Mitochondrial aldehyde dehydrogenase from human liver

Hempel, John; Kaiser, R.; Jörnvall, Hans

doi:10.1111/j.1432-1033.1985.tb09261.x

Cited by 23 publications

(40 citation statements)

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“…The remaining four clones contained shorter cDNA inserts, hence no further work was done with these. As will be discussed in the following section, IrmAL1 contained almost the entire coding region for the mature rat mitochondrial aldehyde dehydrogenase, except for the first two amino acids, based upon the protein sequence of the human enzyme [2].…”

Section: Isolation and Characterization Of Rat Mitochondrial Aldehydementioning

confidence: 99%

“…1A). This sequence contained information coding for 429 amino acid residues of bovine mitochondrial aldehyde dehydrogenase which corresponded to amino acids 72 -500 of human mitochondrial aldehyde dehydrogenase [2]. Since it was not possible to find any cDNA coding for the N-terminal region of bovine mitochondrial aldehyde dehydrogenase in this library, a random-primed, dgtll , cDNA library was also screened using cDNA probes.…”

Section: Isolation and Sequencing Of The Cdna Coding Jor Bovine Livermentioning

confidence: 99%

“…MacGillivray (University of British Columbia, Vancouver) [ 151. A 17-base-long oligonucleotide 5'-GCCC@TCCAT$T-CNGC-3' was synthesized, which was complementary to the coding strand for amino acid residues 281-286 of human mitochondrial aldehyde dehydrogenase [2]. This oligonucleotide was labeled with [Y-~~P]ATP by T4 polynucleotide kinase and used as a hybridization probe.…”

Section: Isolation Of Bovine Aldehyde Dehydrogenare Cdna Clonesmentioning

confidence: 99%

“…The nucleotide sequences are numbered starting at the 5'-end of the rat cDNA. The amino acid sequences are numbered according to the amino acid sequence of the mature human enzyme [2]. Residues labelled -19 to -1 have been postulated to constitute the rat signal peptidc [12].…”

Section: Fig 2 Nucleotidr Sequences Of Rut ( R ) and Bovine ( B ) Mmentioning

confidence: 99%

“…The amino acid sequences of the human [2] and horse [3] liver mitochondrial enzymes have been published. They share 94% identity.…”

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confidence: 99%

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Primary structures of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences

Farrés

Guan

Weiner

1989

European Journal of Biochemistry

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The cDNA coding for rat liver mitochondrial aldehyde dehydrogenase was cloned and sequenced. It contained an open reading frame of 1557 bp. Of the deduced 519 amino acid residues, 19 were proposed to correspond to the signal peptide necessary to allow the protein to enter the mitochondria [Farrts, J., Weiner, H. (1987) Biochem. Biophys. Res. Commun. 1.50, 1083-10871. The sequence of the 500 amino acid residues comprising the mature subunit was 96% identical to that of the corresponding human liver mitochondrial enzyme. The longest cDNA isolated coding for the bovine liver enzyme contained sequence information corresponding to residues 72 -500 of the rat or human enzyme. The deduced protein sequence of these residues was 94% identical to those of the human enzyme.Over 60% of the bases in the coding region of the rat cDNA were G and C. These residues were clustered non-randomly and two potentially stable stem-loop structures could be calculated as existing in the mRNA. One would be found in the region coding for amino acid residues 64 -79; a similar secondary structure could be responsible for the existing truncated cDNAs from the bovine-cDNA libraries. Comparisons with the amino acid sequences of other aldehyde dehydrogenases support the suggestion that the NAD-binding domain may be located in the middle portion of the mature enzyme.Mammalian mitochondrial aldehyde dehydrogenase, a ubiquitous and constitutive NAD-dependent enzyme, is involved in the oxidation of biogenic aldehydes, as well as acetaldehyde formed during the metabolism of ethanol. The enzyme from most species is isolated as a tetramer of molecular mass 220 -250 kDa, resulting in a subunit molecular mass of 55 -60 kDa [l], which is larger than that of most dehydrogenases.The amino acid sequences of the human [2] and horse [3] liver mitochondrial enzymes have been published. They share 94% identity. Cytosolic enzymes from human [4] and horse [5] liver have also been sequenced and they share 91 O h identity. In contrast, mitochondrial and cytoplasmic aldehyde dehydrogenases show just 66 -68% identity.

