title: The pro-peptide is not necessary for active renin secretion from transfected mammalian cells.
abstract: Cultured mouse myeloma cells were transfected with expression vectors encoding the aspartyl proteinase, human renin. The full construct, encoding the renin precursor prorenin, allows transfected cells to secrete the enzymically inactive pro-protein. Activity is detectable only following trypsin treatment which mimics the physiological activation step. Accordingly, it appears that myeloma cells do not contain detectable levels of an appropriate activating proteinase. However, when these cells are transfected with a construct from which the pro-peptide coding sequence has been deleted, they secrete an apparently fully active enzyme which is indistinguishable from mature renin. We conclude that expression of the pro-peptide is not necessary to allow correct folding of the molecule and its passage through the secretory pathway.
authors.affiliation: Department of Biochemistry, University of Leicester, England.
authors.forename: T M
authors.initials: TM
authors.lastname: Harrison
authors.forename: M A
authors.initials: MA
authors.lastname: Chidgey
authors.forename: W J
authors.initials: WJ
authors.lastname: Brammar
authors.forename: G J
authors.initials: GJ
authors.lastname: Adams
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D004792:Enzyme Precursors / Q000235:genetics*; D005822:Genetic Vectors; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D015345:Oligonucleotide Probes; D010957:Plasmids; D011401:Promoter Regions, Genetic; D012083:Renin / Q000096:biosynthesis / Q000235:genetics*; D015183:Restriction Mapping; D014162:Transfection
chemical_list: D004792:Enzyme Precursors; D015345:Oligonucleotide Probes; D012083:Renin