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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Molecular cloning, chromosomal assignment, and expression of the mouse aspartylglucosaminidase gene.

Aspartylglucosaminidase (AGA) is a lysosomal enzyme, the deficiency of which leads to human lysosomal storage disease aspartylglucosaminuria. Here, we describe isolation, chromosomal location, genomic structure, and tissue-specific expression of the mouse Aga gene as well as the intracellular processing of the mouse Aga polypeptide and compare these characteristics to human AGA. The mouse Aga gene was localized to the central area of the B region of chromosome 8, which represents the synteny group in the human chromosome 4q telomeric region where the human AGA gene is located. The mouse gene spans an 11-kb genomic region and contains nine exons and eight introns, which is analogous to the human gene. Furthermore, the exon-intron boundaries of the mouse and human genes are identically positioned. The nucleotide sequence identity of the cDNA and deduced amino acid sequence identity of the protein are 84.4 and 82.4%, respectively. However, the mouse Aga cDNA contains untranslated regions that are shorter than those in the human cDNA, and only one 1.2-kb mRNA transcript is produced in mouse versus two transcripts in human. Expression of the mouse Aga cDNA in COS-1 cells showed that the mouse Aga polypeptide was processed similarly to the human counterpart.[1]

References

  1. Molecular cloning, chromosomal assignment, and expression of the mouse aspartylglucosaminidase gene. Tenhunen, K., Laan, M., Manninen, T., Palotie, A., Peltonen, L., Jalanko, A. Genomics (1995) [Pubmed]
 
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