Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2004-5-27
pubmed:abstractText
Soluble leptin receptor (SLR) represents the major leptin binding activity in plasma. It is generated by alternative splicing of OB-R mRNA (OB-Re) and/or ectodomain shedding of membrane-spanning receptors. To determine the role of SLR in leptin activation of its long-form receptor, OB-Rb, we established in vitro assays using a cell line stably expressing OB-Rb. Human embryonic kidney 293 cell lines stably overexpressing OB-Rb show a dose-dependent leptin-induced signal transducer and activator of transcription 3 (STAT3) tyrosine phosphorylation and STAT3-responsive luciferase (STAT3-luc) activity. We demonstrate that when SLR is incubated with free leptin, binding of leptin to OB-Rb is reduced, with corresponding decrease of leptin-induced STAT3 tyrosine phosphorylation and STAT3-luc activity. However, by preparing leptin/SLR mixtures containing the same amount of free leptin but increasing amounts of leptin-SLR complex, we show that leptin-SLR complex does not inhibit OB-Rb activation by free leptin. These results suggest that in settings in which leptin and SLR coexist, SLR may sequester leptin from productive interactions with OB-Rb. Because plasma SLR levels are independently regulated by many different physiological and pathophysiological conditions, SLR may modulate the actions of leptin in tissues in which direct action of leptin has been demonstrated.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Conditioned, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Leptin, http://linkedlifedata.com/resource/pubmed/chemical/Luciferases, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Leptin, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/STAT3 Transcription Factor, http://linkedlifedata.com/resource/pubmed/chemical/STAT3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine, http://linkedlifedata.com/resource/pubmed/chemical/leptin receptor, human
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0888-8809
pubmed:author
pubmed:issnType
Print
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1354-62
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:15016839-Blotting, Western, pubmed-meshheading:15016839-Cell Line, pubmed-meshheading:15016839-Chromatography, Gel, pubmed-meshheading:15016839-Culture Media, Conditioned, pubmed-meshheading:15016839-DNA-Binding Proteins, pubmed-meshheading:15016839-Dose-Response Relationship, Drug, pubmed-meshheading:15016839-Humans, pubmed-meshheading:15016839-Leptin, pubmed-meshheading:15016839-Luciferases, pubmed-meshheading:15016839-Phosphorylation, pubmed-meshheading:15016839-Protein Structure, Tertiary, pubmed-meshheading:15016839-RNA, Messenger, pubmed-meshheading:15016839-Receptors, Cell Surface, pubmed-meshheading:15016839-Receptors, Leptin, pubmed-meshheading:15016839-Recombinant Proteins, pubmed-meshheading:15016839-STAT3 Transcription Factor, pubmed-meshheading:15016839-Signal Transduction, pubmed-meshheading:15016839-Trans-Activators, pubmed-meshheading:15016839-Transfection, pubmed-meshheading:15016839-Tyrosine
pubmed:year
2004
pubmed:articleTitle
Modulation of direct leptin signaling by soluble leptin receptor.
pubmed:affiliation
Department of Physiology, The University of Texas Southwestern Medical Center, Dallas, Texas 75390-8854, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't