Investigation of the interaction of pig muscle lactate dehydrogenase with acidic phospholipids at low pH

Biochimica et Biophysica Acta - Biomembranes

Volumn 1758, Issue 2, 2006, Pages 133-144

  Terlecki, Grzegorz ^a   Czapiñska, Elzbieta ^a   Rogozik, Katarzyna ^a   Lisowski, Marek ^b   Gutowicz, Jan ^b  

^a WROCLAW MEDICAL UNIVERSITY   (Poland)

^b UNIVERSITY OF WROC AW   (Poland)

Author keywords

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

Indexed keywords

CARDIOLIPIN; DETERGENT; LACTATE DEHYDROGENASE; MUSCLE ENZYME; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLSERINE; PHOSPHOLIPID;

ACIDITY; ARTICLE; BILAYER MEMBRANE; BINDING AFFINITY; BINDING SITE; CIRCULAR DICHROISM; DENSITY; IONIC STRENGTH; MEMBRANE BINDING; MEMBRANE COMPONENT; MEMBRANE VESICLE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN INTERACTION; QUALITATIVE ANALYSIS; QUANTITATIVE ANALYSIS; SURFACE CHARGE; SWINE;

ANIMALS; CARDIOLIPINS; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; KINETICS; L-LACTATE DEHYDROGENASE; LIPID BILAYERS; LIPOSOMES; MUSCLE, SKELETAL; PHOSPHATIDYLCHOLINES; PHOSPHATIDYLSERINES; PHOSPHOLIPIDS; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; SWINE;

SUS SCROFA;

EID: 33646251119     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.02.013     Document Type: Article

References (63)

