Developmental Expression of Alcohol Dehydrogenase (ADH3) in Zebrafish (Danio rerio)
Alcohol dehydrogenase (ADH) is the primary enzyme responsible for metabolism of ethanol to acetaldehyde. One class of ADH has been described in fish, and has been found to be structurally similar to mammalian class III ADH (glutathione-dependent formaldehyde dehydrogenase) but functionally similar t...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2001-09, Vol.286 (5), p.1082-1086 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Dasmahapatra, Asok K. Doucet, Herman L. Bhattacharyya, Champa Carvan, Michael J. |
| description | Alcohol dehydrogenase (ADH) is the primary enzyme responsible for metabolism of ethanol to acetaldehyde. One class of ADH has been described in fish, and has been found to be structurally similar to mammalian class III ADH (glutathione-dependent formaldehyde dehydrogenase) but functionally similar to class I ADH (primarily responsible for ethanol metabolism). We have cloned a cDNA by RT-PCR from zebrafish (Danio rerio) liver representing the zebrafish ADH3 gene product, with a coding region of 1131 nucleotides. The deduced amino acid sequences share 90% identity to ADH3 from the marine fish Sparus aurata, and 82 and 81% identity to the mouse and human sequences, respectively. Using a quantitative competitive RT-PCR assay, ADH3 mRNA was detected at all timepoints analyzed and was lowest between 8 and 24 h postfertilization. Thus, differential ADH3 expression may be at least partly responsible for temporal variations in the sensitivity of zebrafish embryos to developmental alcohol exposure. |
| doi_str_mv | 10.1006/bbrc.2001.5511 |
| format | Article |
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One class of ADH has been described in fish, and has been found to be structurally similar to mammalian class III ADH (glutathione-dependent formaldehyde dehydrogenase) but functionally similar to class I ADH (primarily responsible for ethanol metabolism). We have cloned a cDNA by RT-PCR from zebrafish (Danio rerio) liver representing the zebrafish ADH3 gene product, with a coding region of 1131 nucleotides. The deduced amino acid sequences share 90% identity to ADH3 from the marine fish Sparus aurata, and 82 and 81% identity to the mouse and human sequences, respectively. Using a quantitative competitive RT-PCR assay, ADH3 mRNA was detected at all timepoints analyzed and was lowest between 8 and 24 h postfertilization. Thus, differential ADH3 expression may be at least partly responsible for temporal variations in the sensitivity of zebrafish embryos to developmental alcohol exposure.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.2001.5511</identifier><identifier>PMID: 11527411</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>ADH3 ; ADH3 gene ; alcohol dehydrogenase ; Alcohol Dehydrogenase - biosynthesis ; Alcohol Dehydrogenase - chemistry ; Amino Acid Sequence ; Animals ; Binding, Competitive ; competitive RT-PCR ; Cytosol ; Danio rerio ; DNA, Complementary - metabolism ; Embryo, Nonmammalian - metabolism ; ethanol ; Freshwater ; Glutathione - metabolism ; Humans ; Kinetics ; Larva - metabolism ; Liver - metabolism ; Molecular Sequence Data ; Phylogeny ; Protein Isoforms ; Reverse Transcriptase Polymerase Chain Reaction ; RNA - metabolism ; RNA, Messenger - metabolism ; teratogenesis ; Time Factors ; Zebrafish</subject><ispartof>Biochemical and biophysical research communications, 2001-09, Vol.286 (5), p.1082-1086</ispartof><rights>2001 Academic Press</rights><rights>Copyright 2001 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c371t-a257bcc336d97b784235ac2f02e80c40fe225c32366d1fe6654ce1147eb6ad93</citedby><cites>FETCH-LOGICAL-c371t-a257bcc336d97b784235ac2f02e80c40fe225c32366d1fe6654ce1147eb6ad93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/bbrc.2001.5511$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27922,27923,45993</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11527411$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dasmahapatra, Asok K.</creatorcontrib><creatorcontrib>Doucet, Herman L.</creatorcontrib><creatorcontrib>Bhattacharyya, Champa</creatorcontrib><creatorcontrib>Carvan, Michael J.</creatorcontrib><title>Developmental Expression of Alcohol Dehydrogenase (ADH3) in Zebrafish (Danio rerio)</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Alcohol dehydrogenase (ADH) is the primary enzyme responsible for metabolism of ethanol to acetaldehyde. One class of ADH has been described in fish, and has been found to be structurally similar to mammalian class III ADH (glutathione-dependent formaldehyde dehydrogenase) but functionally similar to class I ADH (primarily responsible for ethanol metabolism). We have cloned a cDNA by RT-PCR from zebrafish (Danio rerio) liver representing the zebrafish ADH3 gene product, with a coding region of 1131 nucleotides. The deduced amino acid sequences share 90% identity to ADH3 from the marine fish Sparus aurata, and 82 and 81% identity to the mouse and human sequences, respectively. Using a quantitative competitive RT-PCR assay, ADH3 mRNA was detected at all timepoints analyzed and was lowest between 8 and 24 h postfertilization. Thus, differential ADH3 expression may be at least partly responsible for temporal variations in the sensitivity of zebrafish embryos to developmental alcohol exposure.