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2003 | 08 | 3 |
Tytuł artykułu

The association of glycolytic enzymes with cellular and model membranes

Warianty tytułu
Języki publikacji
This article deals with the binding of glycolytic enzymes with membranous or protein subcellular structures. The representative papers of the last three decades dealing with this matter are reviewed. The studies evidencing the binding of some glycolytic enzymes to insoluble subcellular proteins and membranous structures are presented. It is currently generally accepted that the glycolytic enzymes work in some organisation. Such organisation undoubtedly plays a marked role, although still poorly known, in the regulation processes of glycolysis. From this review, the conclusion emerges that the regulatory ability of the binding of glycolytic enzymes to cellular membranes should be added to the list of well-known mechanisms of post-translational regulation of the glycolytic enzymes. Some of the results presented are the background for the hypothesis that planar phospholipid domains in/on the membrane surface are capable of functioning as binding sites for these enzymes. Such binding can modify the conformation state of the enzymes, which results in changes in their kinetic properties; thus, it may function as a regulator of catalytic activity.
Opis fizyczny
  • Wroclaw University, Wroclaw, Poland
  • 1.Green, D.E., Murer, E., Hultin, H.O., Richardson, S.H., Salmon, B., Brierley, G.P. and Baum, H. Association of integrated metabolic pathways with membranes. I. Glycolytic enzymes of the red blood corpuscle and yeast. Arch. Biochem. Biophys. 112 (1965) 635-647.
  • 2.Arnold, H. and Pette, D. Binding of glycolytic enzymes to structure proteins of the muscle. Eur. J. Biochem. 6 (1968) 163-171.
  • 3.Arnold, H. and Pette, D. Binding of aldolase and triosephosphate dehydrogenase to F-actin and modification of catalytic properties of aldolase. Eur. J. Biochem. 15 (1970) 360-366.
  • 4.Clarke, F.M. and Masters, C.J. On the reversible and selective adsorption of aldolase isoenzymes in rat brain. Arch. Biochem. Biophys. 153 (1972) 258-265.
  • 5.Tamir, H., Kaufman, H. and Rapport, M.M. Subcellular distribution of pyruvate kinase (EC in cerebral cortex. J. Neurochem. 19 (1972) 1759-1768.
  • 6.Craven, P.A. and Basford, R.E. ADP-induced binding of phosphofructokinase to the brain mitochondrial membrane. Biochim. Biophys. Acta 354 (1974) 49-56.
  • 7.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.
  • 8.Keleti, T. and Ovadi, J. Control of metabolism by dynamic macromolecular interactions. Curr. Top. Cell Regul. 29 (1988) 1-33.
  • 9.Ovadi, J., Batke, J., Bartha, F. and Keleti, T. Effect of association- dissociation on the catalytic properties of glyceraldehyde 3-phosphate dehydrogenase. Arch. Biochem. Biophys. 193 (1979) 28-33.
  • 10.Brooks, S.P. and Storey, K.B. Reevaluation of the "glycolytic complex" in muscle: A multitechnique approach using trout white muscle. Arch. Biochem. Biophys. 267 (1988) 13-22.
  • 11.Wilson, J.E. and Felgner, P.L. An inverse relation between mitochondrial hexokinase content and phosphoglucomutase activity of rat tissues. Mol. Cell. Biochem. 18 (1977) 9-47.
  • 12.Salotra, P.T. and Singh, V.N. Regulation of glucose metabolism in rat lung: Subcellular distribution, isozyme pattern, and kinetic properties of hexokinase. Arch. Biochem. Biophys. 216 (1982) 758-764.
  • 13.Kurokawa, M., Oda, S., Tsubotani, E., Fujiwara, H., Yokoyama, K. and Ishibashi, S. Characterization of hexokinase isoenzyme types I and II in ascites tumor cells by an interaction with mitochondrial membrane. Mol. Cell. Biochem. 5 (1982) 151-157.
  • 14.Radojkovic, J. and Ureta, T. Hexokinase isoenzymes from the Novikoff hepatoma. Purification, kinetic and structural characterization, with emphasis on hexokinase C. Biochem. J. 242 (1987) 895-903.
  • 15.Preller, A. and Wilson, J.E. Localization of the type III isozyme of hexokinase at the nuclear periphery. Arch. Biochem. Biophys. 294 (1992) 482-492.
  • 16.Wilson, J.E. The localization of latent brain hexokinase on synaptosomal mitochondria. Arch. Biochem. Biophys. 150 (1972) 96-104.
  • 17.Sagrista, M.L. and Bozal, J. Lactate and malate dehydrogenase binding to the mitochondrial fraction from chicken liver. Biochimie 69 (1987) 1207-1215.
  • 18.Sanz, M.C. and Lluis, C. Ambiquitous behavior of rabbit liver lactate dehydrogenase. Experientia 44 (1988) 203-208.
  • 19.Karadseh, N.S. and Uyeda, K. Changes in allosteric properties of phosphophructikinase bound to erythrocyte membranes. J. Biol. Chem. 252 (1977) 7418-7420.
  • 20.Higashi T., Richards C.S. and Uyeda K. The interaction of phosphofructokinase with erythorcyte membranes J. Biol. Chem. 254 (1979) 9542-9550.
  • 21.Jenkins, J.D., Kezdy, F.J. and Steck, T.L. Mode of interaction of phosphofructokinase with the erythorocyte membranes J. Biol. Chem. 260 (1985) 10426-10433.
  • 22.Liou, R.S. and Anderson, S. Activation of rabbit muscle phosphofructokinase by F-actin and reconstituted thin filaments. Biochemistry 19 (1980) 2684-2688.
  • 23.Mayr, G.W. and Heilmeyer, L.M. Jr. Phosphofructokinase is a calmodulin binding protein. FEBS Lett. 159 (1983) 51-57.
  • 24.Sherer, P.E. and Lisanti, M.P. Association of phosphofructokinase-M with caveolin-3 in differentiated skeletal myotubes. Dynamic regulation by extracellular glucose and intracellular metabolites. J. Biol. Chem. 272 (1997) 20698-20705.
  • 25.Okamoto, T., Schlegel, A., Scherer, P. and Lisanti, M.P. Caveolins, a family of scaffolding proteins for organizing 'preassembled signaling complexes' at the plasma membrane. J. Biol. Chem. 273 (1998) 5419-5422.
  • 26.Liu, P., Rudick, M. and Andersen, R.G.W. Multiple functions of caveolin-1. J. Biol. Chem. 277 (2002) 41295-41298.
  • 27.Clarke, F.M. and Masters, C.J. Letter: Multi-enzyme aggregates: New evidence for an association of glycolytic components. Biochim. Biophys. Acta 327 (1973) 223-226.
  • 28.Clarke, F.M. and Masters, C.J. On the reversible adsorption of aldolase to a microsomal membrane fraction from rat brain. Int. J. Biochem. 6 (1975) 133-145.
  • 29.Clarke, F.M., Masters, C.J. and Winzor, D.J. Interaction of aldolase with the troponin-tropomyosin complex of beef muscle. Biochem. J. 139 (1974) 785-788.
  • 30.Strapazon, E. and Steck, T.L. Interaction of the aldolase and the membrane of human erythrocytes. Biochemistry 16 (1977) 2966-2971.
  • 31.Yeltman, D.R. and Harris, B.G. Localization and membrane association of aldolase in human erythrocytes. Arch. Biochem. Biophys. 199 (1980) 186-196.
  • 32.Lu, M., Holliday, L.S., Zhang, L., Dunn, W.A. Jr and Gluck, S.L. Interaction between aldolase and vacuolar H+-ATPase: Evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump. J. Biol. Chem. 276 (2001) 30407-30413.
  • 33.Shin, B.C. and Carraway, K.L. Association of glyceraldehyde 3-phosphate dehydrogenase with the human erythrocyte membrane. Effect of detergents, trypsin, and adenosine triphosphate. J. Biol. Chem. 248 (1973) 1436-1444.
  • 34.Melnick, R.L. and Hultin, H.O. Studies on the nature of the subcellular localization of lactate dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase in chicken skeletal muscle. J. Cell Physiol. 81 (1973) 139-147.
  • 35.Wu, K., Aoki, C., Elste, A., Rogalski-Wilk, A.A. and Siekevitz, P. The syntesis of ATP by glycolytic enzymes in the postsynaptic density and the effect of endogenously generated nitric oxide. Proc. Natl. Acad. Sci. USA 94 (1997) 13273-13278.
  • 36.Wrigglesworth, J.M., Keokitichai, S., Wooster, M.S and Millar, FA. Modification of glyceraldehyde 3-phosphate dehydrogenase activity by adsorption to erythrocyte membranes and phospholipid vesicles. Biochem. Soc. Trans. 4 (1976) 637-640.
  • 37.Cseke, E., Varadi, A., Szabolcsi, G. and Biszku, E. On the molecular sieving property of the human erythrocyte membrane and the localization of some glycolytic enzymes in the cell. FEBS Lett. 96 (1978) 15-18.
  • 38.Solti, M., Bartha, F., Halasz, N., Toth, G., Sirokman, F. and Friedrich, P. Localization of glyceraldehyde-3-phosphate dehydrogenase in intact human erythrocytes. Evaluation of membrane adherence is autoradiographs at low grain density. J. Biol. Chem. 256 (1981) 9260-9265.
