J.H Gill
MMP-10 is overexpressed, proteolytically active and a potential target for therapeutic intervention in human lung carcinomas
Gill, J.H; Kirwan, I.G; Seargent, J.M; Martin, S.W; Tijani, S; Anikin, V.A; Mearns, A.J; Bibby, M.C; Anthoney, A; Loadman, P.M
Authors
I.G Kirwan
J.M Seargent
S.W Martin
S Tijani
V.A Anikin
A.J Mearns
M.C Bibby
A Anthoney
P.M Loadman
Abstract
Matrix metalloproteinase (MMP)-mediated degradation of the extracellular matrix is a major factor for tumor development and expansion. This study analysed MMP-10 protein expression and activity in human lung tumors of various grade, stage, and type to address the relationship between MMP-10 and tumor characteristics and to evaluate MMP-10 as a therapeutic target in non small cell lung carcinoma (NSCLC). Unlike the majority of MMPs, MMP-10 was located in the tumor mass as opposed to tumor stroma. MMP-10 protein was observed at low levels in normal human lung tissues and at significantly higher levels in all types of NSCLC. No correlation was observed between MMP-10 protein expression and tumor type, stage, or lymph node invasion. To discriminate between active and inactive forms of MMP-10 in samples of human NSCLC, we have developed an ex vivo fluorescent assay. Measurable MMP-10 activity was detected in 42 of 50 specimens of lung cancer and only 2 of 10 specimens of histologically normal lung tissue. No relationship was observed between MMP-10 activity levels and clinicopathologic characteristics. Our results suggest that MMP-10 is expressed and active at high levels in human NSCLC compared to normal lung tissues, and, as such, is a potential target for the development of novel therapeutics for lung cancer treatment.
Citation
Gill, J., Kirwan, I., Seargent, J., Martin, S., Tijani, S., Anikin, V., …Loadman, P. (2004). MMP-10 is overexpressed, proteolytically active and a potential target for therapeutic intervention in human lung carcinomas. Neoplasia, 6(6), 777-785. https://doi.org/10.1593/neo.04283
Journal Article Type | Article |
---|---|
Publication Date | Nov 1, 2004 |
Deposit Date | Jan 9, 2013 |
Journal | Neoplasia |
Print ISSN | 1522-8002 |
Electronic ISSN | 1476-5586 |
Publisher | Elsevier |
Peer Reviewed | Peer Reviewed |
Volume | 6 |
Issue | 6 |
Pages | 777-785 |
DOI | https://doi.org/10.1593/neo.04283 |
Publisher URL | http://www.ncbi.nlm.nih.gov/pubmed/15720804 |
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