Identification of proteolytic activities in ROS 17/2.8 cell lysates which cleave peptide substrates for protein kinase C-mediated phosphorylation.
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 serine 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.
Guidon
P T
PT
Department of Biology, Seton Hall University, South Orange, New Jersey, USA.
Harrison
P
P
D000595:Amino Acid Sequence; D000818:Animals; D001859:Bone Neoplasms; D002474:Cell-Free System; D010450:Endopeptidases / Q000378:metabolism*; D005456:Fluorescent Dyes; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism*; D012516:Osteosarcoma; D010766:Phosphorylation; D011480:Protease Inhibitors / Q000494:pharmacology; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity; D014407:Tumor Cells, Cultured
D005456:Fluorescent Dyes; D009842:Oligopeptides; D011480:Protease Inhibitors; D011493:Protein Kinase C; D010450:Endopeptidases