rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2006-1-26
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pubmed:abstractText |
Smooth muscle cell (SMC) migration from the tunica media to the intima, a key event in neointimal formation, requires proteolytic degradation of elastin-rich extracellular matrix barriers. Although cathepsin S (Cat S) is overexpressed in atherosclerotic and neointimal lesions, its exact role in SMC behavior remains primarily unresolved. We examined the involvement of Cat S on SMC migration through an extracellular matrix barrier and its localization in SMCs. A selective Cat S inhibitor and the endogenous inhibitor cystatin C significantly attenuated SMC invasion across elastin gel. Western blotting and cell surface biotinylation analysis demonstrated localization of the 28-kd active form of Cat S on the SMC surface, consistent with its role in the proteolysis of subcellular matrices. Treatment with interferon-gamma or interleukin-beta1 significantly augmented the ability of SMC membranes to degrade elastin along with a significant increase in the level of active Cat S compared with controls. Immunofluorescence and confocal microscopy showed a punctuated pattern of Cat S clusters at the periphery of SMCs; further studies demonstrated partial co-localization of Cat S and integrin alphanubeta3 at the cell surfaces. These findings demonstrate that active Cat S co-localizes with integrin alphanubeta3 as a receptor on the SMC surface, playing an important role in the invasive behavior of SMCs.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-10197640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-10362800,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-10764664,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-10993910,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-11120602,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-12149463,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-12538657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-12600886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-12639996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-12939223,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-14645229,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-15297830,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-2129023,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-2744464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-3022933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-3948167,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-6368589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-7542249,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-8013081,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-8157683,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-9521728,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16436681-9691094
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antineoplastic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/CST3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins,
http://linkedlifedata.com/resource/pubmed/chemical/Cst3 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Cystatin C,
http://linkedlifedata.com/resource/pubmed/chemical/Cystatins,
http://linkedlifedata.com/resource/pubmed/chemical/Elastin,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin alphaVbeta3,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/cathepsin S
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0002-9440
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pubmed:author |
pubmed-author:ChengXian WuXW,
pubmed-author:GuiL XLX,
pubmed-author:IguchiAkihisaA,
pubmed-author:KandaShigeruS,
pubmed-author:KuzuyaMasafumiM,
pubmed-author:LiuZexuanZ,
pubmed-author:MuroharaToyoakiT,
pubmed-author:NakamuraKaeK,
pubmed-author:OngGG,
pubmed-author:SasakiTakeshiT,
pubmed-author:ShiGuo-PingGP,
pubmed-author:YokotaMitsuhiroM
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pubmed:issnType |
Print
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pubmed:volume |
168
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
685-94
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16436681-Humans,
pubmed-meshheading:16436681-Animals,
pubmed-meshheading:16436681-Cattle,
pubmed-meshheading:16436681-Rats,
pubmed-meshheading:16436681-Aorta,
pubmed-meshheading:16436681-Cathepsins,
pubmed-meshheading:16436681-Elastin,
pubmed-meshheading:16436681-Antineoplastic Agents,
pubmed-meshheading:16436681-Cell Membrane,
pubmed-meshheading:16436681-Cells, Cultured,
pubmed-meshheading:16436681-RNA, Messenger,
pubmed-meshheading:16436681-Fluorescent Antibody Technique,
pubmed-meshheading:16436681-Subcellular Fractions,
pubmed-meshheading:16436681-Cell Movement,
pubmed-meshheading:16436681-Muscle, Smooth, Vascular,
pubmed-meshheading:16436681-Tunica Intima,
pubmed-meshheading:16436681-Extracellular Matrix,
pubmed-meshheading:16436681-Immunoprecipitation,
pubmed-meshheading:16436681-Interferon-gamma,
pubmed-meshheading:16436681-Interleukin-1,
pubmed-meshheading:16436681-Cystatin C,
pubmed-meshheading:16436681-Cystatins,
pubmed-meshheading:16436681-Blotting, Western
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