 , pp. 119-143
    • Hoppel, C.L.1
  • 37
    • 0020363079 scopus 로고
    • Carnitine and carnitine palmitoyltransferase in fatty acid oxidation and ketosis
    • Hoppel C.L. Carnitine and carnitine palmitoyltransferase in fatty acid oxidation and ketosis. Fed. Proc. 41:1982;2853-2857
    • (1982) Fed. Proc. , vol.41 , pp. 2853-2857
    • Hoppel, C.L.1
  • 38
    • 0019015876 scopus 로고
    • Carnitine metabolism in normal-weight and obese human subjects during fasting
    • Hoppel C.L., Genuth S.M. Carnitine metabolism in normal-weight and obese human subjects during fasting. Am. J. Physiol. 238:1980;E409-E415
    • (1980) Am. J. Physiol. , vol.238
    • Hoppel, C.L.1    Genuth, S.M.2
  • 39
    • 4444247937 scopus 로고    scopus 로고
    • Phosphorylation of rat liver carnitine palmitoyltransferase-I
    • Hoppel C., Kerner J., Distler A., Minkler P. Phosphorylation of rat liver carnitine palmitoyltransferase-I. FASEB J. 18:2004;A862
    • (2004) FASEB J. , vol.18 , pp. 862
    • Hoppel, C.1    Kerner, J.2    Distler, A.3    Minkler, P.4
  • 40
    • 0036498771 scopus 로고    scopus 로고
    • Isolation of hepatic mitochondrial contact sites: Previously unrecognized inner membrane components
    • Hoppel C., Kerner J., Turkaly P., Minkler P., Tandler B. Isolation of hepatic mitochondrial contact sites: previously unrecognized inner membrane components. Anal. Biochem. 302:2002;60-69
    • (2002) Anal. Biochem. , vol.302 , pp. 60-69
    • Hoppel, C.1    Kerner, J.2    Turkaly, P.3    Minkler, P.4    Tandler, B.5
  • 41
    • 0017891065 scopus 로고
    • Carnitine biosynthesis, β-Hydroxylation of trimethyllysine by an α-ketoglutarate-dependent mitochondrial dioxygenase
    • Hulse J.D., Ellis S.R., Henderson L.M. Carnitine biosynthesis, β-Hydroxylation of trimethyllysine by an α-ketoglutarate-dependent mitochondrial dioxygenase. J. Biol. Chem. 253:1978;1654-1659
    • (1978) J. Biol. Chem. , vol.253 , pp. 1654-1659
    • Hulse, J.D.1    Ellis, S.R.2    Henderson, L.M.3
  • 42
    • 0028978665 scopus 로고
    • Fatty acid β-oxidation in peroxisomes and mitochondria: The first, unequivocal evidence for the involvement of carnitine in shuttling propinyl-CoA from peroxisomes to mitochondria
    • Jacobs B.S., Wanders R.J.A. Fatty acid β-oxidation in peroxisomes and mitochondria: the first, unequivocal evidence for the involvement of carnitine in shuttling propinyl-CoA from peroxisomes to mitochondria. Biochem. Biophys. Res. Commun. 213:1995;1035-1041
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 1035-1041
    • Jacobs, B.S.1    Wanders, R.J.A.2
  • 43
    • 0029909714 scopus 로고    scopus 로고
    • Vitamin C depletion is associated with alterations in blood histamine and plasma free carnitine in adults
    • Johnston C.S., Solomon R.E., Corte C. Vitamin C depletion is associated with alterations in blood histamine and plasma free carnitine in adults. J. Am. Coll. Nutr. 15:1996;586-591
    • (1996) J. Am. Coll. Nutr. , vol.15 , pp. 586-591
    • Johnston, C.S.1    Solomon, R.E.2    Corte, C.3
  • 44
    • 4444277089 scopus 로고    scopus 로고
    • Phosphorylation of rat liver mitochondrial carnitine palmitoyltransferase-I (CPT-I): Effect on the enzyme's kinetic properties
    • 2004 July 9 [Epub ahead of print]
    • Kerner, J., Distler, A.M., Minkler, P.E., Parland, W., Peterman, S.M., 2004. Phosphorylation of rat liver mitochondrial carnitine palmitoyltransferase- I (CPT-I): Effect on the enzyme's kinetic properties. J. Biol. Chem. 2004 July 9 [Epub ahead of print]
    • (2004) J. Biol. Chem.
