Brain pyruvate and 2-oxoglutarate dehydrogenase complexes are mitochondrial targets of the CoA ester of the Refsum disease marker phytanic acid

FEBS Letters

Volumn 580, Issue 14, 2006, Pages 3551-3557

  Bunik, Victoria I ^a   Raddatz, Günter ^b   Wanders, Ronald J A ^c   Reiser, Georg ^d  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b MAX PLANCK INSTITUTE FOR BIOLOGICAL CYBERNETICS   (Germany)

^c ACADEMIC MEDICAL CENTER   (Netherlands)

^d OTTO VON GUERICKE UNIVERSITY   (Germany)

Author keywords

2 Oxo acid dehydrogenase complex; Long chain acyl CoA; Neurodegeneration; Peroxisomal inherited disorder; Phytanic acid; Thiamine

Indexed keywords

COENZYME A; DIHYDROLIPOAMIDE ACETYLTRANSFERASE; ESTER; OXOGLUTARATE DEHYDROGENASE; PALMITOYL COENZYME A; PHYTANIC ACID; PYRUVIC ACID;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; BRAIN MITOCHONDRION; COMPLEX FORMATION; DRUG EFFECT; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SUBSTRATE; FEMALE; IC 50; MITOCHONDRIAL RESPIRATION; NEUROLOGIC DISEASE; NONHUMAN; PRIORITY JOURNAL; RAT; REFSUM DISEASE;

ANIMALS; BIOLOGICAL MARKERS; BRAIN; COENZYME A; FEMALE; KETOGLUTARATE DEHYDROGENASE COMPLEX; MODELS, MOLECULAR; PHYTANIC ACID; PYRUVIC ACID; RATS; REFSUM DISEASE;

EID: 33646902437     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.05.040     Document Type: Article

References (42)

