The cDNA structure of the porcine pro‐hormone convertase PC2 and the comparative processing by PC1 and PC2 of the N‐terminal glycopeptide segment of porcine POMC
Open Access
- 5 October 1992
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 310 (3) , 235-239
- https://doi.org/10.1016/0014-5793(92)81339-n
Abstract
The complete cDNA structure of the porcine (p) pro‐protein and pro‐hormone convertase PC2 (pPC2) was obtained from a cDNA library of pituitary neurointermediate lobes mRNA. The deduced amino acid sequence revealed that pPC2 exhibits a 99‐97% sequence identity to the human, mouse and rat homologues. The 3′ end of the 2.1 kb cDNA is the least conserved segment. On Northern blots of pars intermedia poly A+ RNA two transcripts of 3 and 5 kb were detected. Molecular analysis of the N‐terminal glycopeptide products of porcine pro‐opiomelanocortin (pPOMC) co‐expressed with vaccinia virus recombinants of PC1 or PC2, revealed that in cells devoid or containing secretary granules both convertases can cleave pPOMC with PC1 releasing the 1–80, 1–107 and 1–148 glycopeptide fragments, and PC2 cleaving pPOMC directly into pPOMC 1–107.Keywords
This publication has 25 references indexed in Scilit:
- Structure and expression of Xenopus prohormone convertase PC2FEBS Letters, 1992
- Proprotein and prohormone convertases of the subtilisin familyTrends in Endocrinology & Metabolism, 1992
- The cDNA Sequence of the Human Pro-Hormone and Pro-Protein Convertase PC1DNA and Cell Biology, 1992
- Distribution and regulation of the prohormone convertases PC1 and PC2 in the rat pituitaryMolecular Endocrinology, 1992
- Identification of a Second Human Subtilisin-Like Protease Gene in thefes/fpsRegion of Chromosome 15DNA and Cell Biology, 1991
- Production of monoclonal antibodies against the N-terminal glycopeptide of porcine pro-opiomelanocortin: their use for solid-phase radioimmunoassay, western blotting, and immunogold cytochemistryBiochemistry and Cell Biology, 1991
- cDNA Sequence of Two Distinct Pituitary Proteins Homologous to Kex2 and Furin Gene Products: Tissue-Specific mRNAs Encoding Candidates for Pro-Hormone Processing ProteinasesDNA and Cell Biology, 1990
- FIBRONECTIN AND ITS RECEPTORSAnnual Review of Biochemistry, 1988
- Structure and bioactivity of the amino-terminal fragment of pro-opiomelanocortinJournal of Steroid Biochemistry, 1986
- Two glycosylation sites on the N‐terminal segment of porcine pars distalis pro‐opiomelanocortinFEBS Letters, 1980