A method for the histochemical localization of digestive enzymes in whole freeze‐substituted larval fish embedded in glycol methacrylate
Identifieur interne : 000821 ( Istex/Corpus ); précédent : 000820; suivant : 000822A method for the histochemical localization of digestive enzymes in whole freeze‐substituted larval fish embedded in glycol methacrylate
Auteurs : Grant W. Vandenberg ; Diane Gagnon ; Shannon L. Scott ; Joël De LanoüeSource :
- Aquaculture Research [ 1355-557X ] ; 2009-04.
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Abstract
In order to study the localization of digestive enzymes in larval walleye (Sander vitreus vitreus), a novel method of low‐temperature processing of whole, unfixed larvae and subsequent embedding in glycol methacrylate (GMA) was developed. Larval walleye aged 2–10 days post hatch were flash‐frozen in liquid nitrogen and transferred into pre‐chilled acetone for 12 h at a temperature of −25 °C. Acetone was gradually replaced with increasing concentrations of GMA resin monomer over a 6‐h period. The polymer (100%) was further allowed to infiltrate the larvae for 36 h. Resin‐embedded larvae were transferred to embedding moulds and polymerized overnight at −25 °C. Four micrometre sections were stained to identify either alkaline phosphatase, non‐specific esterase, aminopeptidase M or dipeptidyl peptidase IV. All enzymes studied were readily detected and accurately localized, and no enzyme diffusion was observed. Therefore, freeze substitution combined with low‐temperature GMA embedding allows the maintenance of excellent tissue morphology and accurate enzyme localization in whole larval walleye specimens from 2 to 10 days post hatch. It is recommended, however, that samples be frozen in pre‐cooled fluorocarbon‐based liquid coolants in order to assure optimal tissue preservation.
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DOI: 10.1111/j.1365-2109.2009.02168.x
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Larval walleye aged 2–10 days post hatch were flash‐frozen in liquid nitrogen and transferred into pre‐chilled acetone for 12 h at a temperature of −25 °C. Acetone was gradually replaced with increasing concentrations of GMA resin monomer over a 6‐h period. The polymer (100%) was further allowed to infiltrate the larvae for 36 h. Resin‐embedded larvae were transferred to embedding moulds and polymerized overnight at −25 °C. Four micrometre sections were stained to identify either alkaline phosphatase, non‐specific esterase, aminopeptidase M or dipeptidyl peptidase IV. All enzymes studied were readily detected and accurately localized, and no enzyme diffusion was observed. Therefore, freeze substitution combined with low‐temperature GMA embedding allows the maintenance of excellent tissue morphology and accurate enzyme localization in whole larval walleye specimens from 2 to 10 days post hatch. 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Journal Compilation © 2009 Blackwell Publishing Ltd</copyright><eventGroup><event type="firstOnline" date="2009-03-03"></event><event type="publishedOnlineFinalForm" date="2009-04-23"></event><event type="xmlConverted" agent="Converter:BPG_TO_WML3G version:2.3.2 mode:FullText source:FullText result:FullText" date="2010-03-16"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-06"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-15"></event></eventGroup><numberingGroup><numbering type="pageFirst" number="818">818</numbering><numbering type="pageLast" number="824">824</numbering></numberingGroup><correspondenceTo><b>Correspondence:</b> Dr G Vandenberg, Département des sciences animales, Pavillon Paul Comtois, Université Laval, QC, Canada G1V 0A6. E‐mail: <email normalForm="grant.vandenberg@fsaa.ulaval.ca">grant.vandenberg@fsaa.ulaval.ca</email></correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:ARE.ARE2168.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="9"></count><count type="tableTotal" number="1"></count><count type="formulaTotal" number="0"></count><count type="referenceTotal" number="32"></count><count type="wordTotal" number="4222"></count><count type="linksCrossRef" number="29"></count></countGroup><titleGroup><title type="main">A method for the histochemical localization of digestive enzymes in whole freeze‐substituted larval fish embedded in glycol methacrylate</title><title type="shortAuthors">G W Vandenberg <i>et al.</i></title><title type="short">Freeze‐substitution of whole fish larvae</title></titleGroup><creators><creator creatorRole="author" xml:id="cr1" affiliationRef="#a1"><personName><givenNames>Grant W</givenNames><familyName>Vandenberg</familyName></personName></creator><creator creatorRole="author" xml:id="cr2" affiliationRef="#a1"><personName><givenNames>Diane</givenNames><familyName>Gagnon</familyName></personName></creator><creator creatorRole="author" xml:id="cr3" affiliationRef="#a1" noteRef="#fn1"><personName><givenNames>Shannon L</givenNames><familyName>Scott</familyName></personName></creator><creator creatorRole="author" xml:id="cr4" affiliationRef="#a1"><personName><givenNames>Joël</givenNames><familyName>De LaNoüe</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="a1" countryCode="CA"><unparsedAffiliation>Groupe de recherche en recyclage biologique et aquiculture. Département des sciences animales, Université Laval, QC, Canada G1V 