Structure and expression of two kininogen genes in mice

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dc.contributor.author Cardoso, C. C.
dc.contributor.author Garrett, T.
dc.contributor.author Cayla, C.
dc.contributor.author Meneton, P.
dc.contributor.author Pesquero, J. B.
dc.contributor.author Bader, M.
dc.date.accessioned 2016-01-24T12:37:02Z
dc.date.available 2016-01-24T12:37:02Z
dc.date.issued 2004-03-01
dc.identifier http://dx.doi.org/10.1515/BC.2004.025
dc.identifier.citation Biological Chemistry. Berlin: Walter de Gruyter & Co, v. 385, n. 3-4, p. 295-301, 2004.
dc.identifier.issn 1431-6730
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/27668
dc.description.abstract Kininogens serve dual functions by forming a scaffold for the assembly of the protein complex initiating the surfaceactivated blood coagulation cascade and as precursors for the kinin hormones. While rats have three kininogen genes, for mice, cattle, and humans only one gene has been described. Here, we present sequence and expression data of a second mouse kininogen gene. the two genes, kininogenI and kininogenII, are located in close proximity on chromosome 16 in a headtohead arrangement. in liver and kidney, both genes are expressed and for each gene three alternative splice variants are synthesized. Two of them are the expected high and low molecular weight isoforms known from all mammalian kininogens. However, for both genes also a third, hitherto unknown splice variant was detected which lacks part of the high molecular weight mRNA due to splicing from the low molecular weight donor site to alternative splice acceptor sites in exon 10. the physiological functions of the six kininogen isoforms predicted by these findings need to be determined. en
dc.format.extent 295-301
dc.language.iso eng
dc.publisher Walter de Gruyter & Co
dc.relation.ispartof Biological Chemistry
dc.rights Acesso restrito
dc.subject alternative splicing en
dc.subject gene structure en
dc.subject kallikrein-kinin system en
dc.title Structure and expression of two kininogen genes in mice en
dc.type Artigo
dc.contributor.institution Max Delbruck Ctr Mol Med
dc.contributor.institution INSERM
dc.contributor.institution Albany State Univ
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.description.affiliation Max Delbruck Ctr Mol Med, D-13092 Berlin, Germany
dc.description.affiliation INSERM, U367, F-75005 Paris, France
dc.description.affiliation Albany State Univ, Albany, GA 31705 USA
dc.description.affiliation Universidade Federal de São Paulo, Escola Paulista Med, BR-04023062 São Paulo, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Escola Paulista Med, BR-04023062 São Paulo, Brazil
dc.identifier.doi 10.1515/BC.2004.025
dc.description.source Web of Science
dc.identifier.wos WOS:000220848000013



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