  • 39.De, B.K. and Kirtley, M.E. Interaction of phosphoglycerate kinase with human erythrocyte membranes. J. Biol Chem. 252 (1977) 6715-6720.
  • 40.Ratner, J.H., Nitesewojo, P., Hirvay, S. and Hultin, H.O. A study of some factors involved in the interaction between lactate dehydrogenase isozymes and particulate fractions of muscle. Int. J. Biochem. 5 (1974) 525-533.
  • 41.Ross, R.E and Hultin, H.O. A study of binding-solubilization of some glycolytic enzymes in striated muscle in situ. J. Cell Physiol. 105 (1980) 409-416.
  • 42.Lluis, C. Lactate dehydrogenase associated with mitochondrial fraction. Int. J. Biochem. 16 (1984) 997-1004.
  • 43.Nitisewojo, P. and Hultin, H.O. A comparison of some kinetic properties of soluble and bound lactate dehydrogenase isozymes at different temperatures. Eur. J. Biochem. 67 (1976) 87-94.
  • 44.Knull, H.R. Compartmentation of glycolytic enzymes nerve endings as determined by glutaralaldehyde fixation. J. Biol. Chem. 255 (1980) 6439-6444
  • 45.Knull, H.R., Bronstein, W.W., DesJardins, P. and Niehaus, W.G. Jr. Interaction of selected brain glycolytic enzymes with an F-actin-tropomyosin complex. J. Neurochem. 34 (1980) 222-225.
  • 46.Sanz, M.C, Sagrista, L. and Lluis, C. Kinetic behaviour of soluble and mitochondrial bound lactate dehydrogenase. Italian J. Biochem. 39 (1990) 21-29.
  • 47.Lluis, C. Lactate dehydrogenase binding to the mitochondrial inhibitor as a function of isozymatic composition. Int. J. Biochem. 17 (1985) 1219-1226.
  • 48.Kline, E.S., Brandt, R.B., Laux, J.E., Spainhour, S.E., Higgins, E.S., Roger, K.S., Tinsley, S.B. and Water, M.G. Localization of L-lactate dehydrogenase in mitochondria. Arch. Biochem. Biophys. 246 (1986) 673-680.
  • 49.Wilson, J.E. The relationship giycolytic and mitochondrial enzymes in the developing rat brain. J. Neurochem. 19 (1972) 223-227.
  • 50.Mattisson, A.G., Johansson, R.G. and Bostrom, S.L. The cellular localization of lactate dehydrogenase in skeletal muscle of eel (Anguilla anguilla). Comp. Biochem. Physiol. B. 41 (1972) 475-482.
  • 51.Hsu, S.C. and Molday, R.S. Glyceraldehyde-3-phosphate dehydrogenase is a major protein associated with the plasma membrane of retinal photoreceptor outer segments. J. Biol. Chem. 265 (1990) 13308-13313.
  • 52.Hsu, S.C. and Molday, R.S. Glycolytic enzymes and GLUT-1 glucose transporter in the outer segments of rod and cone photoreceptor cells. J. Biol. Chem. 266 (1991) 21745-21752.
  • 53.Keller, A., Demeurie, J., Merkulova, T., Geraud, G., Cywiner-Glenzer, C., Lucas, M. and Chatelet, F.-P. Fibre-type distribution and subcellular localisation of α and β enolase in mouse striated muscle. Biol. Cell 92 (2000) 527-535.
  • 54.Polakis, P.G. and Wilson, J.E. An intact hydrophobic N-terminal sequence is critical for binding of rat brain hexokinase to mitochondria. Arch. Biochem. Biophys. 236 (1985) 328-337.
  • 55.Xie, G.C. and Wilson, J.E. Rat brain hexokinase: The hydrophobic N-terminus of the mitochondrially bound enzyme is inserted in the lipid bilayer. Arch. Biochem. Biophys. 267 (1988) 803-810.
  • 56.Dąbrowska, A., Gutowicz, J. and Terlecki, G. Adsorption of bovine muscle lactate dehydrogenase to erythrocyte membranes. Gen. Physiol. Biophys. 9 (1990) 529-534.
  • 57.Yu, J. and Steck, T.L. Association of Band 3, the predominant polypeptide of the human erythrocyte membrane. J. Biol. Chem. 250 (1975) 9176-9184.
  • 58.Cabantchik, Z.I., Knauf, P.A. and Rothstein, A. The anion transport system of the red blood cell. The role of membrane protein evaluated by the use of 'probes'. Biochim. Biophys. Acta. 515 (1978) 239-302.
  • 59.Gutowicz, J. and Modrzycka, T. Interaction of rabbit muscle aldolase with phospholipid liposomes. Biochim. Biophys. Acta 554 (1979) 358-363.