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Section: Isolation and Characterization Of Rat Mitochondrial Aldehydementioning

confidence: 99%

Section: Isolation and Sequencing Of The Cdna Coding Jor Bovine Livermentioning

confidence: 99%

Section: Isolation Of Bovine Aldehyde Dehydrogenare Cdna Clonesmentioning

confidence: 99%

Section: Fig 2 Nucleotidr Sequences Of Rut ( R ) and Bovine ( B ) Mmentioning

confidence: 99%

“…The amino acid sequences of the human [2] and horse [3] liver mitochondrial enzymes have been published. They share 94% identity.…”

mentioning

confidence: 99%

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Primary structures of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences

Farrés

Guan

Weiner

1989

European Journal of Biochemistry

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Localization of cytosolic aldehyde dehydrogenase in the developing chick retina: In situ hybridization and immunohistochemical analyses

Godbout

Packer

Poppema

et al. 1996

Developmental Dynamics

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Cytosolic aldehyde dehydrogenase (ALDH) mRNA is present at high levels in the undifferentiated chick retina. Tissue maturation is accompanied by a 20–25× decrease in transcript levels. To determine the spatial and temporal distribution pattern of the ALDH transcript and its encoded protein in the developing retina, in situ hybridization and immunohistochemical analyses were carried out using chick embryos at different stages of development. The ALDH transcript and protein were detected at the earliest stage tested, in the inner layer of the optic cup of stage 14 (day 2) embryos. Both the ALDH transcript and protein were found in the dorsal retina of chick embryos from stage 18 (day 3) to day 16 of incubation. Accumulation of the ALDH protein in the neurites of ganglion cells could readily be detected at early developmental stages. Staining of this ganglion fiber layer was strong in the dorsal retina and could be followed up to and into the optic nerve. By day 11, ALDH mRNA was located primarily in the ciliary margin and in the inner nuclear layer of the dorsal retina. In addition to these areas, the ALDH protein was also found in the inner plexiform and optic nerve fiber layers. These results suggest that environmental or transcriptional factors involved in the regulation of the ALDH gene are restricted to the dorsal retina at early developmental stages and that there is a requirement for the compartmentalization of the ALDH transcript/protein in the undifferentiated chick retina. © 1996 Wiley‐Liss, Inc.

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Genetic polymorphism of human liver alcohol and aldehyde dehydrogenases, and their relationship to alcohol metabolism and alcoholism

1986

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It is now widely accepted that the various pharmacologic and addictive consequences of alcohol consumption are related to the tissue concentration of ethanol or its metabolic products. The oxidative metabolism of ethanol in liver is principally catalyzed by alcohol dehydrogenase and aldehyde dehydrogenase. Both of these enzymes exist in multiple molecular forms, and genetic models have been proposed to account for the multiplicity of isoenzymes. Alcohol dehydrogenase subunits are encoded at five different gene loci, and genetic polymorphism occurs at two alcohol dehydrogenase loci. Variant isoenzymes produced at the two polymorphic alcohol dehydrogenase loci account for the differences in enzyme electrophoretic patterns observed among individuals. Some of these variant isoenzymes exhibit widely different kinetic properties, and this may account for the 2- to 3-fold variation in alcohol elimination rate among individuals. Since the protein sequence of several of the alcohol dehydrogenase subunits has been determined and several of the alcohol dehydrogenase genes has been cloned, some of the structural changes which give rise to differences in catalytic and electrophoretic properties are now known. Genetic polymorphism also occurs at the aldehyde dehydrogenase gene locus which encodes the mitochondrial low Km for acetaldehyde aldehyde dehydrogenase isoenzyme. The variant isoenzyme exhibits little or no catalytic activity. Individuals with this "null" variant have higher than normal blood acetaldehyde levels and exhibit an alcohol-flush reaction which appears to be a deterrent to heavy drinking and alcoholism.(ABSTRACT TRUNCATED AT 250 WORDS)

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Mitochondrial aldehyde dehydrogenase from human liver

Abstract: ii few smaller peptlaes n o t recovered from t h e lnltlai dlgrSt.

Cited by 23 publications

References 0 publications

Primary structures of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences

Primary structures of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences

Localization of cytosolic aldehyde dehydrogenase in the developing chick retina: In situ hybridization and immunohistochemical analyses

Genetic polymorphism of human liver alcohol and aldehyde dehydrogenases, and their relationship to alcohol metabolism and alcoholism

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