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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The amino acid compositions of several monomeric NADPH-dependent aldehyde reductases from a variety of species have been determined and analyzed by the difference index method of Metzger et al. (1968). The difference indexes among mammals range from 4.15 - 6.10 indicating considerable homology. Comparison of chicken aldehyde reductase with mammalian aldehyde reductases gave values in the range 6.8 - 9.9 suggesting a close relationship whereas the difference indexes for the enzymes from fruit fly and Baker's yeast versus vertebrate aldehyde reductases (10.9 - 14.4) indicate more distant relationships. The extent of sequence homology among aldehyde reductases from these species was estimated from a plot of difference index versus percent sequence difference for oxido-reductases of known sequence. From this plot, and using a mammal-chicken divergence time of 300 million years and a mammalian order split of 75 million years, the rate of evolution of aldehyde reductases was calculated to lie in the range 5.8 - 15.6% sequence difference per 100 million years. Comparison with rates of evolution of oligomeric dehydrogenases indicates that aldehyde reductases comprise the most rapidly evolving family of oxido-reductases. This is probably related to the monomericity of aldehyde reductases since there is a direct correlation between the number of subunits and the rate of evolution.
J Mol Evol 1979 Dec
PMID:Compositional relatedness of aldehyde reductases from several species. 4 5

Immobilization of myosin, actin, actomyosin and subfragment S1 on kapron fibre was achieved with the help of glutaric aldehyde. The ATPase activity of myosin and its ability to interact with actin is preserved; while the ATPase activity of S1 subfragment decreases considerably. The immobilization on kapron fibre changes the pH-dependance of ATPase activity of myosin and that of subfragment S1, shifting the maximum to low pH zone (pH 5.5), and increases the thermostability of the enzyme. The ions of Ca++ in all cases act as an activating agent on ATPase while the ions of Mg++ either do not affect myosin and subfragment S1 at all, or increase the activity in the case of the immobilized of actomyosin but to a lesser degree than the ions of Ca++. The immobilized actin preserves its ability to form actomyosin complex.
Mol Biol (Mosk)
PMID:[Chemical suturing of myosin and actin to capron fiber]. 13 56

The work of Kenyon and Nissenbaum on aldocyanoin microspheres was repeated and extended. It was determined that the microspheres contained amino acids and that specific amino acids could be incorporated into the microspheres by adding the requisite aldehyde or ketone precursor to the model mixture. Microsphere formation was found to be dependent on the availability of oxygen. Under anaerobic conditions of synthesis, no microspheres formed in the time allotted and the amino acid composition of the macromolecular material was simple. Microparticulate material synthesized by C. Folsome using a quenched spark technique was analyzed and found to contain amino acids that had a qualitative composition similar to both a Miller-Urey discharge and the Kenyon-Nissenbaum microspheres.
J Mol Evol 1979 Oct
PMID:Aldocyanoin microspheres: partial amino acid analysis of the microparticulates formed from simple reactants under various conditions. 50 47

Rats of the Wistar/Af/Han/Mol/(Han 67) strain have previously been shown to respond in a variable way to phenobarbital treatment, as far as the induction of aldehyde dehydrogenase activity is concerned (Marselos 1976). This biochemical property is genetically determined and concerns the high-Km aldehyde dehydrogenase of the hepatic cytosol. In this study, administration of phenobarbital (1 mg/mo of drinking water, for 1 week) produces a uniform induction of aldehyde dehydrogenase in all rats, when measured with micromolar substrate concentration. The inducible low-Km enzyme of the cytosol is not genetically determined like the high-Km enzyme, and shows a wide specificity for aliphatic as well as for aromatic aldehydes. Despite the inducibility of the cytosolic enzymes, no alterations are found in the mitochondrial aldehyde dehydrogenase activities after phenobarbital treatment. The oxidation of D-glucuronolactone takes place only in the cytosol, and seems to be dependent on the low-Km aldehyde dehydrogenase. This is consistent with NMR studies, which showed that a very minimal amount of D-glucuronolactone is in aldehyde form under the measurement conditions usually applied. Further, the oxidation of D-glucuronolactone is also enhanced by phenobarbital in all rats without a genetic predisposition, and its dose-response curve is very similar to that of the low-Km aldehyde dehydrogenase.
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PMID:Inducible aldehyde dehydrogenases in the hepatic cytosol of the rat. 57 55

