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PMID: 1829642 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Clinical phenotype of Gaucher disease in relation to properties of mutant glucocerebrosidase in cultured fibroblasts.

Biochimica et biophysica acta ·Vol. 1096 ·No. 4 ·1991-06-05 ·Pages 301-11

Van Weely S, Van Leeuwen MB, Jansen ID, De Bruijn MA, Brouwer-Kelder EM, Schram AW, Sa Miranda MC, Barranger JA, Petersen EM, Goldblatt J

Abstract

We have investigated several parameters of glucocerebrosidase in cultured skin fibroblasts from patients with various clinical phenotypes of Gaucher disease. In this study no strict correlation was found between the clinical manifestations of Gaucher disease and the parameters investigated in fibroblasts. These parameters included the specific activity of the enzyme in extracts towards natural lipid and artificial substrate in the presence of different activators; the enzymic activity per unit of glucocerebrosidase protein; the rate of synthesis of the enzyme and its stability; and the post-translational processing of the enzyme. In addition, the activity in situ of glucocerebrosidase in fibroblasts was investigated using a novel method by analysis of the catabolism of NBD-glucosylceramide in cells that were loaded with bovine serum albumin-lipid complexes. Again, no complete correlation with the clinical phenotype of patients was detectable. Glucocerebrosidase in fibroblasts from most non-neuronopathic (type 1) Gaucher disease patients differs in some aspects from enzyme in cells from patients with neurological forms (types 2 and 3). The stimulation by activator protein and phospholipid is clearly more pronounced in type 1 than in types 2 and 3; the enzymic activity per unit of glucocerebrosidase protein in type 1 is severely reduced in the presence of taurocholate and the amount of glucocerebrosidase appears (near) normal in contrast to the situation in types 2 and 3 Gaucher fibroblasts. However, this distinction was not always consistent; glucocerebrosidase in fibroblasts from some type 1 Gaucher patients, particularly some South African cases, was comparable in properties to enzyme in type 2 and 3 patients.

MeSH Terms
Cathepsin D/metabolism Cells, Cultured Centrifugation, Density Gradient Electrophoresis, Polyacrylamide Gel Fibroblasts/enzymology Gaucher Disease/enzymology,genetics Glucosylceramidase/genetics,metabolism Glucosylceramides/metabolism Humans Immunoblotting Mutation Phenotype Temperature beta-N-Acetylhexosaminidases/metabolism
Chemicals
Glucosylceramides Glucosylceramidase beta-N-Acetylhexosaminidases Cathepsin D
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Van Weely S
E.C. Slater Institute for Biochemical Research, University of Amsterdam, The Netherlands.
Van Leeuwen M B
Jansen I D
De Bruijn M A
Brouwer-Kelder E M
Schram A W
Sa Miranda M C
Barranger J A
Petersen E M
Goldblatt J
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1991-06-05
Pages
301-11
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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