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Molecular defect in processing alpha-fucosidase in fucosidosis.
In normal human skin fibroblasts, an enzymatically active 53,000-dalton form of alpha-fucosidase is processed to a 50,000-dalton mature form. Endoglycosidase-H treatment of [35S]methionine pulse-chase labelled material immunoprecipated with a polyclonal antibody to alpha-L-fucosidase (Andrews-Smith & Alhadeff, Biochim. Biophys. Acta 715: 90-96 (1982)) indicated the removal of a single N-linked oligosaccharide unit from both precursor and mature form of alpha-L-fucosidase. Tunicamycin pretreatment of normal fibroblasts indicated that no other N-linked oligosaccharide units were present. Studies on fibroblasts from patients with less than 5% of normal alpha-L-fucosidase activity (fucosidosis) showed 8 of 11 patients synthesized no detectable alpha-fucosidase protein whereas 2 synthesized normal amounts of 53,000 dalton precursor, none of the mature 50,000 dalton form was detectable and one contained small amounts of cross-reacting material. This is the first evidence for processing of alpha-L-fucosidase in cells and the first precise evidence of a molecular defect in fucosidosis.
PMID: 4074382 [PubMed - indexed for MEDLINE]
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Cited by 2 PubMed Central articles
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Canine alpha-L-fucosidase in relation to the enzymic defect and storage products in canine fucosidosis.
Barker C, Dell A, Rogers M, Alhadeff JA, Winchester B.
Biochem J. 1988 Sep 15; 254(3):861-8.
[Biochem J. 1988]
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Identification of a mutation in the structural alpha-L-fucosidase gene in fucosidosis.
Willems PJ, Darby JK, DiCioccio RA, Nakashima P, Eng C, Kretz KA, Cavalli-Sforza LL, Shooter EM, O'Brien JS.
Am J Hum Genet. 1988 Nov; 43(5):756-63.
[Am J Hum Genet. 1988]