Linked Life Data

10998257

Source:http://linkedlifedata.com/resource/pubmed/id/10998257

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
2000-10-13
pubmed:abstractText
Rat liver contains two class 1 aldehyde dehydrogenases (ALDHs): a constitutive isozyme (ALDH1) and a phenobarbital-inducible isozyme (ALDH-PB). Defining characteristics of mammalian class 1 ALDHs include a homotetrameric structure, high expression in liver, sensitivity to the inhibitor disulfiram, and high activity for the oxidation of retinal. It is often presumed that ALDH-PB is the rat ortholog of mammalian ALDH1, and the identity of rat ALDH-PB is commonly interchanged with ALDH1. In this study, we characterized recombinant rat liver cytosolic ALDH1 and ALDH-PB. Previous reports indicate that ALDH-PB is a homodimer; however, we found by mass spectrometry and gel electrophoresis that it is a homotetramer. ALDH1 mRNA was highly expressed in untreated rat liver, while ALDH-PB had very weak expression, in contrast to a previous report that ALDH-PB mRNA is expressed in untreated rat liver. Rat liver ALDH1 had a high affinity for retinal (K(m) = 0.6 microM), while no oxidation by ALDH-PB could be detected with 20 microM retinal. ALDH1 was more efficient at oxidizing acetaldehyde, propionaldehyde, and benzaldehyde and was more sensitive to disulfiram inhibition. We conclude that rat liver ALDH1 is the ortholog of mammalian liver ALDH1. Furthermore, despite a high level of sequence identity and classification as a class 1 ALDH, ALDH-PB does not function like ALDH1. ALDH-PB is not merely an inducible ALDH1 isozyme; it is a distinct ALDH isozyme.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11170-6
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:10998257-Aldehyde Dehydrogenase, pubmed-meshheading:10998257-Amino Acid Sequence, pubmed-meshheading:10998257-Animals, pubmed-meshheading:10998257-Cytosol, pubmed-meshheading:10998257-Disulfiram, pubmed-meshheading:10998257-Enzyme Induction, pubmed-meshheading:10998257-Enzyme Inhibitors, pubmed-meshheading:10998257-Isoenzymes, pubmed-meshheading:10998257-Liver, pubmed-meshheading:10998257-Magnesium Chloride, pubmed-meshheading:10998257-Mass Spectrometry, pubmed-meshheading:10998257-Molecular Sequence Data, pubmed-meshheading:10998257-Phenobarbital, pubmed-meshheading:10998257-RNA, Messenger, pubmed-meshheading:10998257-Rats, pubmed-meshheading:10998257-Rats, Sprague-Dawley, pubmed-meshheading:10998257-Recombinant Proteins, pubmed-meshheading:10998257-Retinal Dehydrogenase, pubmed-meshheading:10998257-Sequence Homology, Amino Acid, pubmed-meshheading:10998257-Substrate Specificity
pubmed:year
2000
pubmed:articleTitle
Rat liver constitutive and phenobarbital-inducible cytosolic aldehyde dehydrogenases are highly homologous proteins that function as distinct isozymes.
pubmed:affiliation
Clinical Pharmacology Unit, Department of Molecular Pharmacology and Experimental Therapeutics, and Biomedical Mass Spectrometry Facility, Mayo Clinic and Foundation, Rochester, Minnesota 55905, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.