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Targeting of Lysosomal Acid Phosphatase With Altered Carbohydrate

Targeting of Lysosomal Acid Phosphatase With Altered Carbohydrate

S Gottschalk, A Waheed, K von Figura

Biol Chem Hoppe Seyler. 1989 Jan;370(1):75-80.

PMID: 2540767

Abstract:

Human lysosomal acid phosphatase is transported as a transmembrane protein to lysosomes, where it is converted into a soluble protein by a limited proteolysis (Waheed et al., 1988, EMBO J. 7, 2351-2358). Transport of human lysosomal acid phosphatase in heterologous BHK-21 cells was examined under conditions that impair mannose-6-phosphate receptor-dependent transport, N-glycosylation or processing of N-linked oligosaccharides. Targeting of lysosomal acid phosphatase to lysosomes was neither affected by antibodies blocking the mannose-6-phosphate/IGF II receptor, nor by NH4Cl, which inhibited the mannose-6-phosphate receptor-dependent targeting of soluble lysosomal enzymes. 1-Deoxynojirimycin, 1-deoxymannojirimycin and swainsonine inhibited processing of N-linked oligosaccharides in lysosomal acid phosphatase without significantly affecting its transport. Tunicamycin inhibited N-glycosylation of lysosomal acid phosphatase. The non-glycosylated lysosomal acid phosphatase polypeptides accumulated within light membranes and were not transported to dense lysosomes. These results indicate that transport of lysosomal acid phosphatase is independent of mannose-6-phosphate receptors, does not involve an acid pH-dependent step and does not require processing of N-linked oligosaccharides. N-glycosylation appears to be necessary to achieve a transport competent form of lysosomal acid phosphatase.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP70442238	D-Glucosamine 6-phosphate sodium salt		70442-23-8	Price
AP70442250	D-Mannose 6-phosphate sodium salt		70442-25-0	Price

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