COOH-terminally-extended processing forms of oxytocin in human ovary.
Human granulosa cells synthesize and secrete the oxytocin hormone. We have already shown that oxytocin-Gly, the last post-translational maturation intermediate of pro-hormone, is largely secreted by cultured granulosa cells deprived of ascorbate (Plevrakis et al. (1990) J. Endocrinol. 124, R5-R8). Using a combination of high performance liquid chromatography and radioimmunoassay, the oxytocin-like material present in human granulosa cell extracts, in follicular fluid, in cultured granulosa cell supernatants and in corpora lutea extracts was identified. We have demonstrated the presence of oxytocin-Gly, oxytocin-Gly-Lys and oxytocin-Gly-Lys-Arg, the same post-translational maturation intermediates as those we identified in bovine corpus luteum secretory granules. Thus we conclude that post-translational maturation of pro-oxytocin/neurophysin in human ovary proceeds by the same proteolytic events as those we described in bovine post-pituitary gland and corpus luteum.
Guillou
M D
MD
Recherche Clinique et Biologique en Reproduction, INSERM CIJ 89-08, Hôpital de la Grave, Toulouse, France.
Barre
N
N
Bussenot
I
I
Plevrakis
I
I
Clamagirand
C
C
D000595:Amino Acid Sequence; D002478:Cells, Cultured; D002851:Chromatography, High Pressure Liquid; D003338:Corpus Luteum / Q000737:chemistry; D003470:Culture Media; D005260:Female; D006107:Granulosa Cells / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D010121:Oxytocin / Q000031:analogs & derivatives / Q000378:metabolism*; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D011863:Radioimmunoassay
D003470:Culture Media; D011498:Protein Precursors; D010121:Oxytocin