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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5674
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pubmed:dateCreated |
2004-5-24
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pubmed:databankReference |
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pubmed:abstractText |
Resistin, founding member of the resistin-like molecule (RELM) hormone family, is secreted selectively from adipocytes and induces liver-specific antagonism of insulin action, thus providing a potential molecular link between obesity and diabetes. Crystal structures of resistin and RELMbeta reveal an unusual multimeric structure. Each protomer comprises a carboxy-terminal disulfide-rich beta-sandwich "head" domain and an amino-terminal alpha-helical "tail" segment. The alpha-helical segments associate to form three-stranded coiled coils, and surface-exposed interchain disulfide linkages mediate the formation of tail-to-tail hexamers. Analysis of serum samples shows that resistin circulates in two distinct assembly states, likely corresponding to hexamers and trimers. Infusion of a resistin mutant, lacking the intertrimer disulfide bonds, in pancreatic-insulin clamp studies reveals substantially more potent effects on hepatic insulin sensitivity than those observed with wild-type resistin. This result suggests that processing of the intertrimer disulfide bonds may reflect an obligatory step toward activation.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adiponectin,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Conditioned,
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Hormones, Ectopic,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RETN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Resistin,
http://linkedlifedata.com/resource/pubmed/chemical/Retn protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Retnlb protein, mouse
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
21
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pubmed:volume |
304
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1154-8
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:15155948-Adipocytes,
pubmed-meshheading:15155948-Adiponectin,
pubmed-meshheading:15155948-Amino Acid Sequence,
pubmed-meshheading:15155948-Animals,
pubmed-meshheading:15155948-Cell Line,
pubmed-meshheading:15155948-Crystallization,
pubmed-meshheading:15155948-Crystallography, X-Ray,
pubmed-meshheading:15155948-Culture Media, Conditioned,
pubmed-meshheading:15155948-Disulfides,
pubmed-meshheading:15155948-Glucose,
pubmed-meshheading:15155948-Hormones, Ectopic,
pubmed-meshheading:15155948-Humans,
pubmed-meshheading:15155948-Insulin,
pubmed-meshheading:15155948-Insulin Resistance,
pubmed-meshheading:15155948-Intercellular Signaling Peptides and Proteins,
pubmed-meshheading:15155948-Liver,
pubmed-meshheading:15155948-Mice,
pubmed-meshheading:15155948-Molecular Sequence Data,
pubmed-meshheading:15155948-Molecular Weight,
pubmed-meshheading:15155948-Mutation,
pubmed-meshheading:15155948-Protein Folding,
pubmed-meshheading:15155948-Protein Structure, Quaternary,
pubmed-meshheading:15155948-Protein Structure, Secondary,
pubmed-meshheading:15155948-Protein Structure, Tertiary,
pubmed-meshheading:15155948-Proteins,
pubmed-meshheading:15155948-Resistin
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pubmed:year |
2004
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pubmed:articleTitle |
Disulfide-dependent multimeric assembly of resistin family hormones.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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