File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Genomic structure, alternative splicing and tissue expression of rFrp/sFRP-4, the rat frizzled related protein gene

TitleGenomic structure, alternative splicing and tissue expression of rFrp/sFRP-4, the rat frizzled related protein gene
Authors
KeywordsCysteine rich domain
Netrin-like domain
Ovary
Wnt signaling
Issue Date2005
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/gene
Citation
Gene, 2005, v. 357 n. 1, p. 55-62 How to Cite?
AbstractSecreted frizzled related proteins (sFRP) are regulators of Wnt signaling pathways that play central roles in developmental processes and oncogenesis. Various sFRP genes have been cloned from different tissues and implicated in diverse biological activities. rFrp, the rat homologue of sFRP-4, was initially identified as being upregulated in mutant p53-induced cellular transformation. Here, we report on the isolation of five novel splice variants, rFrp/sFRP-4 II, II, III, IVa and IVb. The complete rFrp/sFRP-4 genomic structure spans over 31 kb covering 9 exons. Except for the variant IVb, which was derived from IVa by alternative polyadenylation signal, variants I to IVa were alternatively spliced to different exons in the 3'end of mRNA and resulted in transcripts with truncated open reading frame. The deduced proteins of the variants had truncated C-termini, however, the two key functional protein domains, the cysteine-rich domain and the netrin-like domain of the isoforms, were not altered. In addition, different transcriptional initiation sites were found with variants II and IV, implying that these variants may be regulated differently from the rFrp/sFRP-4. RT-PCR analysis showed that these splice variants displayed different patterns of tissue-specific expression. Northern blot analysis revealed that the rFrp/sFRP-4 is most abundant in the ovary. Taken together, our findings suggest that alternative splicing of rFrp/sFRP-4 plays a role in regulating tissue-specific expression. The truncated C terminals of rFrp/sFRP-4 variants may confer structural specificity and hence exert different biological functions in different tissues. Characterization of these novel splice variants should help to elucidate the function of the sFRP family gene. © 2005 Elsevier B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/48648
ISSN
2015 Impact Factor: 2.319
2015 SCImago Journal Rankings: 1.043
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYam, JWPen_HK
dc.contributor.authorKoon, WCen_HK
dc.contributor.authorNgan, ESWen_HK
dc.contributor.authorHsiao, WLWen_HK
dc.date.accessioned2008-05-22T04:20:06Z-
dc.date.available2008-05-22T04:20:06Z-
dc.date.issued2005en_HK
dc.identifier.citationGene, 2005, v. 357 n. 1, p. 55-62en_HK
dc.identifier.issn0378-1119en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48648-
dc.description.abstractSecreted frizzled related proteins (sFRP) are regulators of Wnt signaling pathways that play central roles in developmental processes and oncogenesis. Various sFRP genes have been cloned from different tissues and implicated in diverse biological activities. rFrp, the rat homologue of sFRP-4, was initially identified as being upregulated in mutant p53-induced cellular transformation. Here, we report on the isolation of five novel splice variants, rFrp/sFRP-4 II, II, III, IVa and IVb. The complete rFrp/sFRP-4 genomic structure spans over 31 kb covering 9 exons. Except for the variant IVb, which was derived from IVa by alternative polyadenylation signal, variants I to IVa were alternatively spliced to different exons in the 3'end of mRNA and resulted in transcripts with truncated open reading frame. The deduced proteins of the variants had truncated C-termini, however, the two key functional protein domains, the cysteine-rich domain and the netrin-like domain of the isoforms, were not altered. In addition, different transcriptional initiation sites were found with variants II and IV, implying that these variants may be regulated differently from the rFrp/sFRP-4. RT-PCR analysis showed that these splice variants displayed different patterns of tissue-specific expression. Northern blot analysis revealed that the rFrp/sFRP-4 is most abundant in the ovary. Taken together, our findings suggest that alternative splicing of rFrp/sFRP-4 plays a role in regulating tissue-specific expression. The truncated C terminals of rFrp/sFRP-4 variants may confer structural specificity and hence exert different biological functions in different tissues. Characterization of these novel splice variants should help to elucidate the function of the sFRP family gene. © 2005 Elsevier B.V. All rights reserved.en_HK
dc.format.extent215303 bytes-
dc.format.extent3021 bytes-
dc.format.mimetypeapplication/pdf-
dc.format.mimetypetext/plain-
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.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subjectCysteine rich domainen_HK
dc.subjectNetrin-like domainen_HK
dc.subjectOvaryen_HK
dc.subjectWnt signalingen_HK
dc.titleGenomic structure, alternative splicing and tissue expression of rFrp/sFRP-4, the rat frizzled related protein geneen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0378-1119&volume=357&issue=1&spage=55&epage=62&date=2005&atitle=Genomic+structure,+alternative+splicing+and+tissue+expression+of+rFrp/sFRP-4,+the+rat+frizzled+related+protein+geneen_HK
dc.identifier.emailYam, JWP:judyyam@pathology.hku.hken_HK
dc.identifier.emailNgan, ESW:engan@hkucc.hku.hken_HK
dc.identifier.authorityYam, JWP=rp00468en_HK
dc.identifier.authorityNgan, ESW=rp00422en_HK
dc.description.naturepostprinten_HK
dc.identifier.doi10.1016/j.gene.2005.05.025en_HK
dc.identifier.pmid16005582-
dc.identifier.scopuseid_2-s2.0-24644518100en_HK
dc.identifier.hkuros100253-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-24644518100&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume357en_HK
dc.identifier.issue1en_HK
dc.identifier.spage55en_HK
dc.identifier.epage62en_HK
dc.identifier.isiWOS:000232249300007-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridYam, JWP=6603711123-
dc.identifier.scopusauthoridKoon, WC=8727546100-
dc.identifier.scopusauthoridNgan, ESW=22234827500-
dc.identifier.scopusauthoridHsiao, WLW=36795903400-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats