Localization and Properties of Aldehyde Reductase

Wartburg, J. P. von; Ris, Margret M.; Wermuth, Bendicht

doi:10.1016/b978-0-12-691402-3.50024-x

Cited by 4 publications

(1 citation statement)

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“…Kinetic and specificity studies have indicated that only the low-Km enzyme is involved in the reduction of the biogenic aldehydes [Ander son et al, 1976;Whittle and Turner, 1981], Both major forms of this enzyme have been found to be cytoplasmic in mouse liver [Tulsiani and Touster, 1977], but the low-Km forms have been reported to be localized in the mitochondria in rat brain [Anderson et al, 1976;von Wartburg et al, 1977], How ever, Ryle and Tipton [1981] have assessed the location of the low-Km aldehyde reduc tase in ox brain by using pyridine 3-aldehyde and NADH as co-substrates, and concluded that like the high-Km enzyme, it occurs in the cytosol. Similar results have also been found by Turner et al [1982], Little information is available concerning aldehyde-catabolizing enzymes (ALDH and AR) with increasing age.…”

Section: Introductionmentioning

confidence: 99%

Age-Related Changes in Aldehyde Reductase Activity of Rat Brain, Liver and Heart

Danh¹,

Benedetti²,

Dostert³

1984

Gerontology

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Aldehyde reductase (AR) activity was measured in the brain, liver and heart of 23- to 26-month-old and 3-month-old male Wistar rats, using 5 substrates (p-nitrobenzalde-hyde, D-glucuronate, D-xylose, DL-glyceraldehyde and pyridine 3-aldehyde). A significant increase of AR activity was found in whole brain of old rats with P-nitrobenzaldehyde (11 %) and D-glucuronate (24%). Results of experiments carried out with sodium valproate suggest that the AR activity increase in brain of old rats is the high-Km form. A significant increase of AR activity was found in cerebellum (26%), brainstem (19%), hypothalamus (13%), striatum (11 %) and midbrain (6%) of old rats; up to now, the determination of the enzyme activity in the different brain regions has been carried out only with P-nitrobenzaldehyde. A significant increase of AR activity of old rats was also found in liver with D-glucuronate (10%), DL-glyceraldehyde (23%) and pyridine 3-aldehyde (30%), and in heart with P-nitrobenzaldehyde (42%) and DL-glyceraldehyde (20%). A significant decrease of AR activity with D-xylose (15%) was found in heart of old rats compared to matched animals of 3 months. The present study indicates that the regulatory mechanism for AR in brain and peripheral tissues like liver and heart are different with increasing age.

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Section: Introductionmentioning

confidence: 99%

Age-Related Changes in Aldehyde Reductase Activity of Rat Brain, Liver and Heart

Danh¹,

Benedetti²,

Dostert³

1984

Gerontology

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Substrate competition for aldehyde metabolism

Tipton¹,

Smith²,

Ryle³

et al. 1981

Function and Regulation of Monoamine Enzymes: Basic and Clinical Aspects

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Purification and Some Properties of Aldehyde Rcductases from Pig Liver

Branlant

Biellmann

1980

European Journal of Biochemistry

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Two aldehyde reductases (EC 1.1.1.2), I and 11, have been isolated from pig liver. Both are monomeric ( M , % 35 000) and NADPH-dependent. Their activity is inhibited by barbiturates. The enzymes reduce essentially aromatic aldehydes, with a preference for those bearing an electron-withdrawing group in the para position. Substrates with a carboxyl group are specially good substrates for reductase I. This may indicate the presence of a positively charged group in the substrate binding site.The binding of NADPH to reductase I causes a red shift of the coenzyme absorption; this shift is characteristic of B-stereospecific dehydrogenases. Nevertheless, this is not confirmed by the stereochemical study with labelled NADPH. The pro-R hydrogen of NADPH is transferred to the re face of the aldehyde. The stereochemical course of reductase I is identical to that of liver alcohol dehydrogenase, but the two enzymes differ by the absence of Zn and of reactive thiol in reductase I, and by the action of pyrazole on the activity. Considerable differences in substrate specificity and immunological properties have been found between reductase I and I1 but reductases I from liver of different species have some relationship. Reductase I from pig brain and pig kidney seem to be identical to reductase I from pig liver.Monomeric NADPH-dependent aldehyde reductases have been isolated from various mammalian sources [l]. The physiological role of these enzymes, whose activity is sensitive to barbiturate, is still in debate. The reduction of B-hydroxylated biogenic aldehydes is a strong indication in favor of their role in aldehyde detoxification in brain tissue [2,3]. In drug metabolism, it has been demonstrated that daunorubicin, a cancer chemotherapeutic agent, is reduced by a cytoplasmic reductase which proved to be identical to an aldehyde reductase [4,5]. The remarkably broad substrate specificity of aldehyde reductase is in contrast with a rather high substrate specificity of most dehydrogenases. For instance, many substituted benzaldehydes are reduced by these enzymes and particAbbreviutions. clac3PdADP + , 3-chloroacetylpyridine -adenine dinucleotide phosphate; clac3PdADPH, reduced form of clac3-PdADP' ; ac3PdADP+, 3-acetylpyridine-adenine dinucleotide phosphate; ac3PdADPH, reduced form of ac3PdADPH; h:a6-NADPH, 1,4,5,6-tetrahydro-nicotindmide-adenine dinucleotide phosphate; sNADPH, 3-thionicotinamide-odenine dinucleotide phosphate reduced form.

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Localization and Properties of Aldehyde Reductase

Cited by 4 publications

References 15 publications

Age-Related Changes in Aldehyde Reductase Activity of Rat Brain, Liver and Heart

Age-Related Changes in Aldehyde Reductase Activity of Rat Brain, Liver and Heart

Substrate competition for aldehyde metabolism

Purification and Some Properties of Aldehyde Rcductases from Pig Liver

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