Abstract
Aldose reductase (EC 1.1.1.21) has been purified to apparent homogeneity from a variety of tissues including placenta, brain, nerves, kidney, muscle and lens. Multiple molecular forms of aldose reductase have been claimed to be isolated from bovine lens (Jedziniak et al, 1971) and bovine kidney (Gabbay et al 1974). These forms were subsequently described by some authors whereas others found a single form only (for a review see Wermuth, 1985). Conversion by a reducing agent (ß-mercaptoethanol) of one form to a more acidic but activity-retaining form was reported by Wermuth et al (1982), and differential susceptibility to inhibition of different enzyme forms was first described by Maragoudakis et al (1984). Nonlinear kinetics were often attributed to the presence of multiple forms. Thus, two kinetically distinct forms of human erythrocyte aldose reductase were postulated (Srivastava et al 1985) and the presence of bovine aldose reductase oxidized by oxygen radical generating systems was suggested as a possible cause for the nonlinear kinetics (Del Corso et al, 1987). More recently, data seem to firmly establish the existence of different forms of aldose reductase: “activated” and “unactivated” forms were isolated from bovine kidney (Grimshaw (1990) and their persistent peculiar kinetic behavior was then essentially rationalized (Grimshaw, 1991, Grimshaw et al 1990, Kubiseski et al, 1992). Recent advances in molecular biology led to the in vitro expression of rat lens aldose reductase (Old et al 1990) and human aldose reductase (Grundmann et al 1990, Carper et al 1990, Nishimura et al 1990, Bohren et al 1991). Multiple molecular forms of recombinant aldose reductase have so far not been reported with the exception of some charge heterogeneity that is evident upon isoelectric focusing (Bohren et al. 1991).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Bohren, K.M., Bullock, B., Wermuth, B., and Gabbay, K.H., 1989, The aldo-keto reductase superfamily, J. Biol. Chem. 264: 9547–9551
Bohren, K.M., Page, J.L., Shankar, R., Henry, S.P., and Gabbay, K.H., 1991, Expression of human aldose and aldehyde reductases: site-directed mutagenesis of a critical lysine262, J. Biol. Chem., 266: 24031–24037
Bohren, K.M., Page, J.L., Shankar, R., Henry, S.P., and Gabbay, K.H., 1991, Expression of human aldose and aldehyde reductases: site-directed mutagenesis of a critical lysine262, J. Biol. Chem., 266: 24031–24037
Bhatnagar, A., Liu, S., and Srivastava, S.K., 1989, Involvment of sulfhydryl residues in aldose reductase-inhibitor interaction, Mol. Pharmacol. 36: 825–830
Bhatnagar, A., Liu, S., Das, B., Ansari, N.H., and Srivastava, S.K., 1990, Inhibition kinetics of human kidney aldose reductase inhibitors, Biochem. Pharmacol. 30: 1115–1124
Carper, D., Sato S., Old, S., Chung, S. Kador, P.F. 1991, In vitro expression of human placental aldose reductase in Escherichia coli, Adv. Exp. Med. Biol. 284: 129–138
Del Corso, A., Camici, M., and Mura, U. 1987, In vitro modification of bovine aldose reductase activity, Biochem. Biophys. Res. Commun. 148: 369–375
Gabbay, K.H., and Cathcart, E.S., 1974, Purification and immunological identification of aldose reductase, Diabetes 23: 460–468
Gosh, S., Bock, S., Rokita, S., and Kaiser, E., 1986, Modification of the active site of alkaline phosphatase by site-directed mutagenesis, Science 231: 145–148
Grimshaw, C.E., 1990, Chromatographic separation of activated and unactivated forms of aldose reductase, Arch. Biochem. Biophys. 278: 273–276
