1,134
Views
16
CrossRef citations to date
0
Altmetric
Research Article

Inhibition of human muscle-specific enolase by methylglyoxal and irreversible formation of advanced glycation end products

, , &
Pages 356-364 | Received 15 Jan 2007, Accepted 29 Apr 2008, Published online: 01 Apr 2009

References

  • F Wold. Enolase. In: PD Boyer, editor. The enzymes. 3rd ed. New York: Academic Press; (1971). p 499–538.
  • L Lebioda, and B Stec. (1991). Mechanism of enolase-Mg2+-2-phosphoglycerate/phosphoenolpyruvate complex at 2Å resolution. Biochemistry 30:2817–2822.
  • M Nozais, T Merkulova, A Keller, Ch Janmot, AM Lompre, A D'Albis, and M Lucas. (1999). Denervation of rabbit gastrocnemius and soleus muscles. Effect on muscle-specific enolase. Eur J Biochem 263:195–201.
  • P Ulrich, and A Cerami. (2001). Protein glycation, diabetes and aging. Recent Prog Horm Res 56:1–21.
  • R Singh, A Barden, T Mori, and L Beilin. (2001). Advanced glycation end-products. Diabetologia 44:129–146.
  • R GhoshMoulick, J Bhattacharya, S Roy, S Basak, and AJ Dasgupta. (2007). Compensatory secondary structure alterations in protein glycation. Biochim Biophys Acta 1774:233–242.
  • TJ Sims, LM Rasmussen, H Oxlund, and AJ Bailey. (1996). The role of glycation cross-links in diabetes vascular stiffening. Diabetologia 39:946–951.
  • Z Turk, S Ljubic, N Turk, and B Benko. (2001). Detection of autoantibodies against glycation endproducts and AGE-immune complexes in serum of patients with diabetes mellitus. Clin Chim Acta 303:105–115.
  • R Chibber, PA Molinatti, N Rosatto, B Lambourne, and EM Kohner. (1997). Toxic action of advanced glycation end products on cultured retinal capillary pericytes and endothelial cells: Revelance to diabetic retinopathy. Diabetologia 40:156–164.
  • D Suzuki, T Miyata, N Saotome, K Horie, R Inagi, Y Yasuda, K Uschida, Y Izuchara, M Yagame, M Sakai, and K Kurokawa. (1999). Immunohistochemical evidence for increased oxidative stress and carbonyl modification of proteins in diabetic glomerular lesions. J Am Soc Nephrol 10:822–832.
  • AS Duhaiman. (1995). Glycation of human lens proteins from diabetic and nondiabetic senile cataract patients. Glycoconj J 12:618–621.
  • Y Aso, T Inukai, K Tayama, and Y Takemura. (2000). Serum concentrations of advanced glycation end products are associated with development of atherosclerosis as well as diabetic microangiopathy in patients with type 2 diabetes. Acta Diabetol 37:87–92.
  • R Gomes, M Sousa Silva, A Quintas, C Cordeiro, A Freire, P Pereira, A Martins, E Monteiro, E Barroso, and A Ponces-Freire. (2005). Argpyrimidine, a methylglyoxal-derived advanced glycation end product in a familial amyloidic polyneuropathy. Biochem J 385:339–345.
  • C Loske, A Gerdemann, W Schelp, M Wycislo, R Schnizel, D Palm, P Riederer, and G Munch. (2000). Transition metal-mediated glycoxidation accelerates cross-linking of β-amyloid peptide. Eur J Biochem 267:4171–4178.
  • PJ Thornalley. (2005). Dicarbonyl intermediates in the Maillard reaction. Ann N Y Acad Sci 1043:111–117.
  • SA Philips, and PJ Thornalley. (1993). The formation of methylglyoxal from triose phosphates. Investigation using a specific assay for methylglyoxal. Eur J Biochem 212:101–105.
  • JR Knowles. (1991). Enzyme catalysis: Not different, just better. Nature 350:121–124.
  • N Ahmed, S Battah, N Karachalias, R Babaei-Jadidi, M Horanyi, K Baroti, S Hollan, and PJ Thornalley. (2003). Increased formation of methylglyoxal and protein glycation, oxidation and nitrosation in triosephosphate deficiency. Biochim Biophys Acta 1639:121–132.
  • PJ Beisswenger, SK Howell, K Smith, and BS Szwergold. (2003). Glyceraldehyde 3-phosphate dehydrogenase activity as an independent modifier of methylglyoxal levels in diabetes. Biochim Biophys Acta 1637:98–105.
  • PJ Thornalley, A Langborg, and H Minhas. (1999). Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem J 344:109–116.
  • PJ Thornalley. (1993). Pharmacology of methylglyoxal: Formation, modification of proteins and nucleic acids and enzymatic detoxification—a role in pathogenesis and antiproliferative chemotherapy. Gen Pharmacol 27:565–573.
  • M Ray, and S Ray. (1987). Aminoacetone oxidase from goat liver. Formation of methylglyoxal from aminoacetone. J Biol Chem 262:5974–5977.
  • PJ Thornalley. (2003). Glyoxalase I—structure, function and critical role in the enzymatic defense against glycation. Biochem Soc Trans 31:1343–1348.
  • BS Szwergold, and PJ Beisswenger. (2003). Enzymatic deglycation—a new paradigm or an phenomenon?. Biochem Soc Trans 31:1428–1432.
