Murine α- N -Acetylgalactosaminidase: Isolation and Expression of a Full-Length cDNA and Genomic Organization: Further Evidence of an α-Galactosidase Gene Family
Identifieur interne : 00B457 ( Main/Curation ); précédent : 00B456; suivant : 00B458Murine α- N -Acetylgalactosaminidase: Isolation and Expression of a Full-Length cDNA and Genomic Organization: Further Evidence of an α-Galactosidase Gene Family
Auteurs : Anne M. Wang ; Yiannis A. Ioannou ; Ken M. Zeidner ; Robert J. DesnickSource :
- Molecular Genetics and Metabolism [ 1096-7192 ] ; 1998.
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Abstract
Recent characterization of the human sequences encoding two lysosomal hydrolases, α-galactosidase A (α-Gal A) and α-N-acetylgalactosaminidase (α-GalNAc) revealed that these two enzymes with distinct enzymatic activities shared about 50% overall amino acid identity and that their genomic sequences had a conserved common gene structure. These findings suggested that these genes, which are located on different chromosomes, arose by duplication and divergence from a common ancestral gene. To further compare this α-galactosidase gene family, the murine α-GalNAc cDNA and genomic sequences were isolated and characterized. The full-length cDNA contained an open-reading frame of 1245 bp encoding a 415 amino acid polypeptide and had 5′ and 3′ untranslated regions of 94 and 333 bp, respectively. The coding region had 81% nucleotide and 81.9% amino acid identities with those of the corresponding human α-GalNAc sequence. Northern analysis revealed a single transcript of ∼1.9 kb. The functional integrity of the cDNA was demonstrated by transient expression in COS-1 cells. The murine α-GalNAc genomic sequence spanned ∼9 kb and was identical in structure with the human α-GalNAc gene with eight introns interrupting the coding sequence at identical positions. In addition, the deduced amino acid sequence of the murine α-GalNAc gene was highly homologous with α-GalNAc and α-Gal A genes from other species providing further support for a common evolutionary ancestor of the α-galactosidase gene family. The availability of the murine gene will permit additional evolutionary comparisons, structure/function analyses, and the generation of mice with α-GalNAc deficiency by gene targeting.
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DOI: 10.1006/mgme.1998.2750
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Anne M. Wang<affiliation><wicri:noCountry code="subField">10029</wicri:noCountry></affiliation><affiliation><wicri:noCountry code="subField">10029</wicri:noCountry></affiliation><affiliation><wicri:noCountry code="subField">10029</wicri:noCountry></affiliation><affiliation><wicri:noCountry code="subField">10029</wicri:noCountry></affiliation>Le document en format XML
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Desnick</name><affiliation><wicri:noCountry code="subField">10029</wicri:noCountry></affiliation></author></analytic><monogr></monogr><series><title level="j">Molecular Genetics and Metabolism</title><title level="j" type="abbrev">YMGME</title><idno type="ISSN">1096-7192</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998">1998</date><biblScope unit="volume">65</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="165">165</biblScope><biblScope unit="page" to="173">173</biblScope></imprint><idno type="ISSN">1096-7192</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1096-7192</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Fabry disease</term><term>Schindler disease</term><term>cloning</term><term>gene targeting</term><term>α-N-acetylgalactosaminidase</term><term>α-galactosidase</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Recent characterization of the human sequences encoding two lysosomal hydrolases, α-galactosidase A (α-Gal A) and α-N-acetylgalactosaminidase (α-GalNAc) revealed that these two enzymes with distinct enzymatic activities shared about 50% overall amino acid identity and that their genomic sequences had a conserved common gene structure. These findings suggested that these genes, which are located on different chromosomes, arose by duplication and divergence from a common ancestral gene. To further compare this α-galactosidase gene family, the murine α-GalNAc cDNA and genomic sequences were isolated and characterized. The full-length cDNA contained an open-reading frame of 1245 bp encoding a 415 amino acid polypeptide and had 5′ and 3′ untranslated regions of 94 and 333 bp, respectively. The coding region had 81% nucleotide and 81.9% amino acid identities with those of the corresponding human α-GalNAc sequence. Northern analysis revealed a single transcript of ∼1.9 kb. The functional integrity of the cDNA was demonstrated by transient expression in COS-1 cells. The murine α-GalNAc genomic sequence spanned ∼9 kb and was identical in structure with the human α-GalNAc gene with eight introns interrupting the coding sequence at identical positions. In addition, the deduced amino acid sequence of the murine α-GalNAc gene was highly homologous with α-GalNAc and α-Gal A genes from other species providing further support for a common evolutionary ancestor of the α-galactosidase gene family. The availability of the murine gene will permit additional evolutionary comparisons, structure/function analyses, and the generation of mice with α-GalNAc deficiency by gene targeting.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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