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Literature DB >> 3675577

Intracellular transport and processing of lysosomal cathepsin B.

Abstract

Intracellular transport and processing of lysosomal cathepsin B was investigated in the subcellular fractions of rat liver by pulse-labeling experiments with [35S]methionine in vivo. A newly synthesized procathepsin B with a molecular weight of 39 kDa firstly appeared in the rough microsomal fraction at 10 min postinjection of label. This procathepsin B moved from the microsomal fractions to the Golgi subfractions at 30 min postinjection, and then a processed mature enzyme appeared in the lysosomal fraction at 60 min. These results suggest that the propeptide-processing of procathepsin B takes place in lysosomes in the course of intracellular transport from endoplasmic reticulum through Golgi complex to lysosomes.

Entities: Chemical Gene Species

Mesh：

Substances：
Cathepsin B

Year: 1987 PMID： 3675577 DOI： 10.1016/0006-291x(87)91103-x

Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575

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Cited

7 in total

1. Proteolytic processing and glycosylation of cathepsin B. The role of the primary structure of the latent precursor and of the carbohydrate moiety for cell-type-specific molecular forms of the enzyme.

Authors: L Mach; K Stüwe; A Hagen; C Ballaun; J Glössl
Journal: Biochem J Date: 1992-03-01 Impact factor: 3.857

Review 2. The early and late processing of lysosomal enzymes: proteolysis and compartmentation.

Authors: A Hasilik
Journal: Experientia Date: 1992-02-15

3. The identification of active forms of cysteine proteinases in Kirsten-virus-transformed mouse fibroblasts by use of a specific radiolabelled inhibitor.

Authors: R W Mason; D Wilcox; P Wikstrom; E N Shaw
Journal: Biochem J Date: 1989-01-01 Impact factor: 3.857

Intracellular transport and processing of lysosomal cathepsin B.

1. Proteolytic processing and glycosylation of cathepsin B. The role of the primary structure of the latent precursor and of the carbohydrate moiety for cell-type-specific molecular forms of the enzyme.

Review 2. The early and late processing of lysosomal enzymes: proteolysis and compartmentation.

3. The identification of active forms of cysteine proteinases in Kirsten-virus-transformed mouse fibroblasts by use of a specific radiolabelled inhibitor.

4. Immunoenzyme localization of cathepsins in the Golgi region of rat hepatocytes and renal tubule cells.

5. Biochemical and immunohistochemical analysis of cathepsins B, H, L and D in human melanocytic tumours.

6. Purification and Characterization of Cathepsin B from the Muscle of Horse Mackerel Trachurus japonicus.

7. The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity.