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Article: Identification and characterization of a novel human aldose reductase- like gene

TitleIdentification and characterization of a novel human aldose reductase- like gene
Authors
Issue Date1998
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 1998, v. 273 n. 19, p. 11429-11435 How to Cite?
AbstractWe have identified a novel human protein that is highly homologous to aldose reductase (AR). This protein, which we called ARL-1, consists of 316 amino acids, the same size as AR, and its amino acid sequence is 71% identical to that of AR. It is more closely related to the AR-like proteins such as mouse vas deferens protein, fibroblast growth factor-regulated protein, and Chinese hamster ovary reductase, with 81, 82, and 83%, respectively, of its amino acid sequence identical to the amino acid sequence of these proteins. The cDNA of ARL-1 was expressed in Escherichia coli to obtain recombinant protein for characterization of its enzymatic activities. For comparison, the cDNA of human AR was also expressed in E. coli and analyzed in parallel. These two enzymes differ in their pH optima and salt requirement, but they act on a similar spectrum of substrates. Similar to AR, ARL-1 can efficiently reduce aliphatic and aromatic aldehydes, and it is less active on hexoses. While AR mRNA is found in most tissues studied, ARL-1 is primarily expressed in the small intestines and in the colon, with a low level of its mRNA in the liver. The ability of ARL-1 to reduce various aldehydes and the locations of expression of this gene suggest that it may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. Interestingly, ARL-1 and AR are overexpressed in some liver cancers, but it is not clear if they contribute to the pathogenesis of this disease.
Persistent Identifierhttp://hdl.handle.net/10722/49325
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorCao, Den_HK
dc.contributor.authorFan, STen_HK
dc.contributor.authorChung, SSMen_HK
dc.date.accessioned2008-06-12T06:39:32Z-
dc.date.available2008-06-12T06:39:32Z-
dc.date.issued1998en_HK
dc.identifier.citationJournal Of Biological Chemistry, 1998, v. 273 n. 19, p. 11429-11435en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/49325-
dc.description.abstractWe have identified a novel human protein that is highly homologous to aldose reductase (AR). This protein, which we called ARL-1, consists of 316 amino acids, the same size as AR, and its amino acid sequence is 71% identical to that of AR. It is more closely related to the AR-like proteins such as mouse vas deferens protein, fibroblast growth factor-regulated protein, and Chinese hamster ovary reductase, with 81, 82, and 83%, respectively, of its amino acid sequence identical to the amino acid sequence of these proteins. The cDNA of ARL-1 was expressed in Escherichia coli to obtain recombinant protein for characterization of its enzymatic activities. For comparison, the cDNA of human AR was also expressed in E. coli and analyzed in parallel. These two enzymes differ in their pH optima and salt requirement, but they act on a similar spectrum of substrates. Similar to AR, ARL-1 can efficiently reduce aliphatic and aromatic aldehydes, and it is less active on hexoses. While AR mRNA is found in most tissues studied, ARL-1 is primarily expressed in the small intestines and in the colon, with a low level of its mRNA in the liver. The ability of ARL-1 to reduce various aldehydes and the locations of expression of this gene suggest that it may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. Interestingly, ARL-1 and AR are overexpressed in some liver cancers, but it is not clear if they contribute to the pathogenesis of this disease.en_HK
dc.format.extent418 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.rightsJournal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.subject.meshAldehyde Reductase - geneticsen_HK
dc.subject.meshCarcinoma, Hepatocellular - enzymology - geneticsen_HK
dc.subject.meshLiver Neoplasms - enzymology - geneticsen_HK
dc.subject.meshSugar Alcohol Dehydrogenases - geneticsen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.titleIdentification and characterization of a novel human aldose reductase- like geneen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-9258&volume=273&issue=19&spage=11429&epage=11435&date=1998&atitle=Identification+and+characterization+of+a+novel+human+aldose+reductase-like+geneen_HK
dc.identifier.emailFan, ST: stfan@hku.hken_HK
dc.identifier.emailChung, SSM: smchung@hkucc.hku.hken_HK
dc.identifier.authorityFan, ST=rp00355en_HK
dc.identifier.authorityChung, SSM=rp00376en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.doi10.1074/jbc.273.19.11429en_HK
dc.identifier.pmid9565553-
dc.identifier.scopuseid_2-s2.0-2642679232en_HK
dc.identifier.hkuros36091-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-2642679232&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume273en_HK
dc.identifier.issue19en_HK
dc.identifier.spage11429en_HK
dc.identifier.epage11435en_HK
dc.identifier.isiWOS:000073536700007-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridCao, D=7202125033en_HK
dc.identifier.scopusauthoridFan, ST=7402678224en_HK
dc.identifier.scopusauthoridChung, SSM=14120761600en_HK

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