    • Kerner, J.1    Distler, A.M.2    Minkler, P.E.3    Parland, W.4    Peterman, S.M.5
  • 45
    • 0031868466 scopus 로고    scopus 로고
    • Genetic disorders of carnitine metabolism and their nutritional management
    • Kerner J., Hoppel C. Genetic disorders of carnitine metabolism and their nutritional management. Ann. Rev. Nutr. 18:1998;179-206
    • (1998) Ann. Rev. Nutr. , vol.18 , pp. 179-206
    • Kerner, J.1    Hoppel, C.2
  • 46
  • 47
    • 0019302749 scopus 로고
    • Plasma carnitine levels in adult males in India: Effects of high cereal, low fat diet, fat supplementation, and nutrition status
    • Khan-Siddiqui L., Bamji M.S. Plasma carnitine levels in adult males in India: effects of high cereal, low fat diet, fat supplementation, and nutrition status. Am. J. Clin.Nutr. 33:1980;1259-1263
    • (1980) Am. J. Clin.Nutr. , vol.33 , pp. 1259-1263
    • Khan-Siddiqui, L.1    Bamji, M.S.2
  • 48
    • 0027213744 scopus 로고
    • Mature carnitine palmitoyltransferase I retains the N-terminus of the nascentprotein in rat liver
    • Kolodziej M.P., Zammit V.A. Mature carnitine palmitoyltransferase I retains the N-terminus of the nascentprotein in rat liver. FEBS Lett. 327:1993;294-296
    • (1993) FEBS Lett. , vol.327 , pp. 294-296
    • Kolodziej, M.P.1    Zammit, V.A.2
  • 51
    • 0029416813 scopus 로고
    • Beta-oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: A century of continued progress
    • Kunau W.-H., Dommes V., Schulz H. Beta-oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: a century of continued progress. Prog. Lipid Res. 34:1995;267-342
    • (1995) Prog. Lipid Res. , vol.34 , pp. 267-342
    • Kunau, W.-H.1    Dommes, V.2    Schulz, H.3
  • 52
    • 0022600613 scopus 로고
    • Dietary carnitine intake related to skeletal muscle and plasma carnitine concentrations in adult men and women
    • Lennon D.L., Shrago E.R., Madden M., Nagle F.J., Hanson P. Dietary carnitine intake related to skeletal muscle and plasma carnitine concentrations in adult men and women. Am. J. Clin.Nutr. 43:1986;234-238
    • (1986) Am. J. Clin.Nutr. , vol.43 , pp. 234-238
    • Lennon, D.L.1    Shrago, E.R.2    Madden, M.3    Nagle, F.J.4    Hanson, P.5
  • 53
    • 0024313361 scopus 로고
    • Carnitine status of lactoovovegetarians and strict vegetarian adults and children
    • Lombard K.A., Olson A.L., Nelson S.E., Rebouche C.J. Carnitine status of lactoovovegetarians and strict vegetarian adults and children. Am. J. Clin. Nutr. 50:1989;301-306
    • (1989) Am. J. Clin. Nutr. , vol.50 , pp. 301-306
    • Lombard, K.A.1    Olson, A.L.2    Nelson, S.E.3    Rebouche, C.J.4
  • 54
    • 0031043030 scopus 로고    scopus 로고
    • The mitochondrial carnitine palmitoyltransferase system. From concept to molecular analysis
    • McGarry J.D., Brown N.F. The mitochondrial carnitine palmitoyltransferase system. From concept to molecular analysis. Eur. J. Biochem. 244:1997;1-14
    • (1997) Eur. J. Biochem. , vol.244 , pp. 1-14
    • McGarry, J.D.1    Brown, N.F.2
  • 55
    • 0017875758 scopus 로고
    • Carnitine palmitoyltransferase I. The site of inhibition of hepatic fatty acid oxidation by malonyl-CoA
    • McGarry J.D., Leatherman G.F., Foster D.W. Carnitine palmitoyltransferase I. The site of inhibition of hepatic fatty acid oxidation by malonyl-CoA. J. Biol. Chem. 253:1978;4128-4136
    • (1978) J. Biol. Chem. , vol.253 , pp. 4128-4136
    • McGarry, J.D.1    Leatherman, G.F.2    Foster, D.W.3
  • 56
    • 0023475402 scopus 로고
