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Báo cáo khoa học: Molecular characterization, phylogenetic relationships, and developmental expression patterns of prion genes in zebrafish (Danio rerio)

Prion diseases are characterized by the accumulation of a pathogenic mis-folded form of a prion protein (PrP) encoded by the Prnpgene in humans. In the present study in zebrafish, two transcripts and the corresponding genes encoding prion proteins, PrP1 and PrP2, related to human PrP have been characterized with a relatively divergent deduced amino acid sequence, but a well preserved overall organization of structural prion pro-tein motifs. Whole-mount in situ hybridization analysis performed during embryonic and larval development showed a high level of PrP1 mRNA spatially restricted to the anterior floor-plate of the central nervous system and in ganglia. . | iFEBS Journal Molecular characterization phylogenetic relationships and developmental expression patterns of prion genes in zebrafish Danio rerio Emmanuelle Cotto1 2 Michele Andre1 Jean Forgue1 Herve J Fleury2 and Patrick J Babin1 1 Laboratoire Genomique et Physiologie des Poissons UMR 1067 NUAGE INRA-IFREMER Universite Bordeaux 1 Talence France 2 Laboratoire Virologie Systematique et Moleculaire E.A. 2968 Universite Victor Segalen Bordeaux 2 Bordeaux France Keywords brain duplicated genes prion PrP zebrafish Correspondence P.J. Babin Laboratoire Genomique et Physiologie des Poissons UMR 1067 NUAGE INRA-IFREMER Universite Bordeaux I Avenue des Facultes Bat. B2 33405 Talence cedex France Fax 33 5 4000 8915 Tel 33 5 4000 8776 E-mail p.babin@gpp.u-bordeaux1.fr Note The sequence data presented here have been deposited with the GenBank EMBL Data Libraries under the accession numbers AJ850286 for zebrafish PrP1 and AJ620614 for zebrafish PrP2 mRNAs. Received 19 July 2004 revised 12 November 2004 accepted 18 November 2004 doi 10.1111 j.1742-4658.2004.04492.x Prion diseases are characterized by the accumulation of a pathogenic misfolded form of a prion protein PrP encoded by the Prnp gene in humans. In the present study in zebrafish two transcripts and the corresponding genes encoding prion proteins PrP1 and PrP2 related to human PrP have been characterized with a relatively divergent deduced amino acid sequence but a well preserved overall organization of structural prion protein motifs. Whole-mount in situ hybridization analysis performed during embryonic and larval development showed a high level of PrP1 mRNA spatially restricted to the anterior floor-plate of the central nervous system and in ganglia. Transcripts of prp2 were detected in embryonic cells from the mid-blastula transition to the end of the segmentation period. From 24 h postfertilization up to larval stages prp2 transcripts were localized in distinct anatomical structures including a major expression in .