Open AccessIsolation and functional expression of a mammalian prohormone processing enzyme, murine prohormone convertase 1.
Author(s) -
Judith Körner,
Jay Chun,
David H. Harter,
Richard Axel
Publication year - 1991
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.88.15.6834
Subject(s) - prohormone , prohormone convertase , proopiomelanocortin , biology , gene expression , gene , xenopus , cleavage (geology) , biochemistry , microbiology and biotechnology , hormone , paleontology , fracture (geology)
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.