Ultracentrifugation studies of the location of the site involved in the interaction of pig heart lactate dehydrogenase with acidic phospholipids at low pH. A comparison with the muscle form of the enzyme

Cellular and Molecular Biology Letters

Volumn 12, Issue 3, 2007, Pages 378-395

  Terlecki, Grzegorz ^a   Czapińska, Elzbieta ^a   Hotowy, Katarzyna ^a  

^a WROCLAW MEDICAL UNIVERSITY   (Poland)

Author keywords

Acidic phospholipids; Cardiolipin; Lactate dehydrogenase isoenzymes; Lipid protein interaction; Phosphatidylserine

Indexed keywords

ADENINE NUCLEOTIDE; ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; CARDIOLIPIN; CYTIDINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE; HEART ENZYME; ISOENZYME; LACTATE DEHYDROGENASE; LIPOSOME; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PHOSPHATIDYLSERINE; PHOSPHOLIPID; PYRUVIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; URIDINE TRIPHOSPHATE;

ANIMAL TISSUE; ARTICLE; BINDING SITE; COMPLEX FORMATION; CONCENTRATION RESPONSE; CROSS LINKING; ENZYME PHOSPHORYLATION; HEART MUSCLE; IONIC STRENGTH; ISOELECTRIC POINT; MOLECULAR INTERACTION; NONHUMAN; PH; PROTEIN LIPID INTERACTION; SKELETAL MUSCLE; SWINE; ULTRACENTRIFUGATION;

SUIDAE;

ADSORPTION; ANIMALS; CARDIOLIPINS; CROSS-LINKING REAGENTS; HYDROGEN-ION CONCENTRATION; L-LACTATE DEHYDROGENASE; LIPOSOMES; MUSCLE, SKELETAL; MYOCARDIUM; PHOSPHATIDYLSERINES; PHOSPHOLIPIDS; PROTEIN BINDING; RABBITS; SUS SCROFA; ULTRACENTRIFUGATION;

EID: 38049181239     PISSN: 14258153     EISSN: 16891392     Source Type: Journal    
DOI: 10.2478/s11658-007-0010-5     Document Type: Article

References (44)

