Yeast KEX2 endopeptidase correctly cleaves a neuroendocrine prohormone in mammalian cells - PubMed (original) (raw)
. 1988 Jul 8;241(4862):226-30.
doi: 10.1126/science.3291117.
Affiliations
- PMID: 3291117
- DOI: 10.1126/science.3291117
Yeast KEX2 endopeptidase correctly cleaves a neuroendocrine prohormone in mammalian cells
G Thomas et al. Science. 1988.
Abstract
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.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases