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Science 8 July 1988:
Vol. 241. no. 4862, pp. 226 - 230
DOI: 10.1126/science.3291117
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Articles
Science, Vol 241, Issue 4862, 226-230
Copyright © 1988 by American Association for the Advancement of Science
Yeast KEX2 endopeptidase correctly cleaves a neuroendocrine prohormone in mammalian cells
G Thomas,
BA Thorne,
L Thomas,
RG Allen,
DE Hruby,
R Fuller,
and
J Thorner
Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, Portland 97201.
Mammalian cell lines (BSC-40, NG108-15, and GH4C1) that cannot process the murine neuroendocrine peptide precursor prepro-opiomelanocortin (mPOMC) when its synthesis is directed by a vaccinia virus vector were coinfected with a second recombinant vaccinia virus carrying the yeast KEX2 gene, which encodes an endopeptidase that cleaves at pairs of basic amino acid residues. mPOMC was cleaved intracellularly to a set of product peptides normally found in vivo, including mature gamma-lipotropin and beta-endorphin1-31. In GH4C1 cells (a rat pituitary line), product peptides were incorporated into stored secretory granules. These results suggest that the inability of any particular cell line to process a prohormone precursor is due to the absence of a suitable endogenous processing enzyme.
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