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Human lysosomal acid phosphatase is transported as a transmembrane protein to lysosomes in transfected baby hamster kidney cells.

1988; Springer Nature; Volume: 7; Issue: 8 Linguagem: Inglês

10.1002/j.1460-2075.1988.tb03079.x

1460-2075

Abdül Waheed, Stephen Gottschalk, Annette Hille, C. Krentler, Regina Pohlmann, Thomas Braulke, H. Häuser, Hans J. Geuze, Kurt Von Figura,

Cellular transport and secretion

Research Article1 August 1988free access Human lysosomal acid phosphatase is transported as a transmembrane protein to lysosomes in transfected baby hamster kidney cells. A. Waheed A. Waheed Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author S. Gottschalk S. Gottschalk Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author A. Hille A. Hille Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author C. Krentler C. Krentler Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author R. Pohlmann R. Pohlmann Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author T. Braulke T. Braulke Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author H. Hauser H. Hauser Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author H. Geuze H. Geuze Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author K. von Figura K. von Figura Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author A. Waheed A. Waheed Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author S. Gottschalk S. Gottschalk Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author A. Hille A. Hille Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author C. Krentler C. Krentler Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author R. Pohlmann R. Pohlmann Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author T. Braulke T. Braulke Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author H. Hauser H. Hauser Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author H. Geuze H. Geuze Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author K. von Figura K. von Figura Zentrum Biochemie, Universität Göttingen, FRG. Search for more papers by this author Author Information A. Waheed1, S. Gottschalk1, A. Hille1, C. Krentler1, R. Pohlmann1, T. Braulke1, H. Hauser1, H. Geuze1 and K. Figura1 1Zentrum Biochemie, Universität Göttingen, FRG. The EMBO Journal (1988)7:2351-2358https://doi.org/10.1002/j.1460-2075.1988.tb03079.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info BHK cells transfected with human lysosomal acid phosphatase (LAP) cDNA (CT29) expressed 70-fold higher enzyme activities of acid phosphatase than non-transfected BHK cells. The CT29-LAP was synthesized in BHK cells as a heterogeneously glycosylated precursor that was tightly membrane associated. Transfer to the trans-Golgi was associated with a small increase in size (approximately 7 kd) and partial processing of the oligosaccharides to complex type structures. CT29-LAP was transferred into lysosomes as shown by subcellular fractionation, immunofluorescence and immunoelectron microscopy. Lack of mannose-6-phosphate residues suggested that transport does not involve mannose-6-phosphate receptors. Part of the membrane-associated CT29-LAP was processed to a soluble form. The mechanism that converts CT29-LAP into a soluble form was sensitive to NH4Cl, and reduced the size of the polypeptide by 7 kd. In vitro translation of CT29-derived cRNA in the presence of microsomal membranes yielded a CT29-LAP precursor that is protected from proteinase K except for a small peptide of approximately 2 kd. In combination with the sequence data available for LAP, these observations suggest that CT29-LAP is synthesized and transported to lysosomes as a transmembrane protein. In the lysosomes, CT29-LAP is released from the membrane by proteolytic cleavage, which removes a C-terminal peptide including the transmembrane domain and the cytosolic tail of 18 amino acids. Previous ArticleNext Article Volume 7Issue 81 August 1988In this issue RelatedDetailsLoading ...