    • Pivampicillin-promoted excretion of pivaloylcarnitine in humans
    • Melegh B., Kerner J., Bieber L.L. Pivampicillin-promoted excretion of pivaloylcarnitine in humans. Biochem. Pharmacol. 36:1987;3405-3409
    • (1987) Biochem. Pharmacol. , vol.36 , pp. 3405-3409
    • Melegh, B.1    Kerner, J.2    Bieber, L.L.3
  • 57
    • 0017197573 scopus 로고
    • The relationship between serum carnitine levels and the nutritional status of patients with schistosomiasis
    • Mikhail M.M., Mansour M.M. The relationship between serum carnitine levels and the nutritional status of patients with schistosomiasis. Clin. Chim. Acta. 71:1976;207-214
    • (1976) Clin. Chim. Acta , vol.71 , pp. 207-214
    • Mikhail, M.M.1    Mansour, M.M.2
  • 58
    • 4444220059 scopus 로고    scopus 로고
    • Quantitation of long-chain acylcarnitines by HPLC/fluorescence detection: Application to plasma and tissue specimens from patients with carnitine palmitoyltransferase-II deficiency
    • in press
    • Minkler, P.E., Kerner, J., North, K.N., Hoppel, C.L., 2004. Quantitation of long-chain acylcarnitines by HPLC/fluorescence detection: application to plasma and tissue specimens from patients with carnitine palmitoyltransferase-II deficiency. Clin. Chim. Acta, in press
    • (2004) Clin. Chim. Acta
    • Minkler, P.E.1    Kerner, J.2    North, K.N.3    Hoppel, C.L.4
  • 59
    • 0343505447 scopus 로고
    • Malonyl-CoA binding site and the overt carnitine palmitoyltransferase activity reside on opposite sides of the mitochondrial membrane
    • Murthy M.S.R., Pande S.V. Malonyl-CoA binding site and the overt carnitine palmitoyltransferase activity reside on opposite sides of the mitochondrial membrane. Proc. Natl. Acad. Sci. USA. 84:1987;378-382
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 378-382
    • Murthy, M.S.R.1    Pande, S.V.2
  • 60
    • 0028231541 scopus 로고
    • Cholate extracts of mitochondrial outer membranes increase inhibition by malonyl-CoA of carnitine palmitoyltransferase-I by a mechanism involving phospholipids
    • Mynatt R.L., Greenhaw J.J., Cook G.A. Cholate extracts of mitochondrial outer membranes increase inhibition by malonyl-CoA of carnitine palmitoyltransferase-I by a mechanism involving phospholipids. Biochem. J. 299:1994;761-767
    • (1994) Biochem. J. , vol.299 , pp. 761-767
    • Mynatt, R.L.1    Greenhaw, J.J.2    Cook, G.A.3
  • 61
    • 0028950214 scopus 로고
    • Evidence for intermediate channeling in mitochondrial beta-oxidation
    • Nada M.A., Rhead W.J., Sprecher H., Schulz H., Roe C.R. Evidence for intermediate channeling in mitochondrial beta-oxidation. J. Biol. Chem. 270:1995;530-535
    • (1995) J. Biol. Chem. , vol.270 , pp. 530-535
    • Nada, M.A.1    Rhead, W.J.2    Sprecher, H.3    Schulz, H.4    Roe, C.R.5
  • 63
    • 0008497558 scopus 로고
    • Carnitine levels in some higher plants
    • Panter R.A., Mudd J.B. Carnitine levels in some higher plants. FEBS Lett. 5:1969;169-170
    • (1969) FEBS Lett. , vol.5 , pp. 169-170
    • Panter, R.A.1    Mudd, J.B.2
  • 64
    • 0024465259 scopus 로고
    • Induction of ketogenesis and fatty acid oxidation by glucagon and cyclic AMP in cultured hepatocytes from rabbit fetuses. Evidence for a decreased sensitivity of carnitine palmitoyltransferase I to malonyl-CoA inhibition after glucagon or cyclic AMP treatment
