Browse > Article

Activity of Matrix Metalloproteinase-2 and its Significance after Resection of Stage I Non-small Cell Lung Cancer  

Kim Sang Hui (Cancer Research Center for Clinical Research, Samsung Biomedical Research Institue)
Hong Young-Sook (Department of Biochemistry, College of Medicine, Ewha Womans University)
Lee Jinseon (Cancer Research Center for Clinical Research, Samsung Biomedical Research Institue)
Son Dae-Soon (Cancer Research Center for Clinical Research, Samsung Biomedical Research Institue)
Lim Yu-Sung (Cancer Research Center for Clinical Research, Samsung Biomedical Research Institue)
Song In-Seung (Cancer Research Center for Clinical Research, Samsung Biomedical Research Institue)
Lee Hye-Sook (Cancer Research Center for Clinical Research, Samsung Biomedical Research Institue)
Kim Do Hun (Department of Thoracic and Cardiovascular Surgery, Samsung Medical Center, Sungkyunkwan University School of Medicine)
Kim Jingook (Department of Thoracic and Cardiovascular Surgery, Samsung Medical Center, Sungkyunkwan University School of Medicine)
Choi Yong Soo (Department of Thoracic and Cardiovascular Surgery, Samsung Medical Center, Sungkyunkwan University School of Medicine)
Publication Information
Journal of Chest Surgery / v.38, no.1, 2005 , pp. 38-43 More about this Journal
Abstract
Matrix metalloproteinase-2 (MMP-2) is a class of proteolytic enzymes that digest collagen type IV and other components of the basement membrane. It plays a key role in the local invasion and the formation of distant metastases by various malignant tumors. The aim of this study was to evaluate the activity of MMP-2 and its significance as a prognostic marker in resected stage I non-small cell lung cancer (NSCLC). Material and Method: In this study we obtained fresh-frozen samples of tumor and non-tumor tissues from 34 patients with stage I NSCLC who underwent resection without preoperative radiotherapy or chemotherapy. After the extraction of total protein from tissue samples, MMP-2 activities were assessed by gelatin-substrate-zymography. The activities were divided into the higher or lower groups. Result: The MMP-2 activities were higher in tumor tissues than in non-tumor tissues. The MMP-2 activity of non-tumor tissues in recurrent group was higher than in non-recurrent group (p<0.01). Also the patients with higher MMP-2 activity of non-tumor tissues showed poor 5 year survival (p<0.01). Conclusion: This result indicates that the higher level of MMP-2 activity in the non-tumor tissue is associated with the recurrence and survival after the resection of stage I NSCLC. Therefore, MMP-2 activity in the non-tumor tissue could be used as a potential prognostic marker for the resected stage I-NSCLC.
Keywords
Lung neoplasms; Cell biology; Neoplasm proteins; Neoplasm outcomes;
Citations & Related Records
연도 인용수 순위
  • Reference
1 Lyons JG, Birkedal-Hansen B, Moore WG, O'Grady RL, Birkedal-Hansen H. Characteristics of a 95-kDa matrix metalloproteinase produced by mammary carcinoma cells. Biochemistry 1991;30:1449-56   DOI   ScienceOn
2 Polette M, Clavel C, Muller D, Abecassis J, Binninger I, Birembaut P. Detection of mRNAs encoding collagenase I and stromelysin 2 in carcinomas of the head and neck by In situ hybridization. Invasion Metastasis 1991;11:76-83
3 Liabakk NB, Talbot I, Smith RA, Wilkinson K, Balkwill F. Matrix metalloprotease 2 (MMP-2) and matrix metalloprotease 9 (MMP-9) type IV collagenases in colorectal cancer. Cancer Res 1996;56:190-6
4 Passlick B, Sienel W, Seen-Hibler R, et al. Overexpression of matrix metalloproteinase 2 predicts unfavorable outcome in early-stage non-small cell lung cancer. Clin Cancer Res 2000;6:3944-8
5 Moses MA. The regulation of neovascularization by matrix metalloproteinases & their inhibitors. Stem Cells 1997;15:180   DOI   PUBMED   ScienceOn
6 Stetler-Stevenson WG, Liotta LA, Kleiner DE Jr. Extracellular matrix 6: role of matrix metalloproteinases in tumor invasion and metastasis. FASEB J 1993;7:1434-41   DOI
7 Michael M, Babic B, Khokha R, et al. Expression and prognostic significance of metalloproteinases and their tissue inhibitors in patients with small-cell lung cancer. J Clin Oncol 1999;17:1802-8   DOI
8 Powell WC, Knox JD, Navre M, et al. Expression of the metalloproteinase matrilysin in DU-145 cells increases their invasive potential in severe combined immunodeficient mice. Cancer Res 1993;53:417-22
9 Mackay AR, Gomez DE, Cottam DW, Rees RC, Nason AM, Thorgeirsson UP. Identification of the 72-kDa (MMP-2) and 92-kDa (MMP-9) gelatinase/type IV collagenase in preparations of laminin and Matrigel. Biotechniques 1993;15: 1048-51
10 Nakagawa T, Kubota T, Kabuto M, et al. Production of matrix metalloproteinases and tissue inhibitor of metalloproteinases- 1 by human brain tumors. J Neurosurg 1994;81: 69-77   DOI   ScienceOn
11 Chamber AF, Matrisian LM. Changing views of the role of matrix metalloproteinases in metastasis. J Natl Cancer Inst 1997;89:1279
12 Nagase H, Woessner JF Jr. Matrix metalloproteinases. J Biol Chem 1999;274:21491   DOI
13 Crawford HC, Matrisian LM. Mechanisms controlling the transcription of matrix metalloproteinase genes in normal and neoplastic cells. Enzyme Protein 1996;49:20-37   DOI
14 Cox G, Jones JL, O'Byrne KJ. Matrix metalloproteinase 9 and the epidermal growth factor signal pathway in operable non-small cell lung cancer. Clin Cancer Res 2000;6:2349-55
15 Van Wart HE, Birkedal-Hansen H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci U.S.A 1990;87:5578   DOI   ScienceOn
16 Delebecq TJ, Porte H, Zerimech F, et al. Overexpression level of stromelysin 3 is related to the lymph node involvement in non-small cell lung cancer. Clin Cancer Res 2000;6:1086-92
17 Thomas P, Khokha R, Shepherd FA, Feld R, Tsao M. Differential expression of matrix metalloproteinases and their inhibitors in non-small cell lung cancer. J Pathol 2000;190: 150-6   DOI   ScienceOn
18 Liotta LA, Steeg PS, Stetler-Stevenson WG. Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation. Cell. 1991;64:327-36   DOI   ScienceOn
19 Ray JM, Stetler-Stevenson WG. The role of matrix metalloproteases and their inhibitors in tumour invasion, metastasis and angiogenesis. Eur Respir J 1994;7:2062-72
20 Sreenath T, Matrisian LM, Stetler-Stevenson W, Gattoni-Celli S, Pozzatti RO. Expression of matrix metalloproteinase genes in transformed rat cell lines of high and low metastatic potential. Cancer Res 1992;52:4942-7
21 Tryggvason K, Hoyhtya M, Pyke C. Type IV collagenase in invasive tumors. Breast Cancer Res Treat 1993;24:209-18   DOI   ScienceOn
22 Shima I, Sasaguri Y, Kusukawa J, et al. Production of matrix metalloproteinase-2 and metalloproteinase-3 related to malignant behavior of esophageal carcinoma. A clinicopathologic study. Cancer 1992;70:2747-53   DOI   PUBMED   ScienceOn