Human Cathepsin G Lacking Functional Glycosylation Site Is Proteolytically Processed and Targeted for Storage in Granules after Transfection to the Rat Basophilic/Mast Cell Line RBL or the Murine Myeloid Cell Line 32D
Open Access
- 1 November 1995
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 270 (47) , 28413-28418
- https://doi.org/10.1074/jbc.270.47.28413
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- Roles for mannose-6-phosphate receptors in lysosomal enzyme sorting, IGF-II binding and clathrin-coat assemblyTrends in Cell Biology, 1995
- Proteases and lymphocyte cytotoxic killing mechanismsCurrent Opinion in Immunology, 1993
- The Isoforms of Human Neutrophil Elastase and Cathepsin G Differ in their Carbohydrate Side Chain StructuresBiological Chemistry Hoppe-Seyler, 1993
- Theearly andlate processing of lysosomal enzymes: Proteolysis and compartmentationCellular and Molecular Life Sciences, 1992
- Human cathepsin D precursor is associated with a 60 kDa glycosylated polypeptideBiochemical and Biophysical Research Communications, 1992
- A noncytotoxic mast cell tumor line exhibits potent IgE-dependent cytotoxicity after transfection with the cytolysin/perforin geneCell, 1991
- Amino acid sequence of CAP37, a human neutrophil granule‐derived antibacterial and monocyte‐specific chemotactic glycoprotein structurally similar to neutrophil elastaseFEBS Letters, 1990
- An unusual specificity in the activation of neutrophil serine proteinase zymogensBiochemistry, 1990
- Human acid β-glucosidase: Glycosylation is required for catalytic activityBiochemical and Biophysical Research Communications, 1990
- Site-directed mutagenesis by overlap extension using the polymerase chain reactionGene, 1989