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PMID: 3551957 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

C-terminally extended ocytocin and pro-ocytocin: neurophysin peptide converting enzyme in bovine corpus luteum.

Biochemical and biophysical research communications ·Vol. 143 ·No. 2 ·1987-03-13 ·Pages 789-96

Clamagirand C, Camier M, Fahy C, Clavreul C, Créminon C, Cohen P

Abstract

Purified secretory granules from the corpus luteum of super ovulated and fecundated cows, at day 7-8 after the heat period, were used as a source of pro-ocytocin/neurophysin (pro OT/Np) processing enzymes. An endoprotease comparable to the previously described pituitary enzyme both by its catalytic properties and sensitivity to various inhibitors was characterized. This protease cleaves pro OT/Np (1-20) after the basic Lys11Arg12 doublet to release OT Gly10 Lys11 Arg12. Moreover C-terminally extended ocytocin, i.e. OTGlyLys and OTGlyLysArg together with ocytocin were identified in extracts from the corpus luteum. Together these data argue strongly in favor of pro OT/Np processing pathways in which cleavage of the precursor at the Arg12-Ala13 peptide bond is the primary event.

MeSH Terms
Amino Acid Sequence Animals Cattle Corpus Luteum/physiology Cytoplasmic Granules/metabolism Female Neurophysins/metabolism Oxytocin/metabolism Peptide Hydrolases/metabolism Pituitary Gland, Posterior/enzymology Protein Precursors/metabolism Protein Processing, Post-Translational Substrate Specificity
Chemicals
Neurophysins Protein Precursors Oxytocin Peptide Hydrolases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Clamagirand C
Camier M
Fahy C
Clavreul C
Créminon C
Cohen P
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1987-03-13
Pages
789-96
Language
English
Region
United States
NLM ID
0372516
Subset
IM
Corrections
ErratumIn
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