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TRH‐extended peptides in the olfactory lobe are formed by incomplete cleavage at pairs of arginine residues in the TRH prohormone
Author(s) -
Cockle Sheena M.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80261-g
Subject(s) - prohormone , cleavage (geology) , chemistry , thyrotropin releasing hormone , medicine , endocrinology , arginine , peptide , peptide hormone , biochemistry , hormone , biology , amino acid , paleontology , fracture (geology)
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.