Linoleic acid hydroperoxydes (LOOH) containing 13-hydroperoxyoctadeca-9,11-(75%) and 9-hydroperoxyoctadeca-10,12-dienoic acid (25%) were emulsified at pH 6.5. After addition of hemoglobin, ferrous ions, ferric ions, cysteine or ascorbic acid the emulsions were stored 19 hours at 22 degrees C. The decrease in the diene and peroxyde concentrations and the formation of volatile carbonyl compounds were analysed. Ferrous ions and ascorbic acid were the strongest producers of volatile carbonyl compounds. In the presence of 10(-3) Mol ascorbic acid 6 mumol volatile aldehydes arise from 75 mumol LOOH. Hexanal (70 mol-%) was the main component of the aldehyde fraction. For plant foodstuffs the significance of the reaction of fatty acids hydroperoxydes with ascorbic acid for the formation of flavour substances is discussed.
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PMID:[Breakdown of linoeic acid hydroperoxydes. Formation of volatile carbonyl compounds (author's transl)]. 97 38

The alcohol dehydrogenase (ADH) system in the yeast Kluyveromyces lactis is encoded by four ADH genes. In this paper we report evidence that at least three of these genes are transcribed and translated into protein. KIADH1 and KIADH2, which encode cytoplasmic activities, are preferentially expressed in glucose-grown cells with respect to ethanol-grown cells. KIADH4, which encodes one of the two activities localized within mitochondria, is induced at the transcriptional level in the presence of ethanol as is the ADH2 gene in Saccharomyces cerevisiae. However the regulation of the expression of the K. lactis gene is completely different from that of ADH2 and of other known ADH genes in that KIADH4 is insensitive to glucose repression and is not expressed on non-fermentable carbon sources other than ethanol. This kind of regulation can be clearly observed in non-fermenting strains, where the induction of KIADH4 is dependent on the addition of ethanol to the medium. On the contrary, in fermenting strains KIADH4 is always induced by ethanol or acetaldehyde produced endocellularly and this results in constitutive expression of the gene also in the presence of glucose. The mitochondrial localization of the activity encoded by KIADH4 and the peculiar regulation of this gene could be related to the fact that K. lactis is a petite negative yeast in which some mitochondrial functions seem to be essential for cell viability.
Mol Microbiol 1992 Aug
PMID:Ethanol-induced and glucose-insensitive alcohol dehydrogenase activity in the yeast Kluyveromyces lactis. 140 68

Acetaldehyde, the first product in the metabolism of ethanol, is known to condense with plasma proteins, forming stable adducts. We have previously shown that these adducts can be recognized as foreign by the immune system. In the present study the existence of type I hypersensitivity-mediating antibodies against these adducts was investigated in humans and in animals. Immunization of mice with acetaldehyde-protein condensates, followed by adoptive transfer of splenocytes, led to the production of IgE anti-acetaldehyde adducts. A monoclonal IgE antibody was obtained by the hybridization technique. This antibody recognized acetaldehyde adducts, independently of the carrier protein used, indicating that the acetaldehyde moiety behaves as a hapten. The affinity of the antibody for the acetaldehyde adduct of polylysine was 7 orders of magnitude higher than that for polylysine. Passive immunization by intradermal or intravenous administration of this monoclonal antibody to rats rendered the animals hypersensitive to acetaldehyde-protein conjugates, as shown by marked anaphylaxis. A study was conducted to determine the existence of naturally occurring hypersensitivity reactions to alcohol in > 1000 non-Oriental individuals. A prevalence of severe hypersensitivity reactions of 0.46% was found. The reactions were severe enough to deter these individuals from consuming all types of alcoholic beverages. Individuals presenting such reactions had significantly elevated levels of circulating anti-acetaldehyde-protein IgE antibodies.
Mol Pharmacol 1992 Oct
PMID:Hypersensitivity to acetaldehyde-protein adducts. 143 47