    • Pegorier J.-P., Garcia-Garcia M., Prip-Buus C., Duee P.-H., Kohl C., Girard J. Induction of ketogenesis and fatty acid oxidation by glucagon and cyclic AMP in cultured hepatocytes from rabbit fetuses. Evidence for a decreased sensitivity of carnitine palmitoyltransferase I to malonyl-CoA inhibition after glucagon or cyclic AMP treatment. Biochem. J. 264:1989;93-100
    • (1989) Biochem. J. , vol.264 , pp. 93-100
    • Pegorier, J.-P.1    Garcia-Garcia, M.2    Prip-Buus, C.3    Duee, P.-H.4    Kohl, C.5    Girard, J.6
  • 67
    • 0032511158 scopus 로고    scopus 로고
    • Topological and functional analysis of the rat liver carnitine palmitoyltransferase I expressed in Saccharomyces cerevisiae
    • Prip-Buus C., Cohen I., Kohl C., Esser V., McGarry J.D., Girard J. Topological and functional analysis of the rat liver carnitine palmitoyltransferase I expressed in Saccharomyces cerevisiae. FEBS Lett. 429:1998;173-178
    • (1998) FEBS Lett. , vol.429 , pp. 173-178
    • Prip-Buus, C.1    Cohen, I.2    Kohl, C.3    Esser, V.4    McGarry, J.D.5    Girard, J.6
  • 69
    • 0022559004 scopus 로고
    • Synthesis of carnitine precursors and related compounds
    • Rebouche C.J. Synthesis of carnitine precursors and related compounds. Methods Enzymol. 123:1986;290-297
    • (1986) Methods Enzymol. , vol.123 , pp. 290-297
    • Rebouche, C.J.1
  • 70
    • 0024822538 scopus 로고
    • Utilization of dietary precursors for carnitine synthesis in human adults
    • Rebouche C.J., Bosch E.P., Chenard C.A., Schabold K.J., Nelson S.E. Utilization of dietary precursors for carnitine synthesis in human adults. J. Nutr. 119:1989;1907-1913
    • (1989) J. Nutr. , vol.119 , pp. 1907-1913
    • Rebouche, C.J.1    Bosch, E.P.2    Chenard, C.A.3    Schabold, K.J.4    Nelson, S.E.5
  • 71
    • 0025765643 scopus 로고
    • Metabolic fate of dietary carnitine in human adults: Identification and quantification of urinary and fecal metabolites 1
    • Rebouche C.J., Chenard C.A. Metabolic fate of dietary carnitine in human adults: identification and quantification of urinary and fecal metabolites 1. J. Nutr. 121:1991;539-546
    • (1991) J. Nutr. , vol.121 , pp. 539-546
    • Rebouche, C.J.1    Chenard, C.A.2
  • 73
    • 0020483684 scopus 로고
    • Sensitivity of carnitine acyltransferase I to malonly-CoA inhibition in isolated rat liver mitochondria is quantitatively related to hepatic malonyl-CoA concentration in vivo
    • Robinson N., Zammit V.A. Sensitivity of carnitine acyltransferase I to malonly-CoA inhibition in isolated rat liver mitochondria is quantitatively related to hepatic malonyl-CoA concentration in vivo. Biochem. J. 206:1982;177-179
    • (1982) Biochem. J. , vol.206 , pp. 177-179
    • Robinson, N.1    Zammit, V.A.2
  • 74
    • 0021028824 scopus 로고
    • Metabolic response to carnitine in methylmalonic aciduria: An effective strategy for elimination of propionyl groups
    • Roe C.R., Hoppel C.L., Stacey T.E., Chalmers R.A., Tracey B., Millington D.S. Metabolic response to carnitine in methylmalonic aciduria: an effective strategy for elimination of propionyl groups. Arch. Dis. Child. 58:1983;916-920
    • (1983) Arch. Dis. Child. , vol.58 , pp. 916-920
    • Roe, C.R.1    Hoppel, C.L.2    Stacey, T.E.3    Chalmers, R.A.4    Tracey, B.5    Millington, D.S.6
  • 76
    • 0017412248 scopus 로고
    • Deficiency of carnitine in cachectic cirrhotic patients
    • Rudman D., Sewell C.W., Ansley J.D. Deficiency of carnitine in cachectic cirrhotic patients. J. Clin. Invest. 60:1977;716-723
    • (1977) J. Clin. Invest , vol.60 , pp. 716-723
