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Article: Function and cellular localization of farnesoic acid O-methyltransferase (FAMeT) in the shrimp, Metapenaeus ensis

TitleFunction and cellular localization of farnesoic acid O-methyltransferase (FAMeT) in the shrimp, Metapenaeus ensis
Authors
KeywordsFarnesoic acid O-methyltransferase
Juvenile hormone
Methyl farnesoate
Neuropeptides
Shrimp
Issue Date2002
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJB
Citation
European Journal Of Biochemistry, 2002, v. 269 n. 14, p. 3587-3595 How to Cite?
AbstractThe isoprenoid methyl farnesoate (MF) has been implicated in the regulation of crustacean development and reproduction in conjunction with eyestalk molt inhibiting hormones and ecdysteroids. Farnesoic acid O-methyl-transferase (FAMeT) catalyzes the methylation of farnesoic acid (FA) to produce MF in the terminal step of MF synthesis. We have previously cloned and characterized the shrimp FAMeT. In the present study, recombinant FAMeT (rFAMeT) was produced for bioassay and antiserum generation. FAMeT is widely distributed in shrimp tissues with the highest concentration observed in the ventral nerve cord. Interestingly, an additional larger protein in the eyestalk also showed immunoreactivity to anti-FAMeT serum. FAMeT was localized in the neurosecretory cells of the X-organ-sinus gland complex of the eyestalk. As shown by RT-PCR, FAMeT mRNA is constitutively expressed throughout the molt cycle in the eyestalk and the ventral nerve cord. To show that our cloned gene product had FAMeT activity, we demonstrated that expressed rFAMeT gene product catalyzed the conversion of FA to MF in a radiochemical assay. The ubiquitous distribution of FAMeT suggests that this enzyme is involved in physiological processes in addition to gametogenesis, oocyte maturation and development and metamorphosis of the shrimp. We hypothesize that FAMeT directly or indirectly (through MF) modulates the reproduction and growth of crustaceans by interacting with the eyestalk neuropeptides as a consequence of its presence in the neurosecretory cells of the X-organ-sinus gland.
Persistent Identifierhttp://hdl.handle.net/10722/84937
ISSN
2006 Impact Factor: 3.579
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSilva Gunawardene, YINen_HK
dc.contributor.authorTobe, SSen_HK
dc.contributor.authorBendena, WGen_HK
dc.contributor.authorChow, BKCen_HK
dc.contributor.authorYagi, KJen_HK
dc.contributor.authorChan, SMen_HK
dc.date.accessioned2010-09-06T08:58:51Z-
dc.date.available2010-09-06T08:58:51Z-
dc.date.issued2002en_HK
dc.identifier.citationEuropean Journal Of Biochemistry, 2002, v. 269 n. 14, p. 3587-3595en_HK
dc.identifier.issn0014-2956en_HK
dc.identifier.urihttp://hdl.handle.net/10722/84937-
dc.description.abstractThe isoprenoid methyl farnesoate (MF) has been implicated in the regulation of crustacean development and reproduction in conjunction with eyestalk molt inhibiting hormones and ecdysteroids. Farnesoic acid O-methyl-transferase (FAMeT) catalyzes the methylation of farnesoic acid (FA) to produce MF in the terminal step of MF synthesis. We have previously cloned and characterized the shrimp FAMeT. In the present study, recombinant FAMeT (rFAMeT) was produced for bioassay and antiserum generation. FAMeT is widely distributed in shrimp tissues with the highest concentration observed in the ventral nerve cord. Interestingly, an additional larger protein in the eyestalk also showed immunoreactivity to anti-FAMeT serum. FAMeT was localized in the neurosecretory cells of the X-organ-sinus gland complex of the eyestalk. As shown by RT-PCR, FAMeT mRNA is constitutively expressed throughout the molt cycle in the eyestalk and the ventral nerve cord. To show that our cloned gene product had FAMeT activity, we demonstrated that expressed rFAMeT gene product catalyzed the conversion of FA to MF in a radiochemical assay. The ubiquitous distribution of FAMeT suggests that this enzyme is involved in physiological processes in addition to gametogenesis, oocyte maturation and development and metamorphosis of the shrimp. We hypothesize that FAMeT directly or indirectly (through MF) modulates the reproduction and growth of crustaceans by interacting with the eyestalk neuropeptides as a consequence of its presence in the neurosecretory cells of the X-organ-sinus gland.en_HK
dc.languageengen_HK
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJBen_HK
dc.relation.ispartofEuropean Journal of Biochemistryen_HK
dc.rightsEuropean Journal of Biochemistry. Copyright © Blackwell Publishing Ltd.en_HK
dc.subjectFarnesoic acid O-methyltransferaseen_HK
dc.subjectJuvenile hormoneen_HK
dc.subjectMethyl farnesoateen_HK
dc.subjectNeuropeptidesen_HK
dc.subjectShrimpen_HK
dc.titleFunction and cellular localization of farnesoic acid O-methyltransferase (FAMeT) in the shrimp, Metapenaeus ensisen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0014-2956&volume=269&spage=3587&epage=3595&date=2002&atitle=Function+and+cellular+localization+of+farnesoic+acid+O-methyltransferase+(FAMeT)+in+the+shrimp,+Metapenaeus+ensisen_HK
dc.identifier.emailChow, BKC: bkcc@hku.hken_HK
dc.identifier.authorityChow, BKC=rp00681en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1046/j.1432-1033.2002.03048.xen_HK
dc.identifier.pmid12135499en_HK
dc.identifier.scopuseid_2-s2.0-0036373918en_HK
dc.identifier.hkuros75608en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036373918&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume269en_HK
dc.identifier.issue14en_HK
dc.identifier.spage3587en_HK
dc.identifier.epage3595en_HK
dc.identifier.isiWOS:000176920600028-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridSilva Gunawardene, YIN=6507561163en_HK
dc.identifier.scopusauthoridTobe, SS=7102112085en_HK
dc.identifier.scopusauthoridBendena, WG=7004842527en_HK
dc.identifier.scopusauthoridChow, BKC=7102826193en_HK
dc.identifier.scopusauthoridYagi, KJ=9277545000en_HK
dc.identifier.scopusauthoridChan, SM=7404255669en_HK

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