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Article: Characterization of a novel cellular retinoic acid/retinol binding protein from shrimp: Expression of the recombinant protein for immunohistochemical detection and binding assay

TitleCharacterization of a novel cellular retinoic acid/retinol binding protein from shrimp: Expression of the recombinant protein for immunohistochemical detection and binding assay
Authors
KeywordsReproduction
Retinoic acid binding protein
Shrimp
Issue Date2002
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/gene
Citation
Gene, 2002, v. 288 n. 1-2, p. 77-84 How to Cite?
AbstractMembers of the cellular retinoic acid (CRABP) and retinol binding (CRBP) proteins family are involved in the metabolic pathways of retinoic acid (RA) and retinal respectively. The objective of this study is to determine whether such proteins are present in crustaceans. We report here the cloning and isolation of a novel complementary DNA (cDNA) that showed characteristics of the CRABP/CRBP from the ovary and eyestalk of the shrimp. The cDNA is 0.9 Kb in size and the deduced shrimp protein is encoded for a protein of 14 kDa. Although it shows high amino acids sequence similarity to both the vertebrate and invertebrate CRABP, some conserved amino acids identified in other CRABPs were not found in MeCRABP. MeCRABP is expressed in the ovary, eyestalk, testis, epidermis and early larvae. The presence of MeCRABP in early larval stages suggests that the protein may be involved in the early larval development. Recombinant MeCRABP was produced and used to generate a polyclonal antibody. In the immunohistochemical detection study, anti-rCRABP antibody recognized the presence of CRABP in several cell types of the eyestalk as well as the smaller oocytes of the ovary. Although MeCRABP messenger RNA transcripts can be detected in the ovary throughout the ovarian maturation period, CRABP was detected only in the primary oocytes of the ovary. The results suggest that CRABP transcripts in the mature ovary are not translated and may be supplied to the oocyte as maternal messages. The binding property of the recombinant MeCRABP was also tested by a fluorometeric method. The result indicates that rMeCRABP binds to both RA and retinal with similar affinity. This study represents the first cloning and characterization of a cDNA that belongs to a member of retinoid/fatty acid binding protein family in crustaceans. © 2002 Elsevier Science B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/84645
ISSN
2015 Impact Factor: 2.319
2015 SCImago Journal Rankings: 1.043
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorGu, PLen_HK
dc.contributor.authorGunawardene, YINSilvaen_HK
dc.contributor.authorChow, BCen_HK
dc.contributor.authorHe, JGen_HK
dc.contributor.authorChan, SMen_HK
dc.date.accessioned2010-09-06T08:55:28Z-
dc.date.available2010-09-06T08:55:28Z-
dc.date.issued2002en_HK
dc.identifier.citationGene, 2002, v. 288 n. 1-2, p. 77-84en_HK
dc.identifier.issn0378-1119en_HK
dc.identifier.urihttp://hdl.handle.net/10722/84645-
dc.description.abstractMembers of the cellular retinoic acid (CRABP) and retinol binding (CRBP) proteins family are involved in the metabolic pathways of retinoic acid (RA) and retinal respectively. The objective of this study is to determine whether such proteins are present in crustaceans. We report here the cloning and isolation of a novel complementary DNA (cDNA) that showed characteristics of the CRABP/CRBP from the ovary and eyestalk of the shrimp. The cDNA is 0.9 Kb in size and the deduced shrimp protein is encoded for a protein of 14 kDa. Although it shows high amino acids sequence similarity to both the vertebrate and invertebrate CRABP, some conserved amino acids identified in other CRABPs were not found in MeCRABP. MeCRABP is expressed in the ovary, eyestalk, testis, epidermis and early larvae. The presence of MeCRABP in early larval stages suggests that the protein may be involved in the early larval development. Recombinant MeCRABP was produced and used to generate a polyclonal antibody. In the immunohistochemical detection study, anti-rCRABP antibody recognized the presence of CRABP in several cell types of the eyestalk as well as the smaller oocytes of the ovary. Although MeCRABP messenger RNA transcripts can be detected in the ovary throughout the ovarian maturation period, CRABP was detected only in the primary oocytes of the ovary. The results suggest that CRABP transcripts in the mature ovary are not translated and may be supplied to the oocyte as maternal messages. The binding property of the recombinant MeCRABP was also tested by a fluorometeric method. The result indicates that rMeCRABP binds to both RA and retinal with similar affinity. This study represents the first cloning and characterization of a cDNA that belongs to a member of retinoid/fatty acid binding protein family in crustaceans. © 2002 Elsevier Science B.V. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/geneen_HK
dc.relation.ispartofGeneen_HK
dc.rightsGene. Copyright © Elsevier BV.en_HK
dc.subjectReproductionen_HK
dc.subjectRetinoic acid binding proteinen_HK
dc.subjectShrimpen_HK
dc.titleCharacterization of a novel cellular retinoic acid/retinol binding protein from shrimp: Expression of the recombinant protein for immunohistochemical detection and binding assayen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0378-1119&volume=288&spage=77&epage=84&date=2002&atitle=Characterization+of+a+novel+cellular+retinoic+acid/retinol+binding+protein+from+shrimp:+expression+of+the+recombinant+protein+for+immunohistochemical+detection+and+binding+assayen_HK
dc.identifier.emailChow, BC: bkcc@hku.hken_HK
dc.identifier.authorityChow, BC=rp00681en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0378-1119(02)00430-4en_HK
dc.identifier.pmid12034496-
dc.identifier.scopuseid_2-s2.0-0037123361en_HK
dc.identifier.hkuros66134en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0037123361&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume288en_HK
dc.identifier.issue1-2en_HK
dc.identifier.spage77en_HK
dc.identifier.epage84en_HK
dc.identifier.isiWOS:000176373600009-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridGu, PL=8943600800en_HK
dc.identifier.scopusauthoridGunawardene, YINSilva=6506151323en_HK
dc.identifier.scopusauthoridChow, BC=7102826193en_HK
dc.identifier.scopusauthoridHe, JG=35487616500en_HK
dc.identifier.scopusauthoridChan, SM=7404255669en_HK

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