The University of Tokyo · Medicine
Professor Shoji Tsuji's research lab specializes in molecular genetics and enzymology, focusing on the identification and functional characterization of disease-causing mutations in lysosomal enzymes, particularly glucocerebrosidase. The lab investigates the genetic basis of Gaucher disease subtypes, especially type 2 and type 3, using molecular cloning, sequencing, and restriction fragment length polymorphism (RFLP) analysis to link specific mutations to clinical phenotypes. Their work has led to the discovery of key pathogenic mutations, such as the L444P substitution and the N370S mutation, providing critical insights into genotype-phenotype correlations and enabling molecular diagnosis. The lab also employs functional assays and allele-specific detection methods to validate the pathogenicity of mutations and assess their impact on enzyme activity.
Figures are computed from collected data and may differ slightly.
To search for a genetic marker for type 2 Gaucher's disease (acute neuronopathic form), we compared the nucleotide sequence of a cloned glucocerebrosidase gene from a patient with Gaucher's disease with a normal gene. We found only a single base substitution (T----C) in exon X. This mutation results in the substitution of proline for leucine in position number 444 and produces a new cleavage site for the NciI restriction endonuclease. We analyzed NciI enzymatic digests of genomic DNA from 20 pat
Nucleotide sequence analysis of a genomic clone from an Ashkenazic Jewish patient with type 1 Gaucher disease revealed a single-base mutation (adenosine to guanosine transition) in exon 9 of the glucocerebrosidase gene. This change results in the amino acid substitution of serine for asparagine. Transient expression studies following oligonucleotide-directed mutagenesis of the normal cDNA confirmed that the mutation results in loss of glucocerebrosidase activity. Allele-specific hybridization wi
Open papers in the app to read, cite, and organize with AI.
