Publication Date:
1988-07-08
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thomas, G -- Thorne, B A -- Thomas, L -- Allen, R G -- Hruby, D E -- Fuller, R -- Thorner, J -- AI20563/AI/NIAID NIH HHS/ -- DK37274/DK/NIDDK NIH HHS/ -- HD18438/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Jul 8;241(4862):226-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, Portland 97201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3291117" target="_blank"〉PubMed〈/a〉
Keywords:
Cell Line
;
Cloning, Molecular
;
DNA, Recombinant
;
Endopeptidases/*metabolism
;
In Vitro Techniques
;
Pro-Opiomelanocortin/*metabolism
;
Protein Precursors/*metabolism
;
Protein Processing, Post-Translational
;
Saccharomyces cerevisiae/enzymology
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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