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 secretory 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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Glycopeptides / metabolism
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Models, Biological
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Molecular Sequence Data
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Peptide Fragments / metabolism*
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Pituitary Gland / enzymology*
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Pituitary Hormones / metabolism
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Pro-Opiomelanocortin / metabolism*
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Proprotein Convertase 1*
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Proprotein Convertase 2
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Proprotein Convertases
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Protein Processing, Post-Translational*
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Sequence Analysis, DNA
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Serine Endopeptidases / genetics*
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Serine Endopeptidases / metabolism*
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Substrate Specificity
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Swine
Substances
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Glycopeptides
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Peptide Fragments
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Pituitary Hormones
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proopiocortin fragments
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Pro-Opiomelanocortin
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Proprotein Convertases
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Serine Endopeptidases
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Pcsk1 protein, mouse
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Proprotein Convertase 1
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Proprotein Convertase 2
Associated data
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GENBANK/S39995
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GENBANK/S39996
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GENBANK/S40001
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GENBANK/S40008
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GENBANK/S40009
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GENBANK/S40010
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GENBANK/X58277
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GENBANK/X66432
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GENBANK/X68603
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GENBANK/X70912