Immunological and catalytic quantitation of splenic glucocerebrosidase from the three clinical forms of Gaucher disease.
The enzymatic activity of glucocerebrosidase in splenic extracts of the adult nonneurological form of Gaucher disease (type I) was 15% +/- 7% of normal, and the titer of enzyme cross-reacting material (ECRM) in these spleens was 54% +/- 9% of normal. The titer of ECRM in splenic extracts of tissues obtained from patients with the neurological forms of Gaucher disease (types II and III) was essentially the same as in type I Gaucher spleens (59% +/- 10% of normal), but the measurable catalytic activity of glucocerebrosidase in these spleens was substantially lower than that found in type I Gaucher spleens (2.3% +/- 0.6% of normal). Thus, the attentuated glucocerebrosidase activity in spleens from all three forms of Gaucher disease appears to stem from a structurally mutated enzyme that is altered in its catalytic efficiency and possibly in its antigenic expression.
D000293:Adolescent; D000328:Adult; D000818:Animals; D002384:Catalysis; D002648:Child; D003429:Cross Reactions; D005260:Female; D005776:Gaucher Disease / Q000201:enzymology* / Q000235:genetics; D005959:Glucosidases / Q000235:genetics*; D005962:Glucosylceramidase / Q000235:genetics* / Q000276:immunology; D006801:Humans; D007106:Immune Sera; D007118:Immunoassay; D007223:Infant; D008297:Male; D008875:Middle Aged; D009154:Mutation; D011817:Rabbits / Q000276:immunology; D013154:Spleen / Q000201:enzymology*
D007106:Immune Sera; D005959:Glucosidases; D005962:Glucosylceramidase