The synthesis and turnover of 5′-nucleotidase in primary cultured hepatocytes
| Autor: | J P Luzio, M. D. Baron |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
Glycosylation
Glycoside Hydrolases Endoglycosidase 5'-nucleotidase Endoglycosidase H chemistry.chemical_compound Biosynthesis Nucleotidases Acetylglucosaminidase medicine Animals 5'-Nucleotidase Molecular Biology Cells Cultured Methionine biology Tunicamycin Cell Biology Molecular biology Rats Molecular Weight Kinetics Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase medicine.anatomical_structure Liver chemistry Biochemistry Cell culture Hepatocyte biology.protein Half-Life |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 927:81-85 |
| ISSN: | 0167-4889 |
| DOI: | 10.1016/0167-4889(87)90068-1 |
| Popis: | The synthesis and degradation of 5′-nucleotidase has been studied in rat hepatocytes. Primary cultures of rat hepatocytes were established with the cells showing evidence of polarity after 24–36 h in culture. After a 30 h lag period 5′-nucleotidase activity increased to a plateau level similar to the activity found in whole liver. The half life of the enzyme after reaching the plateau of activity was 22.8 h. Pulse-chase biosynthetic labelling studies of 5′-nucleotidase in the cultured hepatocytes using [35S]methionine showed that the 5′-nucleotidase monomer was synthesised as an Mr 67 000 form which was converted to the mature Mr 72 000 form. [35S]Methionine labelling studies in the presence of tunicamycin showed that the unglycosylated protein monomer was an Mr 57 000 form. The immature Mr 67 000 form of 5′-nucleotidase was sensitive to endoglycosidase H, whereas the mature form was sensitive only to endoglycosidase F. The data presented are consistent with 5′-nucleotidase in a polarised cell being synthesised and processed like other membrane glycoproteins, in contrast to earlier reports. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|