| pubmed-article:15967115 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15967115 | lifeskim:mentions | umls-concept:C0376358 | lld:lifeskim |
| pubmed-article:15967115 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:15967115 | lifeskim:mentions | umls-concept:C1706515 | lld:lifeskim |
| pubmed-article:15967115 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:15967115 | lifeskim:mentions | umls-concept:C1622501 | lld:lifeskim |
| pubmed-article:15967115 | lifeskim:mentions | umls-concept:C0205242 | lld:lifeskim |
| pubmed-article:15967115 | lifeskim:mentions | umls-concept:C0334227 | lld:lifeskim |
| pubmed-article:15967115 | lifeskim:mentions | umls-concept:C0025543 | lld:lifeskim |
| pubmed-article:15967115 | lifeskim:mentions | umls-concept:C1704640 | lld:lifeskim |
| pubmed-article:15967115 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:15967115 | lifeskim:mentions | umls-concept:C0767106 | lld:lifeskim |
| pubmed-article:15967115 | lifeskim:mentions | umls-concept:C0331858 | lld:lifeskim |
| pubmed-article:15967115 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:15967115 | pubmed:dateCreated | 2005-6-21 | lld:pubmed |
| pubmed-article:15967115 | pubmed:abstractText | Disruption of the extracellular matrix by proteases is crucial for tumor invasion. Laminin-10 (Ln-10) has previously been identified as a substrate for cell migration and cell adhesion, and is present in the basal lamina (BL) of both normal prostate and prostate cancer. Here, we investigate a role for membrane type 1 matrix metalloprotease (MT1-MMP) in modifying this Ln-10-rich BL. MT1-MMP is a transmembrane member of the MMP family that has been demonstrated to be upregulated as prostate cancer progresses from normal to prostate intraepithelial neoplasia to invasive cancer, suggesting a role for MT1-MMP in the invasion of prostate cancer. We show that MT1-MMP cleaves the alpha5 chain of purified human Ln-10 from its 350-kDa form into 310-, 190-, 160-, and 45-kDa fragments. This cleavage causes a decrease in DU-145 prostate cancer cell adhesion to purified Ln-10, and an increase in transmigration of DU-145 cells through cleaved Ln-10. We also show that prostate cancer cells expressing membrane-bound MT1-MMP cleave the alpha5 chain of Ln-10. Ln alpha5-chain cleavage is also observed in human prostate cancer tissues. These findings suggest that prostate cancer cells expressing high levels of MT1-MMP have increased invasive potential through their ability to degrade and invade Ln-10 barriers. | lld:pubmed |
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| pubmed-article:15967115 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15967115 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15967115 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15967115 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15967115 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15967115 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:15967115 | pubmed:issn | 1522-8002 | lld:pubmed |
| pubmed-article:15967115 | pubmed:author | pubmed-author:KultgenPP | lld:pubmed |
| pubmed-article:15967115 | pubmed:author | pubmed-author:NagleRaymond... | lld:pubmed |
| pubmed-article:15967115 | pubmed:author | pubmed-author:CressAnne EAE | lld:pubmed |
| pubmed-article:15967115 | pubmed:author | pubmed-author:McDanielKathy... | lld:pubmed |
| pubmed-article:15967115 | pubmed:author | pubmed-author:SekiguchiKiyo... | lld:pubmed |
| pubmed-article:15967115 | pubmed:author | pubmed-author:ChenMan... | lld:pubmed |
| pubmed-article:15967115 | pubmed:author | pubmed-author:BairElisabeth... | lld:pubmed |
| pubmed-article:15967115 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15967115 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:15967115 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15967115 | pubmed:authorsComplete | Y | lld:pubmed |
