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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-6-1
pubmed:abstractText
Proteases contribute to tumor invasion and metastasis via their potential to degrade basement membranes and extracellular matrix. Our aim was to compare the level of several proteases: urokinase-type plasminogen activator (u-PA), matrix metalloproteinase 2 (MMP-2; 72-kDa type IV collagenase, also known as gelatinase A), MMP-11 [also known as stromelysin 3 (STR3)], and cathepsins B and L in resected non-small cell lung cancer. Between June 1996 and March 1998, samples of lung tumor tissues were taken from 119 surgically treated patients. Thirty out of the 119 tumor samples were matched with corresponding adjacent normal tissue. u-PA was measured by a commercially available immunoluminometric assay. Metalloproteinases and cathepsins have been evaluated at the RNA level by Northern blot and quantified with a PhosphorImager. Expression of these proteases was compared to the following clinicopathological parameters: pathological diagnosis, tumor size, exposure to asbestos, radiotherapy, neo-adjuvant chemotherapy, tumor-node-metastasis stage, lymph node involvement, presence of metastasis. u-PA, MMP-2, MMP-11/STR3, and cathepsin B were significantly increased in tumor (the tumor:normal ratio was on average increased by 5.4-, 2.2-, 83.5-, and 2.2-fold, respectively). The tumor:normal ratio of MMP-11/ STR3 was found to be significantly linked to the lymph node involvement (P < 0.05). Our results suggest that several proteases are involved in the invasive potential of non-small cell lung cancer and that the quantification of MMP-11/ STR3 could represent an useful prognostic marker.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1078-0432
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1086-92
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10741738-Adult, pubmed-meshheading:10741738-Aged, pubmed-meshheading:10741738-Blotting, Northern, pubmed-meshheading:10741738-Carcinoma, Non-Small-Cell Lung, pubmed-meshheading:10741738-Cathepsin B, pubmed-meshheading:10741738-Cathepsin L, pubmed-meshheading:10741738-Cathepsins, pubmed-meshheading:10741738-Cysteine Endopeptidases, pubmed-meshheading:10741738-Data Interpretation, Statistical, pubmed-meshheading:10741738-Endopeptidases, pubmed-meshheading:10741738-Female, pubmed-meshheading:10741738-Gene Expression Regulation, Neoplastic, pubmed-meshheading:10741738-Humans, pubmed-meshheading:10741738-Immunoassay, pubmed-meshheading:10741738-Lung Neoplasms, pubmed-meshheading:10741738-Lymph Nodes, pubmed-meshheading:10741738-Male, pubmed-meshheading:10741738-Matrix Metalloproteinase 11, pubmed-meshheading:10741738-Matrix Metalloproteinase 2, pubmed-meshheading:10741738-Metalloendopeptidases, pubmed-meshheading:10741738-Middle Aged, pubmed-meshheading:10741738-RNA, Messenger, pubmed-meshheading:10741738-Urokinase-Type Plasminogen Activator
pubmed:year
2000
pubmed:articleTitle
Overexpression level of stromelysin 3 is related to the lymph node involvement in non-small cell lung cancer.
pubmed:affiliation
Laboratoire de Biochimie, Hôpital Claude Huriez, Lille, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't