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Publication : Isolation and functional expression of a mammalian prohormone processing enzyme, murine prohormone convertase 1.

First Author  Korner J Year  1991
Journal  Proc Natl Acad Sci U S A Volume  88
Issue  15 Pages  6834-8
PubMed ID  1862107 Mgi Jnum  J:33624
Mgi Id  MGI:81102 Doi  10.1073/pnas.88.15.6834
Citation  Korner J, et al. (1991) Isolation and functional expression of a mammalian prohormone processing enzyme, murine prohormone convertase 1. Proc Natl Acad Sci U S A 88(15):6834-8
abstractText  We have combined gene cloning with an assay for prohormone biosynthesis and processing in Xenopus oocytes to identify the genes that encode mammalian prohormone processing enzymes. The coinjection of RNA encoding murine prohormone convertase 1 (mPC1), a mammalian endoprotease, along with proopiomelanocortin RNA into an oocyte results in the appropriate cleavage after paired basic residues in the proopiomelanocortin polyprotein necessary to generate corticotropin. The ability of mPC1 to generate corticotropin, along with the observation that mPC1 is specifically expressed in endocrine and neuronal cells, suggests that the mPC1 gene encodes the endopeptidase responsible for the pathway of proopiomelanocortin cleavage observed in the anterior pituitary.
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