rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2009-3-30
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pubmed:abstractText |
Osteoclasts differentiate from macrophage-lineage cells to become specialized for bone resorption function. By a proteomics approach, we found that Lyn was down-regulated by the osteoclast differentiation factor, receptor activator of NF-kappaB ligand (RANKL). The forced reduction of Lyn caused a striking increase in the RANKL-induced PLCgamma1, Ca(2+), and NFATc1 responses during differentiation. These data suggest that Lyn plays a negative role in osteoclastogenesis by interfering with the PLCgamma1-mediated Ca(2+) signaling that leads to NFATc1 activation. Consistent with the in vitro results, in vivo injection of Lyn specific siRNA into mice calvariae provoked a fulminant bone resorption. Our study provides the first evidence of the involvement of Lyn in the negative regulation of osteoclastogenesis by RANKL.
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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/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/NFATC Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Nfatc1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase C gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Plcg1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/RANK Ligand,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/Tnfsf11 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/lyn protein-tyrosine kinase,
http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1873-3468
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
2
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pubmed:volume |
583
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1164-70
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:19285079-Animals,
pubmed-meshheading:19285079-Bone Resorption,
pubmed-meshheading:19285079-Calcium,
pubmed-meshheading:19285079-Calcium Signaling,
pubmed-meshheading:19285079-Cell Differentiation,
pubmed-meshheading:19285079-Cell Line,
pubmed-meshheading:19285079-Down-Regulation,
pubmed-meshheading:19285079-Humans,
pubmed-meshheading:19285079-Mice,
pubmed-meshheading:19285079-NFATC Transcription Factors,
pubmed-meshheading:19285079-Osteoclasts,
pubmed-meshheading:19285079-Phospholipase C gamma,
pubmed-meshheading:19285079-Proteomics,
pubmed-meshheading:19285079-RANK Ligand,
pubmed-meshheading:19285079-RNA, Small Interfering,
pubmed-meshheading:19285079-Skull,
pubmed-meshheading:19285079-src-Family Kinases
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pubmed:year |
2009
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pubmed:articleTitle |
Lyn inhibits osteoclast differentiation by interfering with PLCgamma1-mediated Ca2+ signaling.
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pubmed:affiliation |
Department of Cell and Developmental Biology, Seoul National University, Seoul, Republic of Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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