Grimshaw, C.E., 1991, A kinetic perspective on the peculiarity of aldose reductase, Adv. Exp. Med. Biol. 284: 217–228
Grimshaw, C.E., Shahbaz, M., and Putney, C.G., 1990, Mechanistic basis for nonlinear kinetics of aldehyde reduction catalyzed by aldose reductase, Biochemistry 29: 9947–955
Grimshaw, C.E., Shahbaz, M., and Putney, C.G., 1990, Spectroscopic and kinetic characterization of nonenzymic and aldose reductase mediated covalent NADP-glycolaldehyde adduct formation, Biochemistry 29: 9936–9946
Grundmann, U., Bohn, H., Obermeier, R., and Amann E., 1990, Cloning and prokaryotic expression of a biologically active human placental aldose reductase, DM4. Cell. Biol. 9: 149–157
He, J.J., Quiocho, A., 1991, A nonconservative Serine to Cysteine mutation in the sulfate-binding protein, a transport receptor, Science, 251: 1479–1481
Jedziniak, J.A., and Kinoshita, J.H., 1971, Activators and inhibitors of of lens aldose reductase, Invest. Ophtalmol. 10: 357–366
Kubiseski, T.J, Hyndman, D.J., Morjana, N.A, and Flynn, T.G. 1992, Studies on pig muscle aldose reductase — kinetic mechanism and evidence for slow conformational change upon coenzyme binding, J. Biol. Chem. 267: 6510–6517
Maragoudakis, M.E., Wasvary, J., Hankin, H. and Gargiuolo, P., 1984, Human placenta aldose reductase: forms sensitive and insensitive to inhibition by Alrestatin, Mol. Pharmacol. 25: 425
Nishimura, C., Matsuura Y., Kokai Y., Akera, T., Carper, D., Morjana., N., Lyons, C., and Flynn, T. G., 1990, Cloning and expression of human aldose reductase, J. Biol. Chem. 265: 9788–9792
Old, S.E., Sato, S. Kador, P.F., and Carper, D.A., 1990, In vitro expression of rat lens aldose reductase in E.coli, Proc. Natl Acad. Sci. USA. 87: 4942–4955
Rondeau, J.-M, Tête-Favier, F., Podjarny, A., Reyman. J.-M., Barth, P., Biellmann, J.-F. and Moras, D., 1992, Novel NADPH-binding domain revealed by the crystal structure of aldose reductase, Nature 355: 469–472
Rose, I.A., Hanson, K., Wilkinson, K.D., Wimmer, M.J., 1980, A suggestion for naming faces of ring compounds, Proc. Natl. Acad. Sci. USA, 77: 2439–2441
Smithies, O., 1965, Disulfide-bond cleavage and formation in proteins, Science 150: 1595–1598
Srivastava, S.K., Hair, G.A., and Das, B., 1985, Activated and unactivated forms of human erythrocyte aldose reductase, Proc. Natl. Acad. Sci. USA 82: 7222–78226
Wermuth, B., 1985, Aldo-keto reductases, in “Enzymology of Carbonyl Metabolism 2: Aldehyde Dehydrogenase, Aldo-Keto Reductase, and Alcohol Dehydrogenase”, Flynn, T.G. and Weiner, H., eds., Alan R.Liss Inc., New York., 209–230
Wermuth, B. Bürgisser, H., Bohren, K.M., and von Wartburg, J.-P., 1982, Purification and characterization of human brain aldose reductase, Eur. J. Biochem. 127: 279–284
Wilson, D.K., Bohren, K.M., Gabbay, K.H., and Quiocho, F.A., 1992, An unlikely sugar substrate site in the 1.65 Å structure of the human aldose reductase holoenzyme implicated in diabetic complications, Science 257: 81–84
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1993 Springer Science+Business Media New York
About this chapter
Cite this chapter
Bohren, K.M., Gabbay, K.H. (1993). CYS298 is Responsible for Reversible Thiol-Induced Variation in Aldose Reductase Activity. In: Weiner, H., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 4. Advances in Experimental Medicine and Biology, vol 328. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2904-0_29
Download citation
DOI: https://doi.org/10.1007/978-1-4615-2904-0_29
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-6259-3
Online ISBN: 978-1-4615-2904-0
eBook Packages: Springer Book Archive