TRH‐extended peptides in the olfactory lobe are formed by incomplete cleavage at pairs of arginine residues in the TRH prohormone

FEBS Letters

Cockle, Sheena M.¹ 

[1] Dept. of Biochemistry and Physiology, AMS Building, University of Reading, Whiteknights, PO Box 228, Reading RG6 2AJ, UK

关键词: Olfactory lobe;    Thyrotrophin-releasing hormone;    Prohormone;    Processing;   

DOI  :  10.1016/0014-5793(90)80261-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

High concentrations of thyrotrophin-releasing hormone (TRH) are known to be present in the olfactory lobe, and the processing of the TRH prohormone in this region of the brain has been examined in this study. TRH-extended peptides have been detected in the rat olfactory lobe: these peptides accounted for approximately 11% of the total TRH immunoreactivity present in the tissue and contained the sequence pGlu-His-Pro-Gly-Arg exclusively at their N-termini. Extended peptides containing pGlu-His-Pro-Gly-Lys at their N-termini were not detected suggesting that incomplete cleavage occurs only at Arg-Arg residues in the TRH-prohonnone. In view of the highly specific processing of the prohormone, it is likely that the TRH-extended peptides play important physiological roles.

【 授权许可】

Unknown