Abstract
Aldehyde dehydrogenases (ALDHs) are now recognised as a complex gene family., which includes a group of NAD-dependent ALDH (EC 1.2.1.3) isozymes. Seven human ALDHs have been reported, of which ALDH1, 2, 3, 5, 6, and 7 (Hsu et al, 1994), and a related enzyme, γ-amino butyraldehyde dehydrogenase (GABADH) (Kurys et al, 1993), have been thus far cloned and sequenced (Hsu et al., 1994). Sequence analysis verifies that these are closely related enzymes, and optimised alignments show that 62 amino acids are conserved, including the catalytically significant Gly-245, Gly-250, Glu-268 and Cys-302 (Hsu et al., 1994). Human ALDHs 1, 2 and 3 have been further classified according to their genetic identity as Class 1(ALDH1, liver cytosolic), Class 2 (ALDH2, liver mitochondrial) and Class 3(ALDH3, stomach cytosolic) isozymes. In addition, a gene locus designated ALDHx, which shares 85% homology with Class 2 ALDH, has also been reported (Hsu and Chang, 1991).
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References
Abedinia, M., Pain, T., Algar, E.M. and Holmes, R.S.: Bovine corneal aldehyde dehydrogenase: the major soluble corneal protein with a possible dual protective role for the eye. Exp. Eye Res. 51 (1990) 419–426.
Alexander, R.J., Silverman, B. and Henley, W.L.: Isolation and characterization of BCP54 the major soluble protein of bovine cornea. Exp. Eye Res. 32 (1981) 205–216.
Algar, E.M. and Holmes, R.S.: Kinetic properties of murine liver aldehyde dehydrogenases. In Weiner, H. and Flynn, T.G. (Eds.), Enzymology and Molecular Biology of Carbonyl Metabolism 2. Alan R. Liss, N.Y., 1989 pp>93–103.
Ambroziak, W. and Pietruszko, R.: Human aldehyde dehydrogenase activity with aldehyde metabolites of monoamine, diamines and polyamines. J. Biol. Chem. 266 (1991) 13011–13018.
Ames, G.F.-I.: Resolution of bacterial proteins by Polyacrylamide gel electrophoresis on slabs. J. Biol. Chem. 249 (1974)634–644.
Boesch, J.S., Lee, C. and Lindahl, R.G.: Constitutive expression of class 3 aldehyde dehydrogenase in cultured rat epithelium. J. Biol. Chem. 271 (1996) 5150–5157.
Boettner E.A. and Wolters J.R.: Transmittance of the ocular media. Invest. Ophthalmol. 1 (1962) 776–783.
Cooper, D.L., Bapist, E.W., Enghild, J., Lee, H., Isola, N. and Klintworth, G. K.: Bovine corneal protein 54K (BCP54) is a homologue of the tumour-associated (Class 3) rat aldehyde dehydrogenase (RATALD). Gene 98 (1991) 201–207.
Cooper D.L., Isola N.R., Stevenson K. and Baptist E.W.: Members of the ALDH gene family are lens and corneal crystallins. In Weiner, H., Crabb, D.W., and Flynn, G.F. (Eds.), Enzymology and Molecular Biology of Carbonyl Metabolism 4. Plenum Press, New York, 1993, pp 169–179.
Crabbe, M.J.C. and Hoe, S.T.: Aldehdye dehydrogenase, aldose reductase and free radical scavengers in cataract. Enzyme 45 (1991) 188–193
Dockham, P.A., Lee, M.-O. and Sladek, N.E.: Identification of human liver aldehyde dehydrogenases that catalyse the oxidation of aldophosphamide and retinaldehyde. Biochem. Pharmacol. 43 (1992) 2453–2469.
Evces, S. and Lindahl, R.: Characterisation of rat cornea aldehyde dehydrogenase. Arch. Biochem. Biophys. 274 (1989) 518–529.
Feldman, R.I. and Weiner, H.: Horse liver aldehyde dehydrogenase 1. Purification and characterization. J. Biol. Chem. 247 (1972) 260–266.
Gondhowiardjo, T.D., van Haeringen, N.J., Hoekzema, R., Pels, L., and Kijlstra, A.: Detection of aldehyde dehydrogenase activity in human corneal extracts. Current Eye Research 10 (1991) 1001–1007.
Greenfield, N.J. and Pietruszko, R.: Two aldehyde dehydrogenases from human liver isolation via affinity chromatography and characterization of the isozymes. Biochim. Biophys. Acta 483 (1977) 35–45.
Hempel J.D., Reed, D.N. and Pietruszko, R.: Human aldehyde dehydrogenase: improved purification procedure and comparison of homogeneous isoenzymes E1 and E2. Alcoholism: Clinical and Experimental Research 6 (1982) 417–425.
Holmes, R.S. and VandeBerg, J.L.: Ocular NAD-dependent alcohol dehydrogenase and aldehyde dehydrogenase in the baboon. Exp. Eye Res. 43 (1986) 383–396.