  • 60.Langner, M., Gutowicz, J. and Gomułkiewicz, J. Modification of some properties of spherical lipid membranes induced by the association with fructose-1,6-bisphosphate aldolase. FEBS Letters 196 (1986) 251-254.
  • 61.Gutowicz, J. and Kośmider-Schmidt, A. Fluorescence investigation on conformational state of rabbit muscle aldolase interacting with phospholipid liposomes. Biophys. Chem. 27 (1987) 97-102.
  • 62.Sytnik, A.I., Chumachenko, I.V., Volovik, Z.N. and Demchenko, A.P. Interaction of aldolase A with lecithin liposomes. Ukr. Biokhim. Zh. 60 (1988) 66-72.
  • 63.Wooster, M.S. and Wrigglesworth, J.M. Adsorption of glyceraldehyde 3-phosphate dehydrogenase on condensed monolayers of phospholipid. Biochem. J. 153 (1976) 93-100.
  • 64.Wooster, M.S. and Wrigglesworth, J.M. Modification of glyceraldehyde 3-phosphate dehydrogenase activity by adsorption on phospholipid vesicles. Biochem. J. 159 (1976) 627-31.
  • 65.Gutowicz, J. and Modrzycka, T. Binding of glyceraldehyde-3-phospate dehydrogenase to phospholipid liposomes. Biochim. Biophys. Acta 512 (1978) 105-110.
  • 66.Gutowicz, J. and Modrzycka, T. Liposome-induced conformation changes of glyceraldehyde-3-phosphate dehydrogenase. Gen. Physiol. Biophys. 5 (1986) 297-306.
  • 67.Michalak, K., Gutowicz, J. and Modrzycka, T. Temperature studies of binding of glyceraldehyde-3-phosphate dehydrogenase to liposomes with fluorescence technique. Gen. Physiol. Biophys. 11 (1992) 545-554.
  • 68.Dąbrowska, A. and Gutowicz, J. Interaction of bovine heart lactate dehydrogenase with erythrocyte lipids. Biochim. Biophys. Acta 855 (1986) 99-104.
  • 69.Dąbrowska, 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.
  • 70.Dąbrowska, A., Terlecki, G., Czapińska, E. and Gutowicz, J. Interaction of bovine heart pyruvate kinase with phosphoplipids. Biochim. Biophys. Acta 1236 (1995) 299-305.
  • 71.Sato, T.K., Overduin, M. and Emr, S.D. Location, location, location: Membrane targeting directed by PX domains. Science 294 (2001) 1881-1885.
  • 72.Maffucci, T. and Falasca, M. Specificity in pleckstrin homology (PH) domain membrane targeting: A role for phosphoinositide-protein cooperative mechanism. FEBS Letters 506 (2001) 173-179.
  • 73.Haslam, R.J., Koide, H.B. and Hemmings, B.A. Pleckstrin domain homology. Nature 363 (1993) 309-310.
  • 74.Kim, J.H., Lee, S., Kim, J.H., Lee, T.G., Hirata, M., Suh, P.-G. and Ryu, S.H. Phospholipase D2 directly interacts with aldolase via its PH domain. Biochemistry 41 (2002) 3414-3421.
  • 75.Terlecki, G., Czapińska, 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.
  • 76.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.
  • 77.Marmillot, P., Keith, T., Srivastava, D.K. and Knull, H.R. Effect of tubulin on the activity of the muscle isoenzyme of lactate dehydrogenase. Arch. Biochem. Biophys. 315 (1994) 467-472.
  • 78.Don, M. and Masters, C. Chemical modification of the actin binding site of rabbit muscle aldolase by diethylpyrocarbonate. Mol. Cell Biochem. 81 (1988) 145-153.
  • 79.Kelley, G.E. and Winzor, D.J. Quantitative characterization of the interactions of aldolase and glyceraldehyde-3-phosphate dehydrogenase with erythrocyte membranes. Biochim. Biophys. Acta 778 (1984) 67-73.
  • 80.Salhany, J.M. and Gaines, K.C. Connections between cytoplasmic proteins and the erythrocyte membrane. Trends Biochem. Sci. 6 (1981) 13-15.
  • 81.Michalak, K., Gutowicz, J. and Modrzycka, T. Fluorescence probe studies on binding of glyceraldehyde-3-phosphate dehydrogenase to phosphatidylinositol liposomes. Further evidence for conformational changes. FEBS Lett. 219 (1987) 233-238.
  • 82.Michalak, K. Gutowicz, J. and Modrzycka, T. Temperature studies of binding of glyceraldehyde-3-phosphate dehydrogenase to liposomes using fluorescence technique. Gen. Physiol. Biophys. 11 (1992) 545-554.
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