Acid lability of the mutated glucosylceramide-beta-glucosidase in a lymphoid cell line from type 2 Gaucher disease

Enzyme. 1990;43(2):99-106. doi: 10.1159/000468712.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acids
  • Adult
  • Cell Line
  • Enzyme Stability / drug effects
  • Gaucher Disease / enzymology*
  • Gaucher Disease / genetics
  • Glucosylceramidase / drug effects
  • Glucosylceramidase / genetics*
  • Humans
  • Hydrogen-Ion Concentration
  • Infant, Newborn
  • Lymphocytes / drug effects
  • Lymphocytes / enzymology*
  • Membrane Proteins / drug effects
  • Mutation
  • Phenotype
  • Temperature
  • beta-Glucosidase / drug effects

Substances

  • Acids
  • Membrane Proteins
  • beta-Glucosidase
  • Glucosylceramidase