Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex

Doran (nee Udovikova), O. and Wojtzcak, L. and Polish Academy of Sciences (1998) Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex. The International Journal of Biochemistry & Cell Biology, 30 (5). pp. 597-608. ISSN 1357-2725

Full text not available from this repository

Publisher's URL: http://dx.doi.org/10.1016/S1357-2725(97)00143-X

Abstract

Aldehyde reductase (EC 1.1.1.2) has been regarded so far as an exclusively cytosolic enzyme. The present investigation shows that mitochondria of rat liver, kidney cortex and, tentatively, heart also contain an enzyme catalyzing oxidation of NADPH by aldehydes, p-nitrobenzaldehyde, methylglyoxal and glyceraldehyde. Activity of the mitochondrial enzyme can only be measured after the organelles are disrupted by sonication or solubilized with nonionic detergents. Mitochondrial aldehyde reductase activity contributed to about 4.6% and 2.5% of the total cellular activity in liver and kidney cortex, respectively. However, the specific activity in liver mitochondria was about one third and in kidney cortex mitochondria one tenth of that in the cytosol of the corresponding organ. The mitochondrial enzyme resembled the cytosolic one by its absolute specificity towards NADPH as the electron donor, a similar profile of aldehydic electron acceptors and identical Km values. Mitochondrial aldehyde reductase differed from the cytosolic enzyme by low sensitivity to known inhibitors of cytosolic aldehyde reductase, AL-1576, AL-4114 and ONO-2235. In liver, about 60% of the mitochondrial activity was tightly bound to the membranes whereas about 40% was present in the mitochondrial matrix. The membrane-bound activity was inactivated by digestion of mitoplasts with trypsin, alpha-chymotrypsin or papain, thus pointing to exposition of the substrate-binding site at the external surface of the inner membrane. On the other hand, latency of the enzyme in intact mitochondria indicates that the NADPH-binding site is located at the inner surface. These data provide the first direct evidence for the existence of aldehyde reductase in mitochondria of some rat tissues. PMID:9693960[PubMed - indexed for MEDLINE] Publication Types, MeSH Terms, SubstancesPublication TypesResearch Support, Non-U.S. Gov'tMeSH TermsAldehyde Reductase/isolation & purificationAldehyde Reductase/metabolism*AnimalsCytosol/enzymologyIntracellular Membranes/metabolismKidney Cortex/enzymology*MaleMitochondria/enzymology*Mitochondria, Liver/enzymology*RatsRats, WistarSubstancesAldehyde Reductase LinkOut - more resourcesFull Text SourcesElsevier ScienceIngenta plcEBSCOOhioLINK Electronic Journal CenterSwets Information Services • Supplemental Content Related citations Oxidation of lactaldehyde by cytosolic aldehyde dehydrogenase and inhibition of cytosolic and mitochondrial aldehyde dehydrogenase by metabolites. [Biochim Biophys Acta. 1984] Oxidation of lactaldehyde by cytosolic aldehyde dehydrogenase and inhibition of cytosolic and mitochondrial aldehyde dehydrogenase by metabolites. Ray S, Ray M. Biochim Biophys Acta. 1984 Nov 6; 802(1):128-34. Mitochondrial and cytosolic localization of a single glycerate kinase in rat kidney cortex. [J Biochem. 1979] Mitochondrial and cytosolic localization of a single glycerate kinase in rat kidney cortex. Katayama H, Kitagawa Y, Sugimoto E. J Biochem. 1979 Nov; 86(5):1337-43. Is monoamine oxidase activity in the outer mitochondrial membrane influenced by the mitochondrial respiratory state? [Biochim Biophys Acta. 1995] Is monoamine oxidase activity in the outer mitochondrial membrane influenced by the mitochondrial respiratory state? Wojtczak AB, Brdiczka D, Wojtczak L. Biochim Biophys Acta. 1995 Apr 26; 1229(2):249-55. Review [Cooperation of membrane proteins and cytosolic proteins in metabolic regulation--involvement of binding of hexokinase to mitochondria in regulation of glucose metabolism and association and complex formation between membrane proteins and cytosolic proteins in regulation of active oxygen production]. [Yakugaku Zasshi. 1999] Review [Cooperation of membrane proteins and cytosolic proteins in metabolic regulation--involvement of binding of hexokinase to mitochondria in regulation of glucose metabolism and association and complex formation between membrane proteins and cytosolic proteins in regulation of active oxygen production]. Ishibashi S. Yakugaku Zasshi. 1999 Jan; 119(1):16-34. Review Topology of hepatic mitochondrial carnitine palmitoyltransferase I. [Adv Exp Med Biol. 1999] Review Topology of hepatic mitochondrial carnitine palmitoyltransferase I. Kashfi K, Cook GA. Adv Exp Med Biol. 1999; 466:27-42. See reviews... See all... All links from this record Related Citations Calculated set of PubMed citations closely related to the selected article(s) retrieved using a word weight algorithm. Related articles are displayed in ranked order from most to least relevant, with the “linked from” citation displayed first.Gene Gene records that cite the current articles. Citations in Gene are added manually by NCBI or imported from outside public resources.HomoloGene HomoloGene clusters of homologous genes and sequences that cite the current articles. These are references on the Gene and sequence records in the HomoloGene entry.

Item Type:Article
Uncontrolled Keywords:mitochondria, adehyde reductase, liver, kidney
Faculty/Department:Faculty of Health and Applied Sciences > Department of Biological, Biomedical and Analytical Sciences
ID Code:14944
Deposited By: Professor O. Doran
Deposited On:13 Jun 2011 13:33
Last Modified:12 Aug 2013 08:06

Request a change to this item

Copyright 2013 © UWE better together