1. Clarke F.M., and Masters C.J. On the association of glycolytic enzymes with structural proteins of skeletal muscle. Biochim. Biophys. Acta 381 (1975) 37-46
2. Masters C.J. Interactions between soluble enzymes and subcellular structure. CRC Crit. Rev. Biochem. 11 (1981) 105-143
3. Pierce G.N., and Philipson K.D. Binding of glycolytic enzymes to cardiac sarcolemmal and sarcoplasmic reticular membranes. J. Biol. Chem. 260 (1985) 6862-6870
4. Sagrista M.L., and Bozal J. Lactate and malate dehydrogenase binding to the microsomal fraction from chicken liver. Biochimie 69 (1987) 1207-1215
5. Dabrowska A., and Gutowicz J. Adsorption of bovine muscle lactate dehydrogenase to erythrocyte membranes. Gen. Physiol. Biophys. 9 (1990) 529-534
6. Esakova T.V., and Ivanov M.V. Interaction of lactate dehydrogenase and the sarcoplasmic reticulum membrane. Biokhimiia 57 (1992) 253-266
7. Marmillot P., Keith T., Srivastava D.K., and Knull R. Effect of tubulin on the activity of the muscle isoenzyme of lactate dehydrogenase. Arch. Biochem. Biophys. 315 (1994) 467-472
8. Muronetz V.I., Shcherbatova N.A., and Nagradova N.K. Interaction of NAD-dependent dehydrogenases with human erythrocyte membranes. Evidence that d-glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase are catalytically active in a membrane-bound state. Appl. Biochem. Biotechnol. 61 (1996) 39-46
9. Sanz M.C., and Lluis C. Ambiquitous behavior of rabbit liver lactate dehydrogenase. Experientia 44 3 (1988 Mar. 15) 203-208
10. Biochim. Biophys. Acta 1325 (1997) 108-116
11. Campanelle M.E., Chu H., and Low P.S. Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane. Proc. Natl. Acad. Sci. U. S. A. 102 7 (2005) 2402-24007
12. Etemadi A.H. Membrane asymmetry. A survey and critical appraisal of the methodology: II. Methods for assessing the unequal distribution of lipids. Biochim. Biophys. Acta 604 (1980) 423-475
13. Devaux P.F. Static and dynamic lipid asymmetry in cell membranes. Biochemistry 30 (1991) 1163-1173
14. 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
15. 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
16. Farias R.N., Vinals A.L., and Morero R.D. Fusion of negatively charged phospholipid vesicles by insulin. Relationship with lipid fluidity. J. Biol. Chem. 261 (1986) 15508-15512
17. Agasoster A.V., Halskau O., Fuglebakk E., Froystein N.A., Muga A., Holmsen H., and Martinez A. The interaction of peripheral proteins and membranes studied with alpha-lactalbumin and phospholipid bilayers of various compositions. J. Biol. Chem. 278 (2003) 21790-21797
18. Van Blitterswijk W.J., De Veer G., Krol J.H., and Emmelot P. Comparative lipid analysis of purified plasma membranes and shed extracellular membrane vesicles from normal murine thymocytes and leukemic GRSL cells. Biochim. Biophys. Acta 688 (1982) 495-504
19. Hietanen E., Punnonen K., Punnonen R., and Auvinen O. Fatty acid composition of phospholipids and neutral lipids and lipid peroxidation in human breast cancer and lipoma tissue. Carcinogenesis 7 (1986) 1965-1969
20. Wells K., Farooqui A.A., Liss L., and Horrocks L.A. Neural membrane phospholipids in Alzheimer disease. Neurochem. Res. 20 (1995) 1329-1333
21. Waki A., Fujibayashi Y., Yonekura Y., Sadato N., Ishii Y., and Yokoyama A. Reassessment of FDG uptake in tumor cells: high FDG uptake as a reflection of oxygen-independent glycolysis dominant energy production. Nucl. Med. Biol. 24 (1997) 665-670
22. Xu R.H., Pelicano H., Zhou Y., Carew J.S., Feng L., Bhalla K.N., Keating M.J., and Huang P. Inhibition of glycolysis in cancer cells: a novel strategy to overcome drug resistance associated with mitochondrial respiratory defect and hypoxia. Cancer Res. 65 (2005) 613-621
23. Newell K., Franchi A., Pouyssegur J., and Tannock I. Studies with glycolysis-deficient cells suggest that production of lactic acid is not the only cause of tumor acidity. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 1127-1131
24. Cutaia M., and Parks N. Oxidant stress decreases Na+/H+ antiport activity in bovine pulmonary artery endothelial cells. Am. J. Physiol. 267 (1994) L649-L659
25. Cho Y.L., Lee K.S., Lee S.J., Namkoong S., Kim Y.M., Lee H., Ha K.S., Han J.A., Kwon Y.G., and Kim Y.M. Amiloride potentiates TRAIL-induced tumor cell apoptosis by intracellular acidification-dependent Akt inactivation. Biochem. Biophys. Res. Commun. 326 (2005) 752-758
26. Pedroso de Lima M.C., Nir S., Flasher D., Klappe K., Hoekstra D., and Duzgunes N. Fusion of Sendai virus with human HL-60 and CEM cells: different kinetics of fusion for two isolates. Biochim. Biophys. Acta 1070 (1991) 446-454
27. Ciriolo M.R., Palamara A.T., Incerpi S., Lafavia E., Bue M.C., De Vito P., Garaci E., and Rotilio G. Loss of GSH, oxidative stress, and decrease of intracellular pH as sequential steps in viral infection. J. Biol. Chem. 272 (1997) 2700-2708
28. Dabrowska A., and Gutowicz J. Interaction of bovine heart lactate dehydrogenase with erythrocyte lipids. Biochim. Biophys. Acta 855 (1986) 99-104
29. 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
