Source:http://linkedlifedata.com/resource/pubmed/id/20735983
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2010-10-4
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pubmed:abstractText |
The aggregation of chondroprogenitor mesenchymal cells into precartilage condensation represents one of the earliest events in chondrogenesis. N-cadherin is a key cell adhesion molecule implicated in chondrogenic differentiation. Recently, ADAM10-mediated cleavage of N-cadherin has been reported to play an important role in cell adhesion, migration, development and signaling. However, the significance of N-cadherin cleavage in chondrocyte differentiation has not been determined. In the present study, we found that the protein turnover of N-cadherin is accelerated during the early phase of chondrogenic differentiation in ATDC5 cells. Therefore, we generated the subclones of ATDC5 cells overexpressing wild-type N-cadherin, and two types of subclones overexpressing a cleavage-defective N-cadherin mutant, and examined the response of these cells to insulin stimulation. The ATDC5 cells overexpressing cleavage-defective mutants severely prevented the formation of cartilage aggregates, proteoglycan production and the induction of chondrocyte marker gene expression, such as type II collagen, aggrecan and type X collagen. These results suggested that the cleavage of N-cadherin is essential for chondrocyte differentiation.
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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/ADAM Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ADAM10 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid Precursor Protein Secretases,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/CDH2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1090-2104
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2010 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
400
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
493-9
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pubmed:meshHeading |
pubmed-meshheading:20735983-ADAM Proteins,
pubmed-meshheading:20735983-Amino Acid Sequence,
pubmed-meshheading:20735983-Amyloid Precursor Protein Secretases,
pubmed-meshheading:20735983-Animals,
pubmed-meshheading:20735983-Antigens, CD,
pubmed-meshheading:20735983-Cadherins,
pubmed-meshheading:20735983-Cartilage,
pubmed-meshheading:20735983-Cell Differentiation,
pubmed-meshheading:20735983-Cell Line, Tumor,
pubmed-meshheading:20735983-Chondrocytes,
pubmed-meshheading:20735983-Chondrogenesis,
pubmed-meshheading:20735983-Humans,
pubmed-meshheading:20735983-Membrane Proteins,
pubmed-meshheading:20735983-Mice,
pubmed-meshheading:20735983-Molecular Sequence Data,
pubmed-meshheading:20735983-Mutation,
pubmed-meshheading:20735983-Proteoglycans
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pubmed:year |
2010
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pubmed:articleTitle |
The cleavage of N-cadherin is essential for chondrocyte differentiation.
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pubmed:affiliation |
Department of Orthopaedic Surgery, Mie University Graduate School of Medicine, 2-174, Edobashi, Tsu-city, Mie 514-8507, Japan.
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pubmed:publicationType |
Journal Article
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