  • K Takahashi. (1968). The reaction of phenylglyoxal with arginine residues in proteins. J Biol Chem 243:6171–6179.
  • NW Seidler, and C Kowalewski. (2003). Methylglyoxal-induced glycation affects protein topography. Arch Biochem Biophys 410:149–154.
  • JH Kang. (2003). Modification and inactivation of human Cu,Zn-superoxide dismutase by methylglyoxal. Mol Cells 15:194–199.
  • J Halder, M Ray, and S Ray. (1993). Inhibition of glycolysis and mitochondrial respiration of Ehrlich ascites carcinoma cells by methylglyoxal. Int J Cancer 54:443–449.
  • S Biswas, M Ray, S Misra, DP Dutta, and S Ray. (1997). Selective inhibition of mitochondrial respiration and glycolysis in human leukaemic leucocytes by methylglyoxal. Biochem J 323:343–348.
  • HJ Lee, SK Howell, RJ Sanford, and PJ Beisswenger. (2005). Methylglyoxal can modify GAPDH activity and structure. Ann N Y Acad Sci 1043:135–145.
  • PE Morgan, RT Dean, and MJ Davies. (2002). Inactivation of cellular enzymes by carbonyl and protein-bound glycation/glycoxidation products. Arch Biochem Biophys 403:259–269.
  • RA Gomes, HV Miranda, MS Silva, G Graca, AV Coelho, AE Ferreira, C Cordeiro, and AP Freire. (2006). Yeast protein glycation in vivo by methylglyoxal. Molecular modification of glycolytic enzymes and heat shock proteins. FEBS J 273:5273–5287.
  • D Witkowska, J Pietkiewicz, B Szostko, R Danielewicz, L Masłowski, and A Gamian. (2005). Antibodies against human muscle enolase recognize a 45-kDa bacterial cell wall outer membrane enolase-like protein. FEMS Immunol Med Microbiol 45:53–62.
  • F Wold, and E Ballou. (1957). Studies on the enzyme enolase. I. Equilibrium studies. J Biol Chem 227:301–312.
  • T Baranowski, and E Wolna. Enolase from human muscle In: SP Colowick, and NO Kaplan, editors. Methods in enzymology., Vol. XLII, New York: Academic Press; (1975). p 335–338.
  • K Laemmli. (1977). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685.
  • J Pietkiewicz, I Kustrzeba-Wójcicka, E Wolna, and M Wolny. (1983). Purification and properties of enolase from carp (Cyprinus carpio) muscle. Comparison with enolases from mammals muscles and yeast. Comp Biochem Physiol 75B:693–698.
  • H Lineweaver, and D Burk. (1934). The determination of enzyme dissociation constants. J Am Chem Soc 56:658–666.
  • TW Lo, ME Westwood, AC Mc Lellan, T Selwood, and PJ Thornalley. (1994). Binding and modification of proteins by methylglyoxal under physiological conditions. J Biol Chem 269:32299–32305.
  • AM Martins, CA Cordeiro, and AMJ Ponces Freire. (2001). In situ analysis of methylglyoxal metabolism in Saccharomyces cerevisiae. FEBS Lett 499:41–44.
  • G Munch, D Schicktanz, A Behme, M Gerlach, P Riederer, D Palm, and R Schinzel. (1999). Amino acid specifity of glycation and protein-AGE crosslinking reactivities determined with SPOT library. Nat Biotechnol 17:1006–1010.
  • SC Wilker, P Chellan, BM Arnold, and RH Nagaraj. (2001). Chromatographic quantification of argpyrimidine, a methylglyoxal-derived product in tissue proteins: Comparison with pentosidine. Anal Biochem 290:353–358.
  • J Pietkiewicz, I Kustrzeba-Wójcicka, E Wolna, and M Wolny. (1987). Chemical modification of histidine, tyrosine, tryptophan and cysteine residues in carp (Cyprinus carpio) muscle enolase. Biochem Inter 14:805–814.
  • J Pietkiewicz, and M Wolny. (1991). Inactivation of enolase from carp (Cyprinus carpio) muscle by 2,3-butanedione. Biochem Inter 23:69–74.
  • RR Poyner, WW Cleland, and GH Reed. (2001). Role of metal ions in catalysis by enolase: An ordered kinetic mechanism for a single substrate enzyme. Biochemistry 4:8009–8017.
  • G Chai, JM Brewer, LL Lovelace, T Aoki, V Minor, and L Lebioda. (2004). Expression, purification and the 1,8 Å resolution crystal structure of human neuron specific enolase. J Mol Biol 341:1015–1021.
  • V Pancholi. (2001). Multifunctional alpha-enolase: Its role in diseases. Cell Mol Life Sci 58:902–920.
  • MU Ahmed, SR Thorpe, and JW Baynes. (1986). Identification of N-carboxymethyllysine as a degradation product of fructoselysine in glycated protein. J Biol Chem 261:4889–4894.
  • NG Watkins, CJ Neglia-Fisher, DG Dyer, SR Thorpe, and JW Baynes. (1987). Effect of phosphate on kinetics and specificity of glycation of protein. J Biol Chem 262:7207–7212.
  • GH Reed, RR Poyner, TM Larsen, JE Wedekind, and I Rayment. (1996). Structural and mechanistic studies of enolase. Curr Opin Struct Biol 6:736–743.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.