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The pro‐peptide is not necessary for active renin secretion from transfected mammalian cells
Author(s) -
Harrison T. M.,
Chidgey M. A. J,
Brammar W. J,
Adams G. J
Publication year - 1989
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340050402
Subject(s) - transfection , secretion , peptide , trypsin , enzyme , renin–angiotensin system , signal peptide , biology , microbiology and biotechnology , biochemistry , chemistry , peptide sequence , gene , endocrinology , blood pressure
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 cellsto 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.