Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-10-9
pubmed:abstractText
The osmoregulator peptide (leech osmoregulatory factor, LORF; IPEPYVWD) was first found in the leech central nervous system (CNS). Given the fact that certain peptides can be found in mammals and invertebrates, e.g., opioid, we examined rat brains to determine if LORF was present. This peptide was found and isolated by successive reversed-phase HPLC purification steps and characterized by electrospray mass spectrometry measurement. It was sequenced by Edman degradation and quantified in different tissues by ELISA. Our results demonstrate the presence of LORF in the hypothalamus, thalamus, and striatum (6 pmol/mg of protein extract) and in other brain areas at lower levels. This octapeptide is also present in the rat duodenum and liver (10 to 14 pmol/mg) and at lower levels in heart, lung, pancreas and caudal spinal cord (< 5 pmol/mg). The testes, adrenals and kidneys have the lowest levels of all the tissues examined (ca. 0.5 pmol/mg of protein). Furthermore, we also demonstrate that LORF is coupled to nitric oxide (NO) release in leech CNS, rat hypothalamus and human saphenous vein in a manner which is inhibited by a nitric oxide synthase inhibitor as well as an antibody directed toward LORF. The study demonstrates that LORF, and its function in relation to NO release, has been conserved over more than 400 million years of evolution.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0169-328X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
55
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
173-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9645973-Animals, pubmed-meshheading:9645973-Brain Chemistry, pubmed-meshheading:9645973-Chromatography, High Pressure Liquid, pubmed-meshheading:9645973-Enzyme Inhibitors, pubmed-meshheading:9645973-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:9645973-Evolution, Molecular, pubmed-meshheading:9645973-Ganglia, Invertebrate, pubmed-meshheading:9645973-Humans, pubmed-meshheading:9645973-Leeches, pubmed-meshheading:9645973-Male, pubmed-meshheading:9645973-Mass Spectrometry, pubmed-meshheading:9645973-Myocardium, pubmed-meshheading:9645973-Nerve Tissue Proteins, pubmed-meshheading:9645973-Neuropeptides, pubmed-meshheading:9645973-Nitric Oxide, pubmed-meshheading:9645973-Nitric Oxide Synthase, pubmed-meshheading:9645973-Oligopeptides, pubmed-meshheading:9645973-Organ Specificity, pubmed-meshheading:9645973-Rats, pubmed-meshheading:9645973-Rats, Wistar, pubmed-meshheading:9645973-Saphenous Vein, pubmed-meshheading:9645973-Species Specificity, pubmed-meshheading:9645973-Spinal Cord, pubmed-meshheading:9645973-Testis, pubmed-meshheading:9645973-Viscera
pubmed:year
1998
pubmed:articleTitle
Isolation and characterization of a leech neuropeptide in rat brains: coupling to nitric oxide release in leech, rat and human tissues.
pubmed:affiliation
Centre de Biologie Cellulaire, Université des Sciences et Technologies de Lille, Villeneuve d'Ascq, France. salzet@pop.univ-lille1.fr
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't