    • Rudman, D.1    Sewell, C.W.2    Ansley, J.D.3
  • 77
    • 0019336084 scopus 로고
    • Synthesis of carnitine from epsilon-N-trimethyllysine in post mitochondrial fractions of Neurospora crassa
    • Sachan D.S., Broquist H.P. Synthesis of carnitine from epsilon-N-trimethyllysine in post mitochondrial fractions of Neurospora crassa. Biochem. Biophys. Res. Commun. 96:1980;870-875
    • (1980) Biochem. Biophys. Res. Commun. , vol.96 , pp. 870-875
    • Sachan, D.S.1    Broquist, H.P.2
  • 78
    • 0019325283 scopus 로고
    • Carnitine biosynthesis. Hydroxylation of N6-trimethyl-lysine to 3-hydroxy-N6-trimethyl-lysine
    • Sachan D.S., Hoppel C.L. Carnitine biosynthesis. Hydroxylation of N6-trimethyl-lysine to 3-hydroxy-N6-trimethyl-lysine. Biochem. J. 188:1980;529-534
    • (1980) Biochem. J. , vol.188 , pp. 529-534
    • Sachan, D.S.1    Hoppel, C.L.2
  • 79
    • 0019465834 scopus 로고
    • Effects of fasting, adrenalectomy and streptozotocin-diabetes on sensitivity of hepatic carnitine acyltransferase to malonyl CoA
    • Saggerson E.D., Carpenter C.A. Effects of fasting, adrenalectomy and streptozotocin-diabetes on sensitivity of hepatic carnitine acyltransferase to malonyl CoA. FEBS Lett. 129:1981;225-228
    • (1981) FEBS Lett. , vol.129 , pp. 225-228
    • Saggerson, E.D.1    Carpenter, C.A.2
  • 80
    • 0029072276 scopus 로고
    • Multiple-dose pharmacokinetics and bioequivalence of L-carnitine 330-mg tablet versus 1-g chewable tablet versus enteral solution in healthy adult male volunteers
    • Sahajwalla C.G., Helton E.D., Purich E.D., Hoppel C.L., Cabana B.E. Multiple-dose pharmacokinetics and bioequivalence of L-carnitine 330-mg tablet versus 1-g chewable tablet versus enteral solution in healthy adult male volunteers. J. Pharm.Sci. 84:1995;627-633
    • (1995) J. Pharm.Sci. , vol.84 , pp. 627-633
    • Sahajwalla, C.G.1    Helton, E.D.2    Purich, E.D.3    Hoppel, C.L.4    Cabana, B.E.5
  • 81
    • 0028931890 scopus 로고
    • Fatty acid oxidation in peripheral blood cells: Characterization and use for the diagnosis of defects of fatty acid oxidation
    • Schaefer J., Pourfarzam M., Bartlett K., Jackson S., Turnbull D.M. Fatty acid oxidation in peripheral blood cells: characterization and use for the diagnosis of defects of fatty acid oxidation. Pediatr. Res. 37:1995;354-360
    • (1995) Pediatr. Res. , vol.37 , pp. 354-360
    • Schaefer, J.1    Pourfarzam, M.2    Bartlett, K.3    Jackson, S.4    Turnbull, D.M.5
  • 82
    • 0032483099 scopus 로고    scopus 로고
    • Deletion of the conserved first 18 N-terminal amino acid residues in rat liver carnitine palmitoyltransferase I abolishes malonyl-CoA sensitivity
    • Shi J., Zhu H., Arvidson D.N., Cregg J.M., Woldegiorgis G. Deletion of the conserved first 18 N-terminal amino acid residues in rat liver carnitine palmitoyltransferase I abolishes malonyl-CoA sensitivity. Biochemistry. 37:1998;11033-11038
    • (1998) Biochemistry , vol.37 , pp. 11033-11038
    • Shi, J.1    Zhu, H.2    Arvidson, D.N.3    Cregg, J.M.4    Woldegiorgis, G.5
  • 83
    • 0033515467 scopus 로고    scopus 로고
    • A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver carnitine palmitolytransferase I abolishes malonyl-CoA inhibition and high affinity binding
    • Shi J., Zhu H., Arvidson D.N., Woldegiorgis G. A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver carnitine palmitolytransferase I abolishes malonyl-CoA inhibition and high affinity binding. J. Biol. Chem. 274:1999;9421-9426
