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The biosynthesis and maturation of glucocerebrosidase were studied in fibroblasts from patients with the neurological and non-neurological forms of Gaucher disease and in control cells. In control fibroblasts the precursor of glucocerebrosidase (62-63 kDa), observed after a short pulse with [35S]methionine, was converted during the chase period to a 66-kDa intermediate form and, finally, to the 59-kDa mature protein. In fibroblasts from patients with the non-neurological phenotype of Gaucher disease (type 1) the same biosynthetic forms were seen as in control fibroblasts. These biosynthetic forms correspond to the three-banded pattern seen in control and Gaucher type 1 fibroblast extracts analysed by the immunoblotting procedure, or after electrophoresis and fluorography of extracts of such fibroblasts cultured for 5 days with [14C]leucine. The 59-kDa protein seen in type 1 fibroblasts was unstable and disappeared after a prolonged chase; this disappearance was not observed when the cells were grown in the presence of leupeptin. In fibroblasts from patients with the neurological forms of Gaucher disease (types 2 and 3) the 62.5-kDa precursor of glucocerebrosidase was present in near-normal amounts after a short pulse, but the 59-kDa form was not detected even when cells were cultured with leupeptin. These results are in accordance with the absence of the 59-kDa band in immunoblots of types 2 and 3 fibroblast extracts. Culturing of type 1, type 2 and type 3 Gaucher fibroblasts in the presence of leupeptin led to an increase in the activity of glucocerebrosidase.
L M Jonsson, and
G J Murray, and
S H Sorrell, and
A Strijland, and
J F Aerts, and
E I Ginns, and
J A Barranger, and
J M Tager, and
A W Schram
July 1979,
American journal of human genetics,
L M Jonsson, and
G J Murray, and
S H Sorrell, and
A Strijland, and
J F Aerts, and
E I Ginns, and
J A Barranger, and
J M Tager, and
A W Schram
January 1984,
Human genetics,
L M Jonsson, and
G J Murray, and
S H Sorrell, and
A Strijland, and
J F Aerts, and
E I Ginns, and
J A Barranger, and
J M Tager, and
A W Schram
March 2013,
Chemistry & biology,
L M Jonsson, and
G J Murray, and
S H Sorrell, and
A Strijland, and
J F Aerts, and
E I Ginns, and
J A Barranger, and
J M Tager, and
A W Schram
January 1996,
Human mutation,
L M Jonsson, and
G J Murray, and
S H Sorrell, and
A Strijland, and
J F Aerts, and
E I Ginns, and
J A Barranger, and
J M Tager, and
A W Schram
June 1986,
Molecular biology & medicine,
L M Jonsson, and
G J Murray, and
S H Sorrell, and
A Strijland, and
J F Aerts, and
E I Ginns, and
J A Barranger, and
J M Tager, and
A W Schram
November 1994,
Molecular medicine (Cambridge, Mass.),
L M Jonsson, and
G J Murray, and
S H Sorrell, and
A Strijland, and
J F Aerts, and
E I Ginns, and
J A Barranger, and
J M Tager, and
A W Schram
June 1991,
Biochimica et biophysica acta,
L M Jonsson, and
G J Murray, and
S H Sorrell, and
A Strijland, and
J F Aerts, and
E I Ginns, and
J A Barranger, and
J M Tager, and
A W Schram
October 1986,
Proceedings of the National Academy of Sciences of the United States of America,
L M Jonsson, and
G J Murray, and
S H Sorrell, and
A Strijland, and
J F Aerts, and
E I Ginns, and
J A Barranger, and
J M Tager, and
A W Schram
September 2006,
The FEBS journal,
L M Jonsson, and
G J Murray, and
S H Sorrell, and
A Strijland, and
J F Aerts, and
E I Ginns, and
J A Barranger, and
J M Tager, and
A W Schram
December 1996,
Biochemical and molecular medicine,
