M-LDH Serves as a Regulatory Subunit of the Cytosolic Substrate-channelling Complex in Vivo

Journal of Molecular Biology

Volumn 371, Issue 2, 2007, Pages 349-361

  Jovanović, Sofija ^a   Jovanović, Aleksandar ^a   Crawford, Russell M ^b  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

^b UNIVERSITY OF ST ANDREWS   (United Kingdom)

Author keywords

AMPK; lactate dehydrogenase; NDPK; redox status; substrate channelling

Indexed keywords

ACETYL COENZYME A CARBOXYLASE; CASEIN KINASE II; ENZYME; GLYCOLYTIC ENZYME; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; LACTATE DEHYDROGENASE; MUSCLE ENZYME; NUCLEOSIDE DIPHOSPHATE KINASE A; NUCLEOSIDE DIPHOSPHATE KINASE B; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BIOCHEMISTRY; CELL METABOLISM; CONTROLLED STUDY; ENZYME ACTIVITY; HYPOTHESIS; IN VIVO STUDY; LIVER CYTOSOL; MOUSE; NONHUMAN; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; RAT;

EID: 34447285530     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.05.081     Document Type: Article

References (40)

1. Heidbuchel H., Callewaert G., Vereecke J., and Carmeliet E. Membrane-bound nucleoside diphosphate kinase activity in atrial cells of frog, guinea pig, and human. Circulat. Res. 71 (1992) 808-820
2. Crawford R.M., Treharne K.J., Best O.G., Muimo R., Riemen C.E., and Mehta A. A novel physical and functional association between nucleoside diphosphate kinase A and AMP-activated protein kinase alpha1 in liver and lung. Biochem. J. 392 (2005) 201-209
3. Roymans D., Willems R., Van Blockstaele D.R., and Slegers H. Nucleoside diphosphate kinase (NDPK/NM23) and the waltz with multiple partners: possible consequences in tumor metastasis. Clin. Expt. Metastasis 19 (2002) 465-476
4. Postel E.H. NM23-NDP kinase. Int. J. Biochem. Cell Biol. 30 (1998) 1291-1295
5. Engel M., Veron M., Theisinger B., Lacombe M.L., Seib T., Dooley S., and Welter C. A novel serine/threonine-specific protein phosphotransferase activity of Nm23/nucleoside-diphosphate kinase. Eur. J. Biochem. 234 (1995) 200-207
6. Crawford R.M., Treharne K.J., Best O.G., Riemen C.E., Muimo R., Gruenert D.C., et al. NDPK-A (but not NDPK-B) and AMPK alpha1 (but not AMPK alpha2) bind the cystic fibrosis transmembrane conductance regulator in epithelial cell membranes. Cell Signal 18 (2006) 1595-1603
7. Konig J., Schreiber R., Mall M., and Kunzelmann K. No evidence for inhibition of ENaC through CFTR-mediated release of ATP. Biochim. Biophys. Acta 1565 (2002) 17-28
8. + channel. Proc. Natl Acad. Sci. USA 96 (1999) 5310-5315
9. Kahn B.B., Alquier T., Carling D., and Hardie D.G. AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism. Cell Metab. 1 (2005) 15-25
10. Stapleton D., Mitchelhill K.I., Gao G., Widmer J., Michell B.J., Teh T., et al. Mammalian AMP-activated protein kinase subfamily. J. Biol. Chem. 271 (1996) 611-614
11. Nielsen J.N., Mustard K.J., Graham D.A., Yu H., MacDonald C.S., Pilegaard H., et al. 5′-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle. J. Appl. Physiol. 94 (2003) 631-641
12. Hardie D.G., and Carling D. The AMP-activated protein kinase-fuel gauge of the mammalian cell?. Eur J. Biochem. 246 (1997) 259-273
13. Rafaeloff-Phail R., Ding L., Conner L., Yeh W.K., McClure D., Guo H., et al. Biochemical regulation of mammalian AMP-activated protein kinase activity by NAD and NADH. J. Biol. Chem. 279 (2004) 52934-52939
14. Hardie D.G., and Hawley S.A. AMP-activated protein kinase: the energy charge hypothesis revisited. BioEssays 23 (2001) 1112-1119
15. Pinna L.A. The raison d'etre of constitutively active protein kinases: the lesson of CK2. Accts Chem. Re. 36 (2003) 378-384
16. Meggio F., and Pinna L.A. One-thousand-and -one substrates of protein kinase CK2?. FASEB J. 17 (2003) 349-368
17. Meggio F., Marin O., and Pinna L.A. Substrate specificity of protein kinase CK2. Cell Mol. Biol. Res. 40 (1994) 401-409
18. Biondi R.M., Engel M., Sauane M., Welter C., Issinger O.G., Jimenez de Asua L., and Passeron S. Inhibition of nucleoside diphosphate kinase activity by in vitro phosphorylation by protein kinase CK2. Differential phosphorylation of NDP kinases in HeLa cells in culture. FEBS Letters 399 (1996) 183-187