1. Wanders R.J., Jansen G.A., and Lloyd M.D. Phytanic acid alpha-oxidation, new insights into an old problem, a review. Biochim. Biophys. Acta 1631 (2003) 119-135
2. Schönfeld P., Kahlert S., and Reiser G. In brain mitochondria the branched-chain fatty acid phytanic acid impairs energy transduction and sensitizes for permeability transition. Biochem. J. 383 (2004) 121-128
3. 2+ homeostasis and mitochondria, and reduces cell viability in rat hippocampal astrocytes. Neurobiol. Dis. 18 (2005) 110-118
4. Schönfeld P., and Reiser G. Rotenone-like action of the branched-chain phytanic acid induces oxidative stress in mitochondria. J. Biol. Chem. 281 (2006) 7136-7142
5. 0.5 for α-ketoglutarate. Biochemistry 20 (1981) 2512-2518
6. Lawlis V.B., and Roche T.E. Inhibition of bovine kidney α-ketoglutarate dehydrogenase complex by reduced nicotinamide adenine dinucleotide in the presence or absence of calcium ion and effect of adenosine 5′-diphosphate on reduced nicotinamide adenine dinucleotide inhibition. Biochemistry 20 (1981) 2519-2524
7. Rutter G.A., McCormack J.G., Midgley P.J.W., and Denton R.M. The role of Ca in the hormonal regulation of the activities of pyruvate dehydrogenase and oxoglutarate dehydrogenase complexes. Ann. N. Y. Acad. Sci. 573 (1989) 206-217
8. Bunik V., and Sievers C. Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species. Eur. J. Biochem. 269 (2002) 5004-5015
9. Bunik V. 2-Oxo acid dehydrogenase complexes in redox regulation. Role of the lipoate residues and thioredoxin. Eur. J. Biochem. 270 (2003) 1036-1042
10. Gibson G.E., Blass J.P., Beal M.F., and Bunik V. The α-ketoglutarate dehydrogenase complex, a mediator between mitochondria and oxidative stress in neurodegeneration. Mol. Neurobiol. 31 (2005) 43-63
11. Roche T.E., Hiromasa Y., Turkan A., Gong X., Peng T., Yan X., Kasten S.A., Bao H., and Dong J. Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1. Eur. J. Biochem. 270 (2003) 1050-1056
12. Erfle J.D., and Sauer F. The inhibitory effects of acyl-coenzyme A esters on the pyruvate and alpha-oxoglutarate dehydrogenase complexes. Biochim. Biophys. Acta 178 (1969) 441-452
13. Shen L.C., and Atkinson D.E. Regulation of pyruvate dehydrogenase from Escherichia coli. Interaction of adenylate energy charge and other regulatory parameters. J. Biol. Chem. 245 (1970) 5974-5978
14. Bresters T.W., De Abreu R.A., DeKok A., Visser J., and Veeger C. The pyruvate dehydrogenase complex from Azotobacter vinelandii. 1. Purification and properties. Eur. J. Biochem. 59 (1975) 335-345
15. Bresters T.W., DeKok A., and Veeger C. The pyruvate dehydrogenase complex from Azotobacter vinelandii. 2. Regulation of the activity. Eur. J. Biochem. 59 (1975) 347-353
16. Smith C.M., Bryla J., and Williamson J.R. Regulation of mitochondrial α-ketoglutarate metabolism by product inhibition at α-ketoglutarate dehydrogenase. J. Biol. Chem. 249 (1974) 1497-1505
17. Garland P.B. Some kinetic properties of pig heart oxoglutarate dehydrogenase that provide a basis for metabolic control of the enzyme activity and also a stoichiometric assay for coenzyme A in tissue extracts. Biochem. J. 92 (1964) 10c-12c
18. Gomazkova V.S., and Krasovskaia O.E. Regulation of α-ketoglutarate dehydrogenase complex from pigeon breast muscle. Biokhimiia (Russian) 44 (1979) 1126-1136
19. Hamada M., Koike K., Nakaula Y., Hiraoka T., Koike M., and Hishimoto T. A kinetic study of the α-keto acid dehydrogenase complexes from pig heart mitochondria. J. Biochem. 77 (1975) 1047-1056
20. Kornfeld S., Benziman M., and Milner Y. α-Ketoglutarate dehydrogenase complex of Acetobacter xylinum. Purification and regulatory properties. J. Biol. Chem. 252 (1977) 2940-2947
21. Stumpf D.A., Parker W.D., and Angelini C. Carnitine deficiency, organic acidemias, and Reye's syndrome. Neurology 35 (1985) 1041-1045
22. Casteels M., Foulon V., Mannaerts G.P., and Van Veldhoven P.P. Alpha-oxidation of 3-methyl-substituted fatty acids and its thiamine dependence. Eur. J. Biochem. 270 (2003) 1619-1627
23. Denton R.M., and Hughes W.A. Pyruvate dehydrogenase and the hormonal regulation of fat synthesis in mammalian tissues. Int. J. Biochem. 9 (1978) 545-552
24. Shrago E., Ball M., Sul H.S., Baquer N.Z., and McLean P. Interrelationship in the regulation of pyruvate dehydrogenase and adenine-nucleotide translocase by palmitoyl-CoA in isolated mitochondria. Eur. J. Biochem. 75 (1977) 83-89
25. Olson M.S., Dennis S.C., Routh C.A., and Debuysere M.S. The regulation of pyruvate dehydrogenase by fatty acids in isolated rabbit heart mitochondria. Arch. Biochem. Biophys. 187 (1978) 121-131
26. Fatania H.R., Vary T.C., and Randle P.J. Modulation of pyruvate dehydrogenase kinase activity in cultured hepatocytes by glucagon and n-octanoate. Biochem. J. 234 (1986) 233-236
27. Lai J.C.K., Rimpel-Lamhaouar K., and Cooper A.J.L. Differential inhibition of mitochondrial dehydrogenases by fatty acyl-CoAs. Ann. N. Y. Acad. Sci. 573 (1989) 420-422
28. Bunik V., Denton T.T., Xu H., Thompson C.M., Cooper A.J.L., and Gibson G.E. Phosphonate analogs of α-ketoglutarate inhibit the activity of the α-ketoglutarate dehydrogenase complex isolated from brain and in cultured cells. Biochemistry 44 (2005) 10552-10561
29. Mattevi A., Obmolova G., Kalk K.H., Teplyakov A., and Hol W.G.J. Crystallographic analysis of substrate binding and catalysis in dihydrolipoyltransacetylase (E2p). Biochemistry 32 (1993) 3887-3901
30. Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-Pdb Viewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
31. Van Der Spoel D., Lindahl E., Hess B., Groenhof G., Mark A.E., and Berendsen H.J. GROMACS, fast, flexible, and free. J. Comput. Chem. 26 (2005) 1701-1718
32. Schwede T., Kopp J., Guex N., and Peitsch M.C. SWISS-MODEL, an automated protein homology-modeling server. Nucleic Acids Res. 31 (2003) 3381-3385
33. Rasmussen J.T., Borchers T., and Knudsen J. Comparison of the binding affinities of acyl-CoA-binding protein and fatty-acid-binding protein for long-chain acyl-CoA esters. Biochem. J. 265 (1990) 849-855
34. Bunik V.I., and Pavlova O.G. Inactivation of α-ketoglutarate dehydrogenase during oxidative decarboxylation of α-ketoadipic acid. FEBS Lett. 323 (1993) 166-170
35. Bunik V.I., and Pavlova O.G. Inhibition of α-ketoglutarate dehydrogenase from pigeon breast muscle by the structural analogs of substarte. Biochem. (Mosc.) 62 (1997) 1012-1020
36. Russel G.C., and Guest J.R. Sequence similarities within the family of dihydrolipoyl acyltransferases and discovery of a previously unidentified fungal enzyme. Biochim. Biophys. Acta 1076 (1991) 225-232
37. Cooney G.J., Taegtmeyer H., and Newsholm E.A. Tricarboxylic acid flux and enzyme activities in the isolated working rat heart. Biochem. J. 200 (1981) 701-703
38. Danson M.J., Ferscht A.R., and Perham R.N. Rapid intramolecular coupling of active sites in the pyruvate dehydrogenase complex of Escherichia coli, mechanism for rate enhancement in a multimeric structure. Proc. Natl. Acad. Sci. USA 75 (1978) 5386-5390
39. Hackert M.L., Oliver R.M., and Reed L.J. Evidence for a multiple random coupling mechanism in the α-ketoglutarate dehydrogenase multienzyme complex of Escherichia coli, a computer model analysis. Proc. Natl. Acad. Sci. USA 80 (1983) 2226-2230
40. Powell G.L., Grothusen J.R., Zimmerman J.K., Evans C.A., and Fish W.W. A re-examination of some properties of fatty acyl-CoA micelles. J. Biol. Chem. 256 (1981) 12740-12747
41. Constantinides P.P., and Steim J.M. Physical properties of fatty acyl-CoA. Critical micelle concentration and micellar size and shape. J. Biol. Chem. 12 (1985) 7573-7580
42. Pahan K., Cofer J., Baliga P., and Singh I. Identification of phytanoyl-CoA ligase as a distinct acyl-CoA ligase in peroxisomes from cultured human skin fibroblasts. FEBS Lett. 322 (1993) 101-104