0A6</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en"><keyword xml:id="k1">enzyme</keyword><keyword xml:id="k2">histochemistry</keyword><keyword xml:id="k3">freeze substitution</keyword><keyword xml:id="k4">fish larvae</keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>In order to study the localization of digestive enzymes in larval walleye (<i>Sander vitreus</i> vitreus), a novel method of low‐temperature processing of whole, unfixed larvae and subsequent embedding in glycol methacrylate (GMA) was developed. Larval walleye aged 2–10 days post hatch were flash‐frozen in liquid nitrogen and transferred into pre‐chilled acetone for 12 h at a temperature of −25 °C. Acetone was gradually replaced with increasing concentrations of GMA resin monomer over a 6‐h period. The polymer (100%) was further allowed to infiltrate the larvae for 36 h. Resin‐embedded larvae were transferred to embedding moulds and polymerized overnight at −25 °C. Four micrometre sections were stained to identify either alkaline phosphatase, non‐specific esterase, aminopeptidase M or dipeptidyl peptidase IV. All enzymes studied were readily detected and accurately localized, and no enzyme diffusion was observed. Therefore, freeze substitution combined with low‐temperature GMA embedding allows the maintenance of excellent tissue morphology and accurate enzyme localization in whole larval walleye specimens from 2 to 10 days post hatch. It is recommended, however, that samples be frozen in pre‐cooled fluorocarbon‐based liquid coolants in order to assure optimal tissue preservation.</p></abstract></abstractGroup></contentMeta><noteGroup><note xml:id="fn1" numbered="no"><p><sup>*</sup><b>Present address:</b> S L Scott, Agriculture and Agri‐Food Canada, PO Box 1000A, RR#3, Brandon, MB, Canada R7A 5Y3</p></note></noteGroup></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>A method for the histochemical localization of digestive enzymes in whole freeze‐substituted larval fish embedded in glycol methacrylate</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Freeze‐substitution of whole fish larvae</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>A method for the histochemical localization of digestive enzymes in whole freeze‐substituted larval fish embedded in glycol methacrylate</title></titleInfo><name type="personal"><namePart type="given">Grant W</namePart><namePart type="family">Vandenberg</namePart><affiliation>Groupe de recherche en recyclage biologique et aquiculture. 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Département des sciences animales, Université Laval, QC, Canada G1V 0A6</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><place><placeTerm type="text">Oxford, UK</placeTerm></place><dateIssued encoding="w3cdtf">2009-04</dateIssued><copyrightDate encoding="w3cdtf">2009</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">9</extent><extent unit="tables">1</extent><extent unit="references">32</extent><extent unit="words">4222</extent></physicalDescription><abstract lang="en">In order to study the localization of digestive enzymes in larval walleye (Sander vitreus vitreus), a novel method of low‐temperature processing of whole, unfixed larvae and subsequent embedding in glycol methacrylate (GMA) was developed. Larval walleye aged 2–10 days post hatch were flash‐frozen in liquid nitrogen and transferred into pre‐chilled acetone for 12 h at a temperature of −25 °C. Acetone was gradually replaced with increasing concentrations of GMA resin monomer over a 6‐h period. The polymer (100%) was further allowed to infiltrate the larvae for 36 h. Resin‐embedded larvae were transferred to embedding moulds and polymerized overnight at −25 °C. Four micrometre sections were stained to identify either alkaline phosphatase, non‐specific esterase, aminopeptidase M or dipeptidyl peptidase IV. All enzymes studied were readily detected and accurately localized, and no enzyme diffusion was observed. Therefore, freeze substitution combined with low‐temperature GMA embedding allows the maintenance of excellent tissue morphology and accurate enzyme localization in whole larval walleye specimens from 2 to 10 days post hatch. It is recommended, however, that samples be frozen in pre‐cooled fluorocarbon‐based liquid coolants in order to assure optimal tissue preservation.</abstract><subject lang="en"><genre>keywords</genre><topic>enzyme</topic><topic>histochemistry</topic><topic>freeze substitution</topic><topic>fish larvae</topic></subject><relatedItem type="host"><titleInfo><title>Aquaculture Research</title></titleInfo><genre type="journal">journal</genre><identifier type="ISSN">1355-557X</identifier><identifier type="eISSN">1365-2109</identifier><identifier type="DOI">10.1111/(ISSN)1365-2109</identifier><identifier type="PublisherID">ARE</identifier><part><date>2009</date><detail type="volume"><caption>vol.</caption><number>40</number></detail><detail type="issue"><caption>no.</caption><number>7</number></detail><extent unit="pages"><start>818</start><end>824</end><total>7</total></extent></part></relatedItem><identifier type="istex">69CE395D78143037094B20FADBD8302DAC469DFE</identifier><identifier type="DOI">10.1111/j.1365-2109.2009.02168.x</identifier><identifier type="ArticleID">ARE2168</identifier><accessCondition type="use and reproduction" contentType="copyright">© 2009 The Authors. 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