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Endocrinology, Vol 125, 1492-1497, Copyright © 1989 by Endocrine Society

ARTICLES

Processing of thyrotropin-releasing hormone prohormone (pro-TRH) in the adult rat pancreas: identification and localization of pro-TRH-related peptides in beta-cells of pancreatic islets

P Leduque, M Bulant, PM Dubois, P Nicolas and H Vaudry
Laboratoire d'Histologie-Embryologie, CNRS URA 559, Faculte de Medecine Lyon-Sud, Oullins, France.

Rat TRH prohormone (pro-TRH) contains five separate copies of the TRH progenitor sequence, Gln-His-Pro-Gly. All five sequences are flanked by paired basic amino acid cleavage sites and linked together by connecting sequences. RIAs to synthetic TRH and prepro-TRH-(178-199) were used to investigate pro-TRH processing in the endocrine pancreas of adult rats. HPLC analysis of adult rat pancreatic extracts showed the presence of a major immunoreactive peptide eluting at the position of prepro-TRH-(178-199). An additional peak coeluting with [less than Glu172]prepro-TRH-(172-199) (less than Glu = pyroglutamyl) revealed the presence of a C-terminally extended form of TRH. Quantification of TRH in pancreatic extracts indicated the presence of 22 mol TRH/mol prepro- TRH-(178-199) and 17 mol TRH/mol [less than Glu172]prepro-TRH-(172- 199). Treatment of rats with streptozotocin markedly reduced the pancreatic content of both immunoreactive TRH (-84%) and immunoreactive prepro-TRH-(178-199) (-62%). Light microscopic immunocytochemistry showed that prepro-TRH-(178-199)-like immunoreactivity was exclusively located within insulin-containing cells of the pancreatic islets. At the electron microscopic level, prepro-TRH-(178-199) immunoreactivity appeared to be concentrated in secretory granules. The present study demonstrates that processing of pro-TRH generates both non-TRH- and TRH- related peptides in the adult rat pancreas. Our data also indicate that beta-cells of the endocrine pancreas are the major source of TRH- and pro-TRH-derived peptides.


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E. A. Nillni and K. A. Sevarino
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