1. Aubert, A., Costalat, R., Magistretti, P.J. and Pellerin, L. Brain lactate kinetics: Modeling evidence for neuronal lactate uptake upon activation. Proc. Natl. Acad. Sci. USA 102 (2005) 16448-16453.
2. (ATP) channel subunit essential for cell protection against ischemia. EMBO J. 21 (2002) 3936-3948.
3. Pioli, P.A., Hamilton, B.J., Connolly, J.E., Brewer, G. and Rigby, WF. Lactate dehydrogenase is an AU-rich element-binding protein that directly interacts with AUF1. J. Biol. Chem. 277 (2002) 35738-35745.
4. Li, S.S. Lactate dehydrogenase isoenzymes A (muscle), B (heart) and C (testis) of mammals and the genes coding for these enzymes. Biochem. Soc. Trans. 2 (1989) 304-307.
5. Li, S.S. Human and mouse lactate dehydrogenase genes A (muscle), B (heart), and C (testis): protein structure, genomic organization, regulation of expression, and molecular evolution. Prog. Clin. Biol. Res. 344 (1990) 75-99.
6. Read, J.A., Winter, V.J., Eszes, C.M., Sessions, R.B. and Brady, R.L. Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. Proteins 43 (2001) 175-185.
7. Wang, X.C., Jiang, L. and Zhou, H.M. Minimal functional unit of lactate dehydrogenase. J. Protein Chem. 3 (1997) 227-231.
8. King, L. and Weber, G. Conformational drift of dissociated lactate dehydrogenases. Biochemistry 25 (1986) 3632-3637.
9. Dabrowska, A. and Gutowicz, J. Interaction of bovine heart lactate dehydrogenase with erythrocyte lipids. Biochim. Biophys. Acta 855 (1986) 99-104.
10. Dabrowska, A., Terlecki, G. and Gutowicz, J. Interaction of bovine skeletal muscle lactate dehydrogenase with liposomes. Comparison with the data for the heart enzyme. Biochim. Biophys. Acta 980 (1989) 357-360.
11. Terlecki, G., Czapińska, E., Rogozik, K., Lisowski, M. and Gutowicz, J. Investigation of the interaction of pig muscle lactate dehydrogenase with acidic phospholipids at low pH. Biochim. Biophys. Acta 1758 (2006) 133-144.
12. Terlecki, G., Czapinska, E. and Gutowicz J. The role of lipid phase structure in the interaction of lactate dehydrogenase with phosphatidylserine. Activity studies. Cell. Mol. Biol. Lett. 7 (2002) 895-903.
13. Terlecki, G. and Gutowicz, J. Further evidence for the importance of lipid bilayers in the interaction between lactate dehydrogenase and phosphatidylserine. Cell. Mol. Biol. Lett. 7 (2002) 905-910.
14. Marsh, D. Handbook of Lipids Bilayers, CRC Press, Boca Raton, FL, 1990.
15. Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254.
16. Gottschalk, N. and Jaenicke, R. Chemically crosslinked lactate dehydrogenase: stability and reconstitution after glutaraldehyde fixation. Biotechnology and Applied Biochemistry 9 (1987) 387-400.
17. Rouser, G., Siakatos, A.N. and Fleischer, S. Quantitative analysis of phospholipids by thin-layer chromatography and phosphorus analysis of spots. Lipids 1 (1966) 85-86.
18. Cabiaux, V., Vandenbranden, M., Falmagne, P. and Ruysschaert, J.M. Aggregation and fusion of lipid vesicles induced by diphtheria toxin at low pH: possible involvement of the P site and the NAD+ binding site. Biosci. Rep. 3 (1985) 243-250.
19. Cabiaux, V., Vandenbranden, M., Falmagne, P. and Ruysschaert, J.M. Diphtheria toxin induces fusion of small unilamellar vesicles at low pH. Biochim. Biophys. Acta 775 (1984) 31-36.
20. Wittenberger, C.L. Kinetic studies on the inhibition of a (D(-)-specific lactate dehydrogenase by adenosine triphosphate. J. Biol. Chem. 243 (1968) 3067-3075.
21. Torres-da Matta, J., Batista e Silva, C. and Hasson-Voloch, A. Effect of ATP on purified L(+) lactate dehydrogenase from electric organ of Electrophorus electricus (L.). Int. J. Biochem. 18 (1986) 191-194.
22. Busto, F., de Arriaga, D. and Soler, J. ATP, ADP and AMP on the regulation of lactate dehydrogenase activity of Phycomyces blakesleeanus. Int. J. Biochem. 15 (1983) 73-78.
23. Nemat-Gorgani, M. and Wilson, J.E. Acidic phospholipids may inhibit rat brain hexokinase by interaction at the nucleotide binding site. Arch. Biochem. Biophys. 236 (1985) 220-227.