    • (1999) J. Biol. Chem. , vol.274 , pp. 9421-9426
    • Shi, J.1    Zhu, H.2    Arvidson, D.N.3    Woldegiorgis, G.4
  • 84
    • 0020657746 scopus 로고
    • The outer carnitine palmitoyltransferase and regulation of fatty acid metabolism in rat liver in different thyroid states
    • Stakkestad J.A., Bremer J. The outer carnitine palmitoyltransferase and regulation of fatty acid metabolism in rat liver in different thyroid states. Biochim. Biophys. Acta. 750:1983;244-252
    • (1983) Biochim. Biophys. Acta , vol.750 , pp. 244-252
    • Stakkestad, J.A.1    Bremer, J.2
  • 85
    • 0032212886 scopus 로고    scopus 로고
    • Roles of the N- and C-terminal domains of carnitine palmitoyltransferase I isoforms in malonyl-CoA sensitivity of the enzymes: Insight from expression of chimaeric proteins and mutation of conserved histidine residues
    • Swanson S.T., Foster D.W., McGarry J.D., Brown N.F. Roles of the N- and C-terminal domains of carnitine palmitoyltransferase I isoforms in malonyl-CoA sensitivity of the enzymes: insight from expression of chimaeric proteins and mutation of conserved histidine residues. Biochem. J. 335:1998;513-519
    • (1998) Biochem. J. , vol.335 , pp. 513-519
    • Swanson, S.T.1    Foster, D.W.2    McGarry, J.D.3    Brown, N.F.4
  • 86
    • 0034704135 scopus 로고    scopus 로고
    • Molecular and functional characterization of organic cation/carnitine transporter family in mice
    • Tamai I., Ohashi R., Nezu J.I., Sai Y., Kobayashi D., Oku A., Shimane M., Tsuji A. Molecular and functional characterization of organic cation/carnitine transporter family in mice. J. Biol. Chem. 275:2000;40064-40072
    • (2000) J. Biol. Chem. , vol.275 , pp. 40064-40072
    • Tamai, I.1    Ohashi, R.2    Nezu, J.I.3    Sai, Y.4    Kobayashi, D.5    Oku, A.6    Shimane, M.7    Tsuji, A.8
  • 87
    • 0032493741 scopus 로고    scopus 로고
    • Molecular and functional identification of sodium ion-dependent, high affinity human carnitine transporter OCTN2
    • Tamai I., Ohashi R., Nezu J., Yabuuchi H., Oku A., Shimane M., Sai Y., Tsuji A. Molecular and functional identification of sodium ion-dependent, high affinity human carnitine transporter OCTN2. J. Biol. Chem. 273:1998;20378-20382
    • (1998) J. Biol. Chem. , vol.273 , pp. 20378-20382
    • Tamai, I.1    Ohashi, R.2    Nezu, J.3    Yabuuchi, H.4    Oku, A.5    Shimane, M.6    Sai, Y.7    Tsuji, A.8
  • 88
    • 0021363060 scopus 로고
    • Effect of vitamin C deficiency on hydration of trimethylaminobutyrate to carnitine in the guinea pig
    • Thoma W.J., Henderson L.M. Effect of vitamin C deficiency on hydration of trimethylaminobutyrate to carnitine in the guinea pig. Biochim. Biophys. Acta. 797(1):1984;136-139
    • (1984) Biochim. Biophys. Acta. , vol.797 , Issue.1 , pp. 136-139
    • Thoma, W.J.1    Henderson, L.M.2
  • 89
    • 0032727932 scopus 로고    scopus 로고
    • A 22 kDa polyanion inhibits carnitine-dependent fatty acid oxidation in rat liver mitochondria
    • Turkaly P., Kerner J., Hoppel C. A 22 kDa polyanion inhibits carnitine-dependent fatty acid oxidation in rat liver mitochondria. FEBS Lett. 460:1999;241-245
    • (1999) FEBS Lett. , vol.460 , pp. 241-245
    • Turkaly, P.1    Kerner, J.2    Hoppel, C.3
  • 91
    • 0034468740 scopus 로고    scopus 로고
    • Possible involvement of cytoskeletal components in the control of hepatic carnitine palmitoyltransferase I activity
