pubmed-article:12727852 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12727852 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
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pubmed-article:12727852 | lifeskim:mentions | umls-concept:C1622501 | lld:lifeskim |
pubmed-article:12727852 | lifeskim:mentions | umls-concept:C0205242 | lld:lifeskim |
pubmed-article:12727852 | lifeskim:mentions | umls-concept:C1518174 | lld:lifeskim |
pubmed-article:12727852 | lifeskim:mentions | umls-concept:C1171362 | lld:lifeskim |
pubmed-article:12727852 | lifeskim:mentions | umls-concept:C0025543 | lld:lifeskim |
pubmed-article:12727852 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:12727852 | lifeskim:mentions | umls-concept:C0171955 | lld:lifeskim |
pubmed-article:12727852 | lifeskim:mentions | umls-concept:C1420841 | lld:lifeskim |
pubmed-article:12727852 | lifeskim:mentions | umls-concept:C2698300 | lld:lifeskim |
pubmed-article:12727852 | lifeskim:mentions | umls-concept:C1515670 | lld:lifeskim |
pubmed-article:12727852 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
pubmed-article:12727852 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:12727852 | lifeskim:mentions | umls-concept:C0337112 | lld:lifeskim |
pubmed-article:12727852 | pubmed:issue | 9 | lld:pubmed |
pubmed-article:12727852 | pubmed:dateCreated | 2003-5-2 | lld:pubmed |
pubmed-article:12727852 | pubmed:abstractText | Degradation of the extracellular matrix by proteolytic enzymes is a central aspect of physiological and pathologic tissue-remodeling processes such as trophoblastic implantation, wound healing, and tumor invasion. We have hypothesized that prostate adenocarcinoma cell invasion through the normal basal lamina is attributable in part to metalloproteinase-induced cleavage of laminin-5 (Ln-5) and enhanced motility of the cancer cells. We studied the role of membrane type-1-matrix metalloproteinase (MT1-MMP) expressed on the surface of prostate tumor cells in cleaving Ln-5 and enhancing the migration of prostate tumor cells. We also determined the nature of the MT1-MMP cleavage of human Ln-5 and how this altered Ln-5 changes the migration of prostate carcinoma cells. We found that human MT1-MMP cleaves purified human Ln-5 to an 80-kDa fragment. Mass spectrometry analyses of the 80-kDa cleaved product by trypsin and chymotrypsin gave 14 and 9 different peptide sequences, respectively, that were identical to the expected amino acid sequence of the Ln-5-beta3 chain. The recovered peptides represent 14.4% (trypsin) and 10.3% (chymotrypsin) of Ln-5-beta3 chain by amino acid count. Both trypsin and chymotrypsin digestion of MT1-MMP-cleaved product of Ln-5 did not show any other peptides that were identical to the other chains of Ln-5. Using a linear migration assay we found that the Ln-5 cleaved by MT1-MMP enhanced the migration of DU-145 prostate carcinoma cells by 2-fold compared with uncleaved Ln-5. The use of blocked antisense MT1-MMP oligonucleotides inhibited the migration of DU-145 cells on Ln-5. We also found that the prostate carcinoma cells expressing high levels of MT1-MMP, such as PC3N and PPC, demonstrated enhanced migration on human Ln-5-coated substrate, and this migration was inhibited using blocked antisense MT1-MMP oligonucleotides. In conclusion, this is a novel and important finding where we have shown that beta3-chain is cleaved by MT1-MMP, and this cleavage enhances migration of prostate cancer cells. | lld:pubmed |
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pubmed-article:12727852 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:12727852 | pubmed:language | eng | lld:pubmed |
pubmed-article:12727852 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12727852 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:12727852 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12727852 | pubmed:month | May | lld:pubmed |
pubmed-article:12727852 | pubmed:issn | 0008-5472 | lld:pubmed |
pubmed-article:12727852 | pubmed:author | pubmed-author:NagleRaymond... | lld:pubmed |
pubmed-article:12727852 | pubmed:author | pubmed-author:CressAnne EAE | lld:pubmed |
pubmed-article:12727852 | pubmed:author | pubmed-author:BowdenG... | lld:pubmed |
pubmed-article:12727852 | pubmed:author | pubmed-author:UdayakumarThi... | lld:pubmed |
pubmed-article:12727852 | pubmed:author | pubmed-author:ChenMan... | lld:pubmed |
pubmed-article:12727852 | pubmed:author | pubmed-author:BairElisabeth... | lld:pubmed |
pubmed-article:12727852 | pubmed:author | pubmed-author:Von... | lld:pubmed |
pubmed-article:12727852 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12727852 | pubmed:day | 1 | lld:pubmed |
pubmed-article:12727852 | pubmed:volume | 63 | lld:pubmed |
pubmed-article:12727852 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12727852 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12727852 | pubmed:pagination | 2292-9 | lld:pubmed |
pubmed-article:12727852 | pubmed:dateRevised | 2009-10-6 | lld:pubmed |
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pubmed-article:12727852 | pubmed:meshHeading | pubmed-meshheading:12727852... | lld:pubmed |
pubmed-article:12727852 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12727852 | pubmed:articleTitle | Membrane type-1-matrix metalloproteinase expressed by prostate carcinoma cells cleaves human laminin-5 beta3 chain and induces cell migration. | lld:pubmed |
pubmed-article:12727852 | pubmed:affiliation | Department of Radiation Oncology, Arizona Cancer Center, The University of Arizona, Tucson 85724-5024, USA. | lld:pubmed |
pubmed-article:12727852 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12727852 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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