Transient membrane association of the precursors of cathepsin C during their transfer into lysosomes
| Autor: | Robert Wattiaux, Francis Mainferme, V Burge |
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| Rok vydání: | 1991 |
| Předmět: |
Golgi Apparatus
Biology Centrifugation Isopycnic Cell Fractionation Endoplasmic Reticulum Biochemistry Cathepsin C symbols.namesake Liver Neoplasms Experimental Lysosome medicine Tumor Cells Cultured Animals Centrifugation Protein Precursors Dipeptidyl-Peptidases and Tripeptidyl-Peptidases Molecular Biology Immunosorbent Techniques chemistry.chemical_classification Endoplasmic reticulum Cell Membrane Biological membrane Biological Transport Cell Biology Golgi apparatus Molecular biology Kinetics medicine.anatomical_structure Enzyme chemistry Cell culture symbols Lysosomes Research Article |
| Zdroj: | The Biochemical journal. 275 |
| ISSN: | 0264-6021 |
| Popis: | Transport of the lysosomal enzyme cathepsin C was studied in Morris hepatoma 7777 cells. Subcellular fractions obtained after isopyenic centrifugation in sucrose gradients of labelled cell homogenates were sequentially extracted by hypo-osmotic shock, Na2CO3 and Triton X-100. Polypeptides related to cathepsin C were immunoprecipitated and analysed by SDS/PAGE and fluorography. At early times after synthesis and for up to 60 min, precursor polypeptides of cathepsin C are distributed in endoplasmic reticulum and Golgi fractions, in membrane-associated form, as Triton X-100 is necessary for their extraction. At 2 h and later after synthesis, intermediate and mature forms of the enzyme can be totally extracted by hypo-osmotic shock from gradient fractions corresponding to the lysosomes of Morris hepatoma 7777 cells. |
| Databáze: | OpenAIRE |
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