ArticleJournal of cancer research and clinical oncology2005
Matrix metalloproteinases 2 and 9 in oral squamous cell carcinomas: manifestation and localization of their activity.
Article in Journal of cancer research and clinical oncology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.
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Who cites it
27 citing papers in PubMed, 1 synthesis or guideline pooled it, 67 citations in OpenAlex.
- Pooled it
- Immunohistochemical expression of matrix metalloproteinase-9 and 13 in oral squamous cell carcinoma and their role in predicting lymph node metastasis.World journal of methodology · 2025Article
- Diagnostic and Prognostic Accuracy of MMPs and TIMPs in Oral Cancer Patients on Enzyme-Linked Immunosorbent Assay (ELISA) as Compared to Immunohistochemistry (IHC).Indian journal of surgical oncology · 2025Article
- Serum Concentration of MMP-9 as a Predictive Biomarker for the Progression of Oral Cancer.Journal of maxillofacial and oral surgery · 2024Article
- Article
- Estimation of serum and salivary matrix metalloproteinase levels in oral squamous cell carcinoma patients: a systematic review and meta-analysis.Postepy dermatologii i alergologii · 2021Review
- Ethanolic Extract of Ocimum sanctum Leaves Reduced Invasion and Matrix Metalloproteinase Activity of Head and Neck Cancer Cell Lines.Asian Pacific journal of cancer prevention : APJCP · 2020Article
- miR‑148a modulates the viability, migration and invasion of oral squamous cell carcinoma cells by regulating HLA‑G expression.Molecular medicine reports · 2019Article
- Matrix metalloproteinases (MMPs) and inhibitor of metalloproteinases (TIMP) mRNA and protein expression in laryngeal squamous cell carcinoma.Archives of medical science : AMS · 2019Article
- Article
- Mesenchymal Stem Cells Promote Tumor Progression via Inducing Stroma Remodeling on Rabbit VX2 Bladder Tumor Model.International journal of biological sciences · 2018Article
- [Effects of geranylgeranyltransferase Ⅰ gene silencing by RNA interference on the migration and invasion of tongue carcinoma].Hua xi kou qiang yi xue za zhi = Huaxi kouqiang yixue zazhi = West China journal of stomatology · 2017Article
- May High MMP-2 and TIMP-2 Expressions Increase or Decrease the Aggressivity of Oral Cancer?Pathology oncology research : POR · 2017Article
- Deregulated Levels of the NF-κB1, NF-κB2, and Rel Genes in Ukrainian Patients with Leukemia and Lymphoma in the Post-Chernobyl Period.Turkish journal of haematology : official journal of Turkish Society of Haematology · 2016Article
- Review
- Bortezomib and Arsenic Trioxide Activity on a Myelodysplastic Cell Line (P39): A Gene Expression Study.Turkish journal of haematology : official journal of Turkish Society of Haematology · 2015Article
- Prognostic value of matrix metalloproteinases in oral squamous cell carcinoma.Biotechnology, biotechnological equipment · 2014Article
- The tumor microenvironment contribution to development, growth, invasion and metastasis of head and neck squamous cell carcinomas.Journal of Cancer · 2013Article
- Fluctuating roles of matrix metalloproteinase-9 in oral squamous cell carcinoma.TheScientificWorldJournal · 2013Review
- Gene Expression Signatures of Lymph Node Metastasis in Oral Cancer: Molecular Characteristics and Clinical Significances.Current cancer therapy reviews · 2010Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeThe process of invasion and metastasis is closely related to the prognosis of oral squamous cell carcinoma (OSCC). Matrix metalloproteinases (MMPs) are a group of enzymes characterized by their ability to degrade extracellular matrix proteins and contribute to the tumor invasion and metastasis. Especially MMP-2 and MMP-9 are known to be related to destruction of basement membrane as collagenases. This study focused on protein expression of MMP-2 and MMP-9 and their extracellular matrix degradation activity in OSCCs.
methodsFreshly frozen samples from 31 OSCC patients were analyzed for the localization and activity of MMP-2 and MMP-9. Serial frozen sections were used by routine hematoxylin and eosin staining, immunohistochemistry for MMP-2 and MMP-9, and film in situ zymography (FIZ) for gelatinolytic activity. We also evaluated the activity of MMP-2 and MMP-9 by zymography using the same samples as frozen sections. The activated form/proform ratio of MMPs in zymography was evaluated using an image scanner.
resultsIn MMP-2 the proportion in T3 and T4 clinical stage groups was significantly higher than that in T1 and T2. The proportion in lymph node metastasis cases (N+) was also significantly higher than that in non-lymph node metastasis cases (N-). In contrast to MMP-2, the activated form/proform ratio of MMP-9 was very low, suggesting that MMP-9 is not activated in the matrix degradation of OSCC, although both MMP-2 and MMP-9 protein expression are presented in tumor cells. FIZ revealed MMP in both tumor cells and stromal cells of 70% of the N+ cases and of 47.6% of the N- cases.
conclusionsThese results indicate that two types of proform and activated form matrix metalloproteinases, MMP-2 and MMP-9, are present in human OSCC, and that the activated MMP-2 could be a main enzymatic activity of gelatinolysis in OSCC. Interaction of tumor cells and stromal cells seems to play an important role in the invasion and metastasis of human OSCC. Combination analysis of zymography and FIZ is a useful method to detect activity and localization of MMPs in human OSCC.
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Registered trials
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