Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1990-10-22
pubmed:abstractText
Based on the deduced amino acid sequence of rat TRH prohormone (pro-TRH), proteolytic processing of this polyprotein precursor is expected to produce, beside TRH, several other novel peptides. These peptides should correspond to connecting segments flanking the repeated TRH progenitor sequence and to various C- and/or N-terminally extended forms of TRH. The profile of the endogenous products of the TRH system was studied in rat brain using multiple RIAs coupled to molecular sieve filtration and HPLC separations. In extracts from the rat hypothalamus, TRH and two pro-TRH-connecting peptides, prepro-TRH-(160-169) and prepro-TRH-(178-199) were detected in molar ratios corresponding to those expected for a nearly complete processing of the prohormone molecule. In the olfactory bulb, pro-TRH is processed differently, since peptides containing TRH at their N-termini, [pGlu172] prepro-TRH-(172-199) and [pGlu154]prepro-TRH-(154-169), were found to be major end products along with prepro-TRH-(160-169) and prepro-TRH-(178-199). The dissimilarity in tissue content suggests that differential processing of TRH precursor by various enzymatic pathways may act as a regulating mechanism for TRH and TRH-related activities. The cellular localization of C-terminally extended forms of TRH in rat olfactory bulb was examined by the indirect immunoperoxidase method, using antisera directed against prepro-TRH-(160-169) and pre-pro-TRH-(178-199). Cell bodies and nerve fibers were detected in the glomerular and external plexiform layers of the main olfactory bulb. The presence of extended forms of TRH in interneurons and middle tufted cells of the main olfactory bulb suggests that in light of the recent biological properties described for prepro-TRH-(160-169), these peptides may act as neuromodulators for olfactory epithelium inputs or neurotransmitters within more rostrally located olfactory areas in the forebrain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0013-7227
pubmed:author
pubmed:issnType
Print
pubmed:volume
127
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1978-85
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:2119297-Amino Acid Sequence, pubmed-meshheading:2119297-Animals, pubmed-meshheading:2119297-Chromatography, Gel, pubmed-meshheading:2119297-Chromatography, High Pressure Liquid, pubmed-meshheading:2119297-Cyanogen Bromide, pubmed-meshheading:2119297-Immunoenzyme Techniques, pubmed-meshheading:2119297-Male, pubmed-meshheading:2119297-Molecular Sequence Data, pubmed-meshheading:2119297-Molecular Weight, pubmed-meshheading:2119297-Olfactory Bulb, pubmed-meshheading:2119297-Oxidation-Reduction, pubmed-meshheading:2119297-Peptide Fragments, pubmed-meshheading:2119297-Protein Precursors, pubmed-meshheading:2119297-Pyrrolidonecarboxylic Acid, pubmed-meshheading:2119297-Radioimmunoassay, pubmed-meshheading:2119297-Rats, pubmed-meshheading:2119297-Rats, Inbred Strains, pubmed-meshheading:2119297-Thyrotropin-Releasing Hormone
pubmed:year
1990
pubmed:articleTitle
Processing of thyrotropin-releasing hormone (TRH) prohormone in the rat olfactory bulb generates novel TRH-related peptides.
pubmed:affiliation
Laboratoire de Bioactivation des Peptides, Institut Jacques Monod, CNRS, Université Paris 7, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't