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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6 Pt 1
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pubmed:dateCreated |
1992-7-29
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pubmed:abstractText |
We demonstrate that two enzymes, soluble unspecific pyroglutamyl peptidase I and prolyl endopeptidase, able to degrade thyrotropin-releasing hormone (TRH) in vitro were present in pancreas at the early stage of rat development. Specific particulate pyroglutamyl peptidase II remained undetectable during ontogenesis. Pyroglutamyl peptidase I specific activity increased until day 3 and decreased after day 5. Furthermore, prolyl endopeptidase specific activity rose slightly to a peak on postnatal day 20. A good correlation between immunoreactive TRH and deaminated TRH (TRH-OH) was found in the 1st wk after birth. However, His-Pro diketopiperazine (DKP) levels were stable and low during development. We show that hot acidic extraction conditions could artefactually generate His-Pro DKP. In vivo, active site-directed inhibitors of pyroglutamyl peptidase I and prolyl endopeptidase enzymes do not show any TRH-deamidating and/or pyroglutamyl peptidase I pathways in neonatal rat pancreas. The data suggest that these two enzymes are not involved in intra- or extracellular control of TRH levels in neonatal rat pancreas and that pancreatic TRH content appears to be principally regulated by biosynthetic steps. Nevertheless, low levels of endogenous His-Pro DKP and TRH-OH identified in neonatal rat pancreas suggest that TRH or TRH-like peptides may be metabolized in this tissue in intact rats, albeit at low rates.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Pyroglutamyl-Peptidase I,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Thyrotropin-Releasing Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/prolyl oligopeptidase
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0002-9513
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
262
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
E845-50
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1352085-Aging,
pubmed-meshheading:1352085-Animals,
pubmed-meshheading:1352085-Cell Membrane,
pubmed-meshheading:1352085-Endopeptidases,
pubmed-meshheading:1352085-Female,
pubmed-meshheading:1352085-Kinetics,
pubmed-meshheading:1352085-Male,
pubmed-meshheading:1352085-Pancreas,
pubmed-meshheading:1352085-Protease Inhibitors,
pubmed-meshheading:1352085-Pyroglutamyl-Peptidase I,
pubmed-meshheading:1352085-Rats,
pubmed-meshheading:1352085-Rats, Inbred Strains,
pubmed-meshheading:1352085-Serine Endopeptidases,
pubmed-meshheading:1352085-Thyrotropin-Releasing Hormone
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pubmed:year |
1992
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pubmed:articleTitle |
Ontogeny of prolyl endopeptidase, pyroglutamyl peptidase I, TRH, and its metabolites in rat pancreas.
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pubmed:affiliation |
Laboratoire de Neuroendocrinologie Experimentale, Institut National de la Santé et de la Recherche Médicale U297, Faculté de Médecine Nord, Marseille, France.
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pubmed:publicationType |
Journal Article
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