    • Velasco G., Geelen M.J.H., Gomez del Pulgar T., Guzman M. Possible involvement of cytoskeletal components in the control of hepatic carnitine palmitoyltransferase I activity. Adv. Exp. Med. Biol. 466:1999;43-52
    • (1999) Adv. Exp. Med. Biol. , vol.466 , pp. 43-52
    • Velasco, G.1    Geelen, M.J.H.2    Gomez Del Pulgar, T.3    Guzman, M.4
  • 92
    • 0031908208 scopus 로고    scopus 로고
    • Phytanic acid and pristanic acid are oxidized by sequential peroxisomal and mitochondrial reactions in cultured fibroblasts
    • Verhoeven N.M., Roe D.S., Kok R.M., Wanders R.J.A., Jacobs C., Roe C.R. Phytanic acid and pristanic acid are oxidized by sequential peroxisomal and mitochondrial reactions in cultured fibroblasts. J. Lipid Res. 39:1998;66-74
    • (1998) J. Lipid Res. , vol.39 , pp. 66-74
    • Verhoeven, N.M.1    Roe, D.S.2    Kok, R.M.3    Wanders, R.J.A.4    Jacobs, C.5    Roe, C.R.6
  • 94
    • 0023693078 scopus 로고
    • Skeletal muscle mitochondrial beta-oxidation. A study of the products of oxidation of [U-14C]hexadecanoate by h.p.l.c. using continuous on-line radiochemical detection
    • Watmough N.J., Bhuiyan A.K.M.J., Bartlett K., Sherratt H.S.A., Turnbull D.M. Skeletal muscle mitochondrial beta-oxidation. A study of the products of oxidation of [U-14C]hexadecanoate by h.p.l.c. using continuous on-line radiochemical detection. Biochem. J. 253:1988;541-547
    • (1988) Biochem. J. , vol.253 , pp. 541-547
    • Watmough, N.J.1    Bhuiyan, A.K.M.J.2    Bartlett, K.3    Sherratt, H.S.A.4    Turnbull, D.M.5
  • 95
    • 0034212998 scopus 로고    scopus 로고
    • Structural and functional characteristics and tissue distribution pattern of rat OCTN1, an organic cation transporter, cloned from placenta
    • Wu X., George R.L., Huang W., Wang H., Conaway S.J., Leibach F.H., Ganapathy V. Structural and functional characteristics and tissue distribution pattern of rat OCTN1, an organic cation transporter, cloned from placenta. Biochem. Biophys. Acta. 1466:2000;315-327
    • (2000) Biochem. Biophys. Acta , vol.1466 , pp. 315-327
    • Wu, X.1    George, R.L.2    Huang, W.3    Wang, H.4    Conaway, S.J.5    Leibach, F.H.6    Ganapathy, V.7
  • 96
    • 0032528903 scopus 로고    scopus 로고
    • Expression of novel isoforms of carnitine palmitoyltransferase I (CPT-I) generated by alternative splicing of the CPT-Iβ gene
    • Yu G.-S., Lu Y.-C., Gulick T. Expression of novel isoforms of carnitine palmitoyltransferase I (CPT-I) generated by alternative splicing of the CPT-Iβ gene. Biochem. J. 334:1998;225-231
    • (1998) Biochem. J. , vol.334 , pp. 225-231
    • Yu, G.-S.1    Lu, Y.-C.2    Gulick, T.3
  • 97
    • 0032584555 scopus 로고    scopus 로고
    • Rat carnitine palmitoyltransferase Iβ mRNA splicing isoforms
    • Yu G.-S., Lu Y.-C., Gulick T. Rat carnitine palmitoyltransferase Iβ mRNA splicing isoforms. Biochim. Biophys. Acta. 1393:1998;166-172
    • (1998) Biochim. Biophys. Acta , vol.1393 , pp. 166-172
    • Yu, G.-S.1    Lu, Y.-C.2    Gulick, T.3
  • 98
    • 0031967840 scopus 로고    scopus 로고
    • Lipid molecular order in liver mitochondrial outer membranes, and sensitivity of carnitine palmitoyltransferase I to malonyl-CoA
    • Zammit V.A., Corstorphine C., Kolodziej M., Fraser F. Lipid molecular order in liver mitochondrial outer membranes, and sensitivity of carnitine palmitoyltransferase I to malonyl-CoA. Lipids. 33:1998;371-376
    • (1998) Lipids , vol.33 , pp. 371-376
    • Zammit, V.A.1    Corstorphine, C.2    Kolodziej, M.3    Fraser, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.