Intracellular calcium levels play an important role in myofibril disintegration and regeneration of muscle fibers. Earlier studies have shown that the calcium activated protease, calpain, is involved in the removal of Z-discs from myofibrils of striated muscle and the tripeptide-aldehyde, leupeptin, which is an inhibitor of calpain, inhibits this activity. In the present communication, we demonstrate that leupeptin and another calpain inhibitor, E64d, inhibit the fusion of mouse skeletal muscle C2C12 myoblasts to form multinucleated myotubes in tissue culture.
Cell Mol Biol 1992 Aug
PMID:The effect of protease inhibitors, leupeptin and E64d, on differentiation of C2C12 myoblasts in tissue culture. 146 8

Intracellular calcium levels play an important role in myofibril disintegration and regeneration of muscle fibers. Earlier studies have shown that the calcium activated protease, calpain, is involved in the removal of Z-discs from myofibrils of striated muscle and the tripeptide-aldehyde, leupeptin, which is an inhibitor of calpain, inhibits this activity. In the present communication, we demonstrate that leupeptin and another calpain inhibitor, E64d, inhibit the fusion of mouse skeletal muscle C2C12 myoblasts to form multinucleated myotubes in tissue culture.
Cell Mol Biol (Noisy-le-grand)
PMID:The effect of protease inhibitors, leupeptin and E64d, on differentiation of C2C12 myoblasts in tissue culture. 148 17

Aldehydes are highly reactive molecules that may have a variety of effects on biological systems. They can be generated from a virtually limitless number of endogenous and exogenous sources. Although some aldehyde-mediated effects such as vision are beneficial, many effects are deleterious, including cytotoxicity, mutagenicity, and carcinogenicity. A variety of enzymes have evolved to metabolize aldehydes to less reactive forms. Among the most effective pathways for aldehyde metabolism is their oxidation to carboxylic acids by aldehyde dehydrogenases (ALDHs). ALDHs are a family of NADP-dependent enzymes with common structural and functional features that catalyze the oxidation of a broad spectrum of aliphatic and aromatic aldehydes. Based on primary sequence analysis, three major classes of mammalian ALDHs--1, 2, and 3--have been identified. Classes 1 and 3 contain both constitutively expressed and inducible cytosolic forms. Class 2 consists of constitutive mitochondrial enzymes. Each class appears to oxidize a variety of substrates that may be derived either from endogenous sources such as amino acid, biogenic amine, or lipid metabolism or from exogenous sources, including aldehydes derived from xenobiotic metabolism. Changes in ALDH activity have been observed during experimental liver and urinary bladder carcinogenesis and in a number of human tumors, including some liver, colon, and mammary cancers. Changes in ALDH define at least one population of preneoplastic cells having a high probability of progressing to overt neoplasms. The most common change is the appearance of class 3 ALDH dehydrogenase activity in tumors arising in tissues that normally do not express this form. The changes in enzyme activity occur early in tumorigenesis and are the result of permanent changes in ALDH gene expression. This review discusses several aspects of ALDH expression during carcinogenesis. A brief introduction examines the variety of sources of aldehydes. This is followed by a discussion of the mammalian ALDHs. Because the ALDHs are a relatively understudied family of enzymes, this section presents what is currently known about the general structural and functional properties of the enzymes and the interrelationships of the various forms. The remainder of the review discusses various aspects of the ALDHs in relation to tumorigenesis. The expression of ALDH during experimental carcinogenesis and what is known about the molecular mechanisms underlying those changes are discussed. This is followed by an extended discussion of the potential roles for ALDH in tumorigenesis. The role of ALDH in the metabolism of cyclophosphamidelike chemotherapeutic agents is described. This work suggests that modulation of ALDH activity may an important determinant of the effectiveness of certain chemotherapeutic agents.(ABSTRACT TRUNCATED AT 400 WORDS)
Crit Rev Biochem Mol Biol 1992
PMID:Aldehyde dehydrogenases and their role in carcinogenesis. 152 60


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