Proteose peptone enhances production of tissue-type plasminogen activator from human diploid fibroblasts.
Proteose peptone markedly enhanced the production of human tissue-type plasminogen activator (t-PA) from confluently cultured cell of human diploid fibroblasts. The cells continued synthesizing and secreting high levels of t-PA under periodic replacement of medium containing proteose peptone for more than one month. The highly increased activity correlated with equally increased levels of t-PA antigen and concomitantly increased levels of t-PA specific mRNA.
D002364:Caseins / Q000494:pharmacology*; D002460:Cell Line; D002850:Chromatography, Gel; D004171:Diploidy; D004591:Electrophoresis, Polyacrylamide Gel; D005347:Fibroblasts / Q000187:drug effects / Q000201:enzymology*; D006801:Humans; D005779:Immunodiffusion; D008970:Molecular Weight; D010446:Peptide Fragments / Q000494:pharmacology*; D010461:Peptones; D010959:Tissue Plasminogen Activator / Q000096:biosynthesis*; D014568:Urokinase-Type Plasminogen Activator / Q000096:biosynthesis
D002364:Caseins; D010446:Peptide Fragments; D010461:Peptones; C018135:proteose-peptone; D010959:Tissue Plasminogen Activator; D014568:Urokinase-Type Plasminogen Activator