Identification of proteolytic activities in ROS 17/2.8 cell lysates which cleave peptide substrates for protein kinase C-mediated phosphorylation
| Autor: | Peter T. Guidon, Patricia Harrison |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
medicine.medical_treatment
Peptide Bone Neoplasms Substrate Specificity chemistry.chemical_compound Endopeptidases medicine Tumor Cells Cultured Animals Protease Inhibitors Amino Acid Sequence Phosphorylation Protein kinase A Molecular Biology Protein kinase C Protein Kinase C Fluorescent Dyes chemistry.chemical_classification Osteosarcoma Protease Cell-Free System Phosphoramidon Leupeptin Molecular biology Protease inhibitor (biology) Rats Biochemistry chemistry Oligopeptides Pepstatin medicine.drug |
| Zdroj: | Matrix biology : journal of the International Society for Matrix Biology. 15(1) |
| ISSN: | 0945-053X |
| Popis: | We have observed two proteolytic activities in cell lysates from the rat osteoblastic osteosarcoma cell line ROS 17/2.8 which are capable of cleaving a peptide substrate for protein kinase C-mediated phosphorylation, and other peptides containing similar sequences. Both activities are inhibited by Pefabloc, a serie protease inhibitor, while one of the activities is inhibited by either EDTA or aprotinin. The protease inhibitors pepstatin, bestatin, E-64, leupeptin and phosphoramidon do not block either of these proteolytic activities. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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