Source:http://linkedlifedata.com/resource/pubmed/id/12060675
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
2002-8-2
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pubmed:abstractText |
Alteration in renal glomerular mesangial cell growth and fibronectin matrix deposition is a hallmark of glomerulosclerosis, which ultimately leads to end-stage renal failure. We have previously shown that the expression of integrin-linked kinase (ILK), a cytoplasmic component of the cell-extracellular matrix contacts, is increased in mesangial cells in human patients with diabetic nephropathy. We show here that ILK forms a complex with PINCH and CH-ILKBP in primary mesangial cells, which are co-clustered at fibrillar adhesions, sites that are involved in fibronectin matrix deposition. To investigate functional significance of the PINCH-ILK-CH-ILKBP complex formation, we expressed the PINCH-binding N-terminal fragment and the CH-ILKBP-binding C-terminal fragment of ILK, respectively, in mesangial cells by using an adenoviral expression system. Overexpression of either the N-terminal fragment or the C-terminal fragment of ILK effectively inhibited the PINCH-ILK-CH-ILKBP complex formation. Inhibition of the PINCH-ILK-CH-ILKBP complex formation significantly reduced fibronectin matrix deposition and inhibited cell proliferation. These results indicate that the PINCH-ILK-CH-ILKBP complex is critically involved in the regulation of mesangial fibronectin matrix deposition and cell proliferation, and suggest that it may potentially serve as a useful target in the therapeutic control of progressive renal failure and other pathological processes involving abnormal cell proliferation and fibronectin matrix deposition.
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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/Actinin,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PARVA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/PARVB protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/integrin-linked kinase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1530-6860
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1298-300
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:12060675-Actinin,
pubmed-meshheading:12060675-Animals,
pubmed-meshheading:12060675-Carrier Proteins,
pubmed-meshheading:12060675-Cell Adhesion,
pubmed-meshheading:12060675-Cell Division,
pubmed-meshheading:12060675-Cells, Cultured,
pubmed-meshheading:12060675-DNA-Binding Proteins,
pubmed-meshheading:12060675-Extracellular Matrix,
pubmed-meshheading:12060675-Fibronectins,
pubmed-meshheading:12060675-Glomerular Mesangium,
pubmed-meshheading:12060675-Macromolecular Substances,
pubmed-meshheading:12060675-Microfilament Proteins,
pubmed-meshheading:12060675-Models, Biological,
pubmed-meshheading:12060675-Peptide Fragments,
pubmed-meshheading:12060675-Protein-Serine-Threonine Kinases,
pubmed-meshheading:12060675-Rats,
pubmed-meshheading:12060675-Transfection
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pubmed:year |
2002
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pubmed:articleTitle |
Regulation of fibronectin matrix deposition and cell proliferation by the PINCH-ILK-CH-ILKBP complex.
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pubmed:affiliation |
Department of Pathology, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, USA.
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pubmed:publicationType |
Journal Article
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