19. Crawford R.M., Treharne K.J., Arnaud-Dabernat S., Daniel J.Y., Foretz M., Viollet B., and Mehta A. Protein kinase CK2 acts as a signal molecule switching between the NDPK-A/AMPK {alpha}1 complex and NDPK-B. FASEB J 21 (2006) 88-98
20. Makkonen M., Puhakainen E., Hanninen O., and Castren O. Lactate dehydrogenase isoenzymes in human myometrium during pregnancy and labor. Acta Obstet. Gynecol. Scand. 61 (1982) 35-37
21. Prabhakaram M., and Singh S.N. Alterations in rat lactate dehydrogenase: age-related comparison of M- and H-LDH. Biochem. Int. 9 (1984) 399-404
22. Sjodin B. Lactate dehydrogenase in human skeletal muscle. Acta Physiol. Scand. Suppl. 436 (1976) 1-32
23. Crawford R.M., Budas G.R., Jovanovic S., Ranki H. J., Wilson T.J., Davies A.M., and Jovanovic A. M-LDH serves as a sarcolemmal K(ATP) channel subunit essential for cell protection against ischemia. EMBO J. 21 (2002) 3936-3948
24. Crawford R.M., Treharne K.J., Arnaud-Dabernat S., Daniel J.Y., Foretz M., Viollet B., and Mehta A. Understanding the molecular basis of the interaction between NDPK-A and AMPK {alpha}1. Mol. Cell Biol. 26 (2006) 5921-5931
25. Ranki H.J., Crawford R.M., Budas G.R., and Jovanovic A. Ageing is associated with a decrease in the number of sarcolemmal ATP-sensitive K+ channels in a gender-dependent manner. Mech. Ageing Dev. 123 (2002) 695-705
26. + channel in vivo. FASEB J. 16 (2002) 102-104
27. Sullivan J.E., Carey F., Carling D., and Beri R.K. Characterisation of 5′-AMP-activated protein kinase in human liver using specific peptide substrates and the effects of 5′-AMP analogues on enzyme activity. Biochem. Biophys. Res. Commun. 200 (1994) 1551-1556
28. Muimo R., Hornickova Z., Riemen C.E., Gerke V., Matthews H., and Mehta A. Histidine phosphorylation of annexin I in airway epithelia. J. Biol. Chem. 275 (2000) 36632-36636
29. Kim S.H., and Lee G.M. Down-regulation of lactate dehydrogenase-A by siRNAs for reduced lactic acid formation of Chinese hamster ovary cells producing thrombopoietin. Appl. Microbiol. Biotechnol. 74 (2007) 152-159
30. Chang C.L., Strahler J.R., Thoraval D.H., Qian M. G., Hinderer R., and Hanash S.M. A nucleoside diphosphate kinase A (nm23-H1) serine 120 → glycine substitution in advanced stage neuroblastoma affects enzyme stability and alters protein-protein interaction. Oncogene 12 (1996) 659-667
31. Milne E.M., and Doxey D.L. Lactate dehydrogenase and its isoenzymes in the tissues and sera of clinically normal dogs. Res. Vet. Sci. 43 (1987) 222-224
32. McClelland G.B., Khanna S., Gonzalez G.F., Butz C.E., and Brooks G.A. Peroxisomal membrane monocarboxylate transporters: evidence for a redox shuttle system?. Biochem. Biophys. Res. Commun. 304 (2003) 130-135
33. Kim M.S., and Lee K.U. Role of hypothalamic 5′-AMP-activated protein kinase in the regulation of food intake and energy homeostasis. J. Mol. Med. 83 (2005) 514-520
34. Shen Q.W., Means W.J., Underwood K.R., Thompson S.A., Zhu M.J., McCormick R.J., et al. Early post-mortem AMP-activated protein kinase (AMPK) activation leads to phosphofructokinase-2 and -1 (PFK-2 and PFK-1) phosphorylation and the development of pale, soft, and exudative (PSE) conditions in porcine longissimus muscle. J. Agric. Food Chem. 54 (2006) 5583-5589
35. Brooks G.A. Lactate shuttle - between but not within cells?. J. Physiol. 541 (2002) 333-334
36. Brooks G.A. Lactate shuttles in nature. Biochem. Soc. Trans. 30 (2002) 258-264
37. Ide K., and Secher N.H. Cerebral blood flow and metabolism during exercise. Prog. Neurobiol. 61 (2000) 397-414
38. Pellerin L., Pellegri G., Martin J.L., and Magistretti P. J. Expression of monocarboxylate transporter mRNAs in mouse brain: support for a distinct role of lactate as an energy substrate for the neonatal vs. adult brain. Proc. Natl Acad. Sci. USA 95 (1998) 3990-3995
39. Cerdan S., Rodrigues T.B., Sierra A., Benito M., Fonseca L.L., Fonseca C.P., and Garcia-Martin M.L. The redox switch/redox coupling hypothesis. Neurochem. Int. 48 (2006) 523-530
40. Trabold O., Wagner S., Wicke C., Scheuenstuhl H., Hussain M.Z., Rosen N., et al. Lactate and oxygen constitute a fundamental regulatory mechanism in wound healing. Wound Repair Regen. 11 (2003) 504-509