30. 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
31. 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
32. Rand R.P., and Sengupta S. Structural studies by X-ray diffraction of model phospholipid-insulin membranes. Biochim. Biophys. Acta 255 (1972) 484-492
33. Hubner W., Mantsch H.M., and Kates M. Intramolecular hydrogen bonding in cardiolipin. Biochim. Biophys. Acta 1066 (1991) 166-174
34. Hoch F.L. Cardiolipins and biomembrane function. Biochim. Biophys. Acta 1113 (1992) 71-133
35. Ortiz A., Killian J.A., Verklij A.J., and Wilshnut J. Membrane fusion and the lamellar-to-inverted-hexagonal phase transition in cardiolipin vesicle systems induced by divalent cations. Biophys. J. 77 (1999) 2003-2014
36. 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
37. Bergmeyer H.U., Bernt E., and Hess B. In: Bergmeyer H.U. (Ed). Methods in Enzymatic Analysis (1965), Verlag Chemie, Weinheim 736-743
38. Bartlett G.R. Colorimetric assay methods for free and phosphorylated glyceric acids. J. Biol. Chem. 234 (1959) 466-468
39. MacDonald R.C., MacDonald R.I., Menco B.Ph.M., Takeshita K., Subbarao N.K., and Hu L. Small-volume extrusion apparatus for preparation of large, unilamellar vesicles. Biochim. Biophys. Acta 1061 (1991) 297-303
40. Rytomaa M., and Kinnunen P.K.J. Reversibility of the binding of cytochrome c to liposomes. Implications for lipid-protein interactions. J. Biol. Chem. 270 (1995) 3197-3202
41. Lakowicz J. Principles of Fluorescence Spectroscopy. Second edition (1999), Plenum Publishing
42. 2: identification of an inactive membrane bound state. Biochemistry 34 (1995) 14819-14828
43. Tsai I.H., Murthy S.N., and Steck T.L. Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 257 (1982) 1438-1442
44. Zhao H., Tuominen E.K.J., and Kinnunen P.K.J. Formation of amyloid fibers triggered by phosphatidylserine-containing membranes. Biochemistry 43 (2004) 10303-10307
45. Lovell S.J., and Winzor D.J. Effects of phosphate on the dissociation and enzymic stability of rabbit muscle lactate dehydrogenase. Biochemistry 13 (1974) 3527-3531
46. Wang X.C., Jiang L., and Zhou H.M. Minimal functional unit of lactate dehydrogenase. J. Protein. Chem. 16 (1997) 227-231
47. Marsh D. Handbook of Lipids Bilayers (1990), CRC Press, Boca Raton, FL
48. W.W. Christie, www.lipid.co.uk/infores/lipids.html.
49. Christie W.W. Lipid Analysis (2003), The Oily Press Lipid Library
50. Susor W.A., Kochman M., and Rutter W.J. Heterogeneity of presumably homogeneous protein preparations. Science 165 (1969) 1260-1262
51. Weller D.L., Heaney A., Franceschi R.T., Boudreau R.E., and Shaw D.E. Isoelectric focusing and study of ribosomal proteins and lactate dehydrogenase. Ann. N.Y. Acad. Sci. 209 (1973) 258-280
52. Pettit S.M., Nealon D.A., and Henderson A.R. Purification of lactate dehydrogenase isoenzyme-5 from human liver. Clin. Chem. 27 (1981) 88-93
53. Rytomaa M., and Kinnunen P.K.J. Reversibility of binding of cytochrome C to liposomes. J. B.C. 270 (1995) 3197-3202
54. Gutowicz J., and Kosmider-Schmidt A. Fluorescence investigation on conformational state of rabbit muscle aldolase interacting with phosphatidylinositol liposomes. Biophys. Chem. 27 (1987) 97-102
55. Michalak K., Gutowicz J., and Modrzycka T. Fluorescent probe studies on binding of glyceraldehyde-3-phosphate dehydrogenase to phosphatidylinositol liposomes. Further evidence for conformational changes. FEBS Lett. 219 (1987) 233-238
56. Kiltz H.H., Keil W., Griesbach M., Petry K., and Meyer H. The primary structure of porcine lactate dehydrogenase: isoenzymes M4 and H4. Hoppe-Seyler's Physiol. Chem. 358 (1977) 123-127
57. Burstein E.A., Vendenkina M.S., and Ivkova M.N. Fluorescence and the location of tryptophan residues in protein molecules. Photochem. Photobiol. 18 (1973) 263-279
58. Langner M., and Kubica K. The electrostatics of lipid surfaces. Chem. Phys. Lipids 101 (1999) 3-35
59. Verkleij A.J., Zwaal R.F., Roelofsen B., Comfurius P., Kastelijn D., and van Deenen L.L. The asymmetric distribution of phospholipids in the human red cell membrane. A combined study using phospholipases and freeze-etch electron microscopy. Biochim. Biophys. Acta 323 (1973) 178-193
60. Daum G. Lipids of mitochondria. Biochim. Biophys. Acta 822 (1985) 1-42
61. Hovius R., Lambrechts H., Nicolay K., and de Kruijff B. Improved methods to isolate and subfractionate rat liver mitochondria. Lipid composition of the inner and outer membrane. Biochim. Biophys. Acta 1021 (1990) 217-226
62. de Kroon A.I., Dolis D., Mayer A., Lill R., and de Kruijff B. Phospholipid composition of highly purified mitochondrial outer membranes of rat liver and Neurospora crassa. Is cardiolipin present in the mitochondrial outer membrane?. Biochim. Biophys. Acta 1325 (1997) 108-116
63. Hovius R., Thijssen J., van der Linden P., Nicolay K., and de Kruijff B. Phospholipid asymmetry of the outer membrane of rat liver mitochondria. Evidence for the presence of cardiolipin on the outside of the outer membrane. FEBS Lett. 330 (1993) 71-76