Holmes, R.S.: Alcohol dehydrogenases and aldehyde dehydrogenases of anterior eye tissues from humans and other mammals. In Kuriyama, K., Takada, A. and Ishii, H. (Eds.), Biomedical and Social Aspects of Alcohol and Alcoholism. Elsevier Science Publishers, Amsterdam (1988), pp 51–57.
Holmes, R.S., Cheung, B., and Vandeberg, J.L.: Isoelectric focusing studies of aldehyde dehydrogenases, alcohol dehydrogenases and oxidases from mammalian anterior eye tissues. Comp. Biochem. Physiol. 93B (1989). 271–277.
Hsu, L.C. and Chang, W-C.: Cloning and characterization of a new functional aldehyde dehydrogenase gene. J. Biol. Chem. 266, (1991) 12257–12265.
Hsu L.C., Chang W.-C. and Yoshida A.: Cloning of a cDNA encoding human ALDH7, a new member of the aldehyde dehydrogenase family. Gene 151 (1994) 285–289.
Jones, D.E., Brennan, M.D., Hempel, J. and Lindahl, R.: Cloning and complete nucleotide sequence of a full-length cDNA encoding a catalytically functional tumour-associated aldehyde dehydrogenase. Proc. Natl. Acad. Sci. USA 85 (1988) 1782–1786.
Kagan, V., Schvedova, A., Novikov, K and Kozlov, Y.: Light induced free radical oxidation of membrane lipid photoreceptors of frog retina.Biochem. Biophys. Acta 330 (1973) 76–79.
King, G. and Holmes, R.: Human corneal aldehyde dehydrogenase. Purification, kinetic characterization and phenotypic variation. Biochem. and Mol. Biol. Int. 31 (1993) 49–63.
Kurys, G., Shah, P.C., Kikonyogo, A., Reed, D., Ambroziak, W., and Pietruszko, R.: Human aldehyde dehydrogenase cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde. Eur. J. Biochem. 218 (1993) 311–320.
Laemmli, U.K.: Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680–685.
Pereira, F., Rosenmann, E., Nylen, E., Kaufman, M., Pinsky, L. and Wrogemann, K.: The 56 kDa androgen binding protein is an aldehyde dehydrogenase. Biochem. Biophys. Res. Comm. 175 (1991) 831–838.
Piatigorsky, J., O’Brien, W.E., Norman, B.L., Kalumuck, K., Wistow, G.J., Borras, T., Nickerson, J.M. and Wawrousek, E.F.: Gene sharing by δ-crystallin and argininosuccinate lyase. Proc. Nat. Acad. Sci. USA 85 (1988) 3479–3483.
Pietruszko, R.: Aldehyde dehydrogenase isozymes. In Isozymes: Current Topics in Biological and Medical Research 8. Alan R. Liss, Inc. New York, 1983, pp 195–217.
Scopsi, L., Larsson, L.-I.: Increased sensitivity in peroxidase immunochemistry: A comparative study of a number of peroxidase visualisation methods employing a model system. J. Histochem. 84 (1986) 221–230.
Sidhu, R.S. and Blair, A.H.: Human liver aldehyde dehydrogenase esterase activity. J. Biol. Chem. 250 (1975) 7894–7898.
Smith, P.-K., Krohn, R.I., Hermanson, G.T., Mallia, A.K., Gartner, F.H., Provenzana, M.D., Fujimoto, E.K., Goeke, N.M., Olsen, B.J., and Klenk, D.C.: Measurement of protein using bicinchoninic acid. Anal. Biochem. 150, (1985) 76–85.
Tomarev, S.I. and Piatigorsky, J.: Lens crystallins of invertebrates: diversity and recruitment from detoxification enzymes and novel proteins. Eur. J. Biochem. 235 (1996) 449–465.
van Heyningen, R.: Fluorescent glucosides in the human lens. Nature 230 (1970) 393–394.
Verhagen, C., Hoekzema, R., Verjans, G.M.G.M. and Kijlstra, A.: Identification of bovine corneal protein 54 (BCP 54) as an aldehyde dehydrogenase. Exp. Eye Res. 53 (1991) 283–284.
Wistow, G. and Kim, H.: Lens proteins expression in mammals: taxon-specificity and the recruitment of crystallins. J. Mol. Evol. 32 (1991) 262–269.
Zigman S.: The role of sunlight in human cataract formation. Surv. Ophthalmol. 27 (1983) 317–326.
Zigman, S.: Photobiology of the lens. In Maisel, H. (ed.), The Ocular Lens. Marcel Dekker Inc., 1985, pp 301–347.
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King, G., Holmes, R. (1996). Human Corneal and Lens Aldehyde Dehydrogenases. In: Weiner, H., Lindahl, R., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 6. Advances in Experimental Medicine and Biology, vol 414. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5871-2_4
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