Acid lability of the mutated glucosylceramide-beta-glucosidase in a lymphoid cell line from type 2 Gaucher disease.
Lymphoid cell lines from patients with infantile (type-2) and juvenile (type 3) Gaucher disease have been established by Epstein-Barr virus transformation and investigated and compared with the adult phenotype (type 1) with the view to enzymology. The enzymatic defect in glucosylceramide(GlcCer)-beta-glucosidase activity was more severe in type 2 and 3 than in type 1 cells. The mutant GlcCer-beta-glucosidase from our studied type 2 lymphoid cells was profoundly labile at pH 4.0 and 37 degrees C, whereas the residual GlcCer-beta-glucosidase from type 1 and type 3 were stable similar to the normal enzyme. In contrast to the distinct stability of the GlcCer-beta-glucosidases from the three phenotypes, the acid lability of the nonspecific membrane-bound beta-glucosidases from type 1, 2 and 3 were quite similar.
Maret
A
A
Laboratoire de Biochimie, Faculté de Médecine, Toulouse, France.
Salvayre
R
R
Troly
M
M
Douste-Blazy
L
L
D000143:Acids; D000328:Adult; D002460:Cell Line; D004795:Enzyme Stability / Q000187:drug effects; D005776:Gaucher Disease / Q000201:enzymology* / Q000235:genetics; D005962:Glucosylceramidase / Q000187:drug effects / Q000235:genetics*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007231:Infant, Newborn; D008214:Lymphocytes / Q000187:drug effects / Q000201:enzymology*; D008565:Membrane Proteins / Q000187:drug effects; D009154:Mutation; D010641:Phenotype; D013696:Temperature; D001617:beta-Glucosidase / Q000187:drug effects
D000143:Acids; D008565:Membrane Proteins; D001617:beta-Glucosidase; D005962:Glucosylceramidase