</description><subject>ADH3</subject><subject>ADH3 gene</subject><subject>alcohol dehydrogenase</subject><subject>Alcohol Dehydrogenase - biosynthesis</subject><subject>Alcohol Dehydrogenase - chemistry</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding, Competitive</subject><subject>competitive RT-PCR</subject><subject>Cytosol</subject><subject>Danio rerio</subject><subject>DNA, Complementary - metabolism</subject><subject>Embryo, Nonmammalian - metabolism</subject><subject>ethanol</subject><subject>Freshwater</subject><subject>Glutathione - metabolism</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Larva - metabolism</subject><subject>Liver - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Phylogeny</subject><subject>Protein Isoforms</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA - metabolism</subject><subject>RNA, Messenger - metabolism</subject><subject>teratogenesis</subject><subject>Time Factors</subject><subject>Zebrafish</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0M9LwzAYxvEgis7p1aPkJHrozJs06Xocm79g4EEP4iWk6VsXaZuZdMP993Zs4Ek85fLJA--XkAtgI2BM3RZFsCPOGIykBDggA2A5Sziw9JAMWC8SnsPbCTmN8bNXkKr8mJwASJ6lAAPyMsM11n7ZYNuZmt59LwPG6HxLfUUntfULX9MZLjZl8B_Ymoj0ejJ7FDfUtfQdi2AqFxf0emZa52nA4PzNGTmqTB3xfP8Oyev93ev0MZk_PzxNJ_PEigy6xHCZFdYKoco8K7JxyoU0lleM45jZlFXIubSCC6VKqFApmVrsL8iwUKbMxZBc7WaXwX-tMHa6cdFiXZsW_SrqDECkUqb_QhizXCqe9XC0gzb4GANWehlcY8JGA9Pb3HqbW29z623u_sPlfnlVNFj-8n3fHox3APsOa4dBR-uwtVi6gLbTpXd_bf8A1sKMzA</recordid><startdate>20010907</startdate><enddate>20010907</enddate><creator>Dasmahapatra, Asok K.</creator><creator>Doucet, Herman L.</creator><creator>Bhattacharyya, Champa</creator><creator>Carvan, Michael J.</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>L.G</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20010907</creationdate><title>Developmental Expression of Alcohol Dehydrogenase (ADH3) in Zebrafish (Danio rerio)</title><author>Dasmahapatra, Asok K. ; Doucet, Herman L. ; Bhattacharyya, Champa ; Carvan, Michael J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c371t-a257bcc336d97b784235ac2f02e80c40fe225c32366d1fe6654ce1147eb6ad93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>ADH3</topic><topic>ADH3 gene</topic><topic>alcohol dehydrogenase</topic><topic>Alcohol Dehydrogenase - biosynthesis</topic><topic>Alcohol Dehydrogenase - chemistry</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding, Competitive</topic><topic>competitive RT-PCR</topic><topic>Cytosol</topic><topic>Danio rerio</topic><topic>DNA, Complementary - metabolism</topic><topic>Embryo, Nonmammalian - metabolism</topic><topic>ethanol</topic><topic>Freshwater</topic><topic>Glutathione - metabolism</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Larva - metabolism</topic><topic>Liver - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Phylogeny</topic><topic>Protein Isoforms</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RNA - metabolism</topic><topic>RNA, Messenger - metabolism</topic><topic>teratogenesis</topic><topic>Time Factors</topic><topic>Zebrafish</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dasmahapatra, Asok K.</creatorcontrib><creatorcontrib>Doucet, Herman L.</creatorcontrib><creatorcontrib>Bhattacharyya, Champa</creatorcontrib><creatorcontrib>Carvan, Michael J.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dasmahapatra, Asok K.</au><au>Doucet, Herman L.</au><au>Bhattacharyya, Champa</au><au>Carvan, Michael J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Developmental Expression of Alcohol Dehydrogenase (ADH3) in Zebrafish (Danio rerio)</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2001-09-07</date><risdate>2001</risdate><volume>286</volume><issue>5</issue><spage>1082</spage><epage>1086</epage><pages>1082-1086</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Alcohol dehydrogenase (ADH) is the primary enzyme responsible for metabolism of ethanol to acetaldehyde. One class of ADH has been described in fish, and has been found to be structurally similar to mammalian class III ADH (glutathione-dependent formaldehyde dehydrogenase) but functionally similar to class I ADH (primarily responsible for ethanol metabolism). We have cloned a cDNA by RT-PCR from zebrafish (Danio rerio) liver representing the zebrafish ADH3 gene product, with a coding region of 1131 nucleotides. The deduced amino acid sequences share 90% identity to ADH3 from the marine fish Sparus aurata, and 82 and 81% identity to the mouse and human sequences, respectively. Using a quantitative competitive RT-PCR assay, ADH3 mRNA was detected at all timepoints analyzed and was lowest between 8 and 24 h postfertilization. Thus, differential ADH3 expression may be at least partly responsible for temporal variations in the sensitivity of zebrafish embryos to developmental alcohol exposure.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11527411</pmid><doi>10.1006/bbrc.2001.5511</doi><tpages>5</tpages></addata></record> |
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| subjects | ADH3 ADH3 gene alcohol dehydrogenase Alcohol Dehydrogenase - biosynthesis Alcohol Dehydrogenase - chemistry Amino Acid Sequence Animals Binding, Competitive competitive RT-PCR Cytosol Danio rerio DNA, Complementary - metabolism Embryo, Nonmammalian - metabolism ethanol Freshwater Glutathione - metabolism Humans Kinetics Larva - metabolism Liver - metabolism Molecular Sequence Data Phylogeny Protein Isoforms Reverse Transcriptase Polymerase Chain Reaction RNA - metabolism RNA, Messenger - metabolism teratogenesis Time Factors Zebrafish |
| title | Developmental Expression of Alcohol Dehydrogenase (ADH3) in Zebrafish (Danio rerio) |
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