24. Craig, D.B. and Wallace, C.J. ATP binding to cytochrome c diminishes electron flow in the mitochondrial respiratory pathway. Protein Sci. 2 (1993) 966-976.
25. .Kimelberg, H.K and Lee, C.P. Binding and electron transfer to cytochrome c in artificial phospholipid membranes. Biochem. Biophys. Res. Commun. 34 (1969) 784-790.
26. Vanderkooi, J., Erecinska, M. and Chance, B. Cytochrome c interaction with membranes. II. Comparative study of the interaction of c cytochromes with the mitochondrial membrane. Arch. Biochem. Biophys. 152 (1973) 531-540.
27. Mustonen, P., Virtanen, J.A., Somerharju, P.J. and Kinnunen, P.K. Binding of cytochrome c to liposomes as revealed by the quenching of fluorescence from pyrene-labeled phospholipids. Biochemistry 26 (1987) 2991-2997.
28. Demel, R.A., Jordi, W., Lambrechts, H., van Damme, H., Hovius, R. and de Kruijff, B. Differential interactions of apo- and holocytochrome c with acidic membrane lipids in model systems and the implications for their import into mitochondria. J. Biol. Chem. 264 (1989) 3988-3997.
29. Nicholls, P. Cytochrome c binding to enzymes and membranes. Biochim. Biophys. Acta 346 (1974) 261-310.
30. Brown, L.R. and Wuthrich, K. NMR and ESR studies of the interactions of cytochrome c with mixed cardiolipin-phosphatidylcholine vesicles. Biochim. Biophys. Acta 468 (1977) 389-410.
31. Rytomaa, M., Mustonen, P. and Kinnunen, P.K. Reversible, nonionic, and pH-dependent association of cytochrome c with cardiolipin-phosphatidylcholine liposomes. J. Biol. Chem. 267 (1992) 22243-22248.
32. Rytomaa, M. and Kinnunen, P.K. Evidence for two distinct acidic phospholipid-binding sites in cytochrome c. J. Biol. Chem. 269 (1994) 1770-1774.
33. Lovell, S.J. and Winzor, D.J. Effects of phosphate on the dissociation and enzymatic stability of rabbit muscle lactate dehydrogenase. Biochemistry 13 (1974) 3527-3531.
34. Okeley, N.M. and Gelb, M.H. A designed probe for acidic phospholipids reveals the unique enriched anionic character of the cytosolic face of the mammalian plasma membrane. J. Biol. Chem. 279 (2004) 21833-21840.
35. Korzeniewski, B. and Zoladz, J.A. Influence of rapid changes in cytosolic pH on oxidative phosphorylation in skeletal muscle: theoretical studies. Biochem. J. 365 (2002) 249-258.
36. Korzeniewski, B. AMP deamination delays muscle acidification during heavy exercise and hypoxia. J. Biol. Chem. 281 (2006) 3057-3066.
37. Kraayenhof, R., Sterk, G.J. and Sang, H.W. Probing biomembrane interfacial potential and pH profiles with a new type of float-like fluorophores positioned at varying distance from the membrane surface. Biochemistry 32 (1993) 10057-10066.
38. Zhao, H., Tuominen, E.K. and Kinnunen, P.K. Formation of amyloid fibers triggered by phosphatidylserine-containing membranes. Biochemistry 43 (2004) 10302-10307.
39. Baba, N. and Sharma, H.M. Histochemistry of lactic dehydrogenase in heart and pectoralis muscles of rat. J. Cell. Biol. 51 (1971) 621-635.
40. Kline, E.S., Brandt, R.B., Laux, J.E., Spainhour, S.E., Higgins, E.S., Rogers, K.S., Tinsley, S.B. and Waters, M.G. Localization of L-lactate dehydrogenase in mitochondria. Arch. Biochem. Biophys. 246 (1986) 673-680.
41. Brandt, R.B., Laux, J.E., Spainhour, S.E. and Kline, E.S. Lactate dehydrogenase in rat mitochondria. Arch. Biochem. Biophys. 259 (1987) 412-422
42. Gladden, LB. Lactate metabolism: a new paradigm for the third millennium. J. Physiol. 558 (2004) 5-30.
43. Brooks, G.A., Dubouchaud, H., Brown, M., Sicurello, J.P. and Butz, C.E. Role of mitochondrial lactate dehydrogenase and lactate oxidation in the intracellular lactate shuttle. Proc. Natl. Acad. Sci. USA 96 (1999) 1129-1134.
44. Hashimoto, T., Hussien, R. and Brooks, G.A. Colocalization of MCT1, CD147, and LDH in mitochondrial inner membrane of L6 muscle cells: evidence of a mitochondrial lactate oxidation complex. Am. J. Physiol. Endocrinol. Metab. 290 (2006) 1237-1244.