Literature DB >> 1815998

Synthesis and processing of pro-ocytocin in bovine corpus luteum and granulosa cells.

M Camier1, D Benveniste, N Barré, N Brakch, P Cohen.   

Abstract

Bovine corpus luteum is the site of intense production of pro-ocytocin-neurophysin mRNA at day 1 after estrus (Ivell et al. (1985) FEBS Lett. 190, 263-267) which is followed by apparent delayed production of ocytocin. Therefore it is a good model to study both the translational and post-translational production of this neuropeptide in non-hypothalamic tissues and its regulation. In order to assess if this mRNA is translated during the lag period we have analyzed the neurophysin-like species produced in this organ. As early as day 2 after estrus one neurophysin species (pI approximately 4.7) could be detected and was unequivocally identified as pro-ocytocin-neurophysin. In primary cultures of luteinizing granulosa cells, biosynthetic intermediates were characterized, i.e. ocytocin-Gly, ocytocin-Gly-Lys and ocytocin-Gly-Lys-Arg, whereas amidated, fully mature, ocytocin was undetectable. We conclude that translation of pro-ocytocin-neurophysin mRNA takes place soon after transcription and we propose that incomplete processing could be responsible for the low level of ocytocin in the early bovine corpus luteum.

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Year:  1991        PMID: 1815998     DOI: 10.1016/0303-7207(91)90068-4

Source DB:  PubMed          Journal:  Mol Cell Endocrinol        ISSN: 0303-7207            Impact factor:   4.102


  1 in total

1.  Evidence for the presence of a secondary structure at the dibasic processing site of prohormone: the pro-ocytocin model.

Authors:  L Paolillo; M Simonetti; N Brakch; G D'Auria; M Saviano; M Dettin; M Rholam; A Scatturin; C Di Bello; P Cohen
Journal:  EMBO J       Date:  1992-07       Impact factor: 11.598

  1 in total

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