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. 2004 Apr;13(2):105–109. doi: 10.1080/09629350410001688549

The presence of promatrix metalloproteinase-3 and its relation with different categories of coal workers' pneumoconiosis.

Remzi Altin 1, Levent Kart 1, Ishak Tekin 1, Ferah Armutcu 1, Meltem Tor 1, Tacettin Ornek 1
PMCID: PMC1781544  PMID: 15203551

Abstract

Extracellular matrix formation (ECM) and remodeling are critical events related to the pathogenesis of pulmonary fibrosis. Matrix metalloproteinases play an essential role in degrading and remodeling the ECM. In this study, we tried to show the presence and correlation of promatrix metalloproteinase-3 (proMMP-3) (the inactive form of metalloproteinase-3) levels in coal workers' pneumoconiosis (CWP) with different categories. The study population consisted of 44 coal miners with CWP (pos CWP). Coal miners without CWP (neg CWP, n = 24) and non-underground personnel (controls, n = 17) were taken as controls. All coal miners were stable and had no systemic infection or disease. Standard posterio-anterior chest radiographs and pulmonary function tests were performed to exclude any diseases other than CWP. Serum proMMP-3 was analysed using the sandwich enzyme-linked immunosorbent assay according to the manufacturer's instructions (The Binding Site, Birmingham, UK). Mean proMMP-3 values of the all three groups were compared and a significant statistical difference obtained (p < 0.001). In addition, a statistically significant difference was found between categories of the disease and proMMP-3 values (p < 0.05). The effects of age, exposure duration and cigarette smoking on proMMP-3 values in coal miners with CWP were investigated. There were no correlations between age, smoking and proMMP-3 values. However, a positive correlation was found between exposure duration and proMMP-3 values (r = 0.447, p = 0.008). In conclusion, proMMP-3 (prostromelysin 1) may play an essential role in degrading and remodeling the ECM in workers with pneumoconiosis. ProMMP-3 may also reflect the stage of pneumoconiosis disease.

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Selected References

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  1. Allan J. A., Hembry R. M., Angal S., Reynolds J. J., Murphy G. Binding of latent and high Mr active forms of stromelysin to collagen is mediated by the C-terminal domain. J Cell Sci. 1991 Aug;99(Pt 4):789–795. doi: 10.1242/jcs.99.4.789. [DOI] [PubMed] [Google Scholar]
  2. Ashcroft G. S., Horan M. A., Herrick S. E., Tarnuzzer R. W., Schultz G. S., Ferguson M. W. Age-related differences in the temporal and spatial regulation of matrix metalloproteinases (MMPs) in normal skin and acute cutaneous wounds of healthy humans. Cell Tissue Res. 1997 Dec;290(3):581–591. doi: 10.1007/s004410050963. [DOI] [PubMed] [Google Scholar]
  3. Birkedal-Hansen H., Moore W. G., Bodden M. K., Windsor L. J., Birkedal-Hansen B., DeCarlo A., Engler J. A. Matrix metalloproteinases: a review. Crit Rev Oral Biol Med. 1993;4(2):197–250. doi: 10.1177/10454411930040020401. [DOI] [PubMed] [Google Scholar]
  4. Brown G. M., Brown D. M., Donaldson K. Persistent inflammation and impaired chemotaxis of alveolar macrophages on cessation of dust exposure. Environ Health Perspect. 1992 Jul;97:91–94. doi: 10.1289/ehp.929791. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Constantin Arnaud, Lauwers-Cancès Valérie, Navaux Frédérique, Abbal Michel, van Meerwijk Joost, Mazières Bernard, Cambon-Thomsen Anne, Cantagrel Alain. Stromelysin 1 (matrix metalloproteinase 3) and HLA-DRB1 gene polymorphisms: Association with severity and progression of rheumatoid arthritis in a prospective study. Arthritis Rheum. 2002 Jul;46(7):1754–1762. doi: 10.1002/art.10336. [DOI] [PubMed] [Google Scholar]
  6. Gomez D. E., Alonso D. F., Yoshiji H., Thorgeirsson U. P. Tissue inhibitors of metalloproteinases: structure, regulation and biological functions. Eur J Cell Biol. 1997 Oct;74(2):111–122. [PubMed] [Google Scholar]
  7. Guo L., Hussain A. A., Limb G. A., Marshall J. Age-dependent variation in metalloproteinase activity of isolated human Bruch's membrane and choroid. Invest Ophthalmol Vis Sci. 1999 Oct;40(11):2676–2682. [PubMed] [Google Scholar]
  8. Katrib A., Tak P. P., Bertouch J. V., Cuello C., McNeil H. P., Smeets T. J., Kraan M. C., Youssef P. P. Expression of chemokines and matrix metalloproteinases in early rheumatoid arthritis. Rheumatology (Oxford) 2001 Sep;40(9):988–994. doi: 10.1093/rheumatology/40.9.988. [DOI] [PubMed] [Google Scholar]
  9. Klimiuk P. A., Sierakowski S., Latosiewicz R., Cylwik B., Skowronski J., Chwiecko J. Serum matrix metalloproteinases and tissue inhibitors of metalloproteinases in different histological variants of rheumatoid synovitis. Rheumatology (Oxford) 2002 Jan;41(1):78–87. doi: 10.1093/rheumatology/41.1.78. [DOI] [PubMed] [Google Scholar]
  10. Kuhn D. C., Stauffer J. L., Gaydos L. J., Demers L. M. Inflammatory and fibrotic mediator release by alveolar macrophages from coal miners. J Toxicol Environ Health. 1995 Sep;46(1):9–21. doi: 10.1080/15287399509532014. [DOI] [PubMed] [Google Scholar]
  11. Liu Ping-Yen, Chen Jyh-Hong, Li Yi-Heng, Wu Hua-Lin, Shi Guey-Yueh. Synergistic effect of stromelysin-1 (matrix metallo-proteinase-3) promoter 5A/6A polymorphism with smoking on the onset of young acute myocardial infarction. Thromb Haemost. 2003 Jul;90(1):132–139. [PubMed] [Google Scholar]
  12. Manicourt D. H., Fujimoto N., Obata K., Thonar E. J. Serum levels of collagenase, stromelysin-1, and TIMP-1. Age- and sex-related differences in normal subjects and relationship to the extent of joint involvement and serum levels of antigenic keratan sulfate in patients with osteoarthritis. Arthritis Rheum. 1994 Dec;37(12):1774–1783. doi: 10.1002/art.1780371211. [DOI] [PubMed] [Google Scholar]
  13. Posthumus M. D., Limburg P. C., Westra J., Cats H. A., Stewart R. E., van Leeuwen M. A., van Rijswijk M. H. Serum levels of matrix metalloproteinase-3 in relation to the development of radiological damage in patients with early rheumatoid arthritis. Rheumatology (Oxford) 1999 Nov;38(11):1081–1087. doi: 10.1093/rheumatology/38.11.1081. [DOI] [PubMed] [Google Scholar]
  14. Rom W. N. Basic mechanisms leading to focal emphysema in coal workers' pneumoconiosis. Environ Res. 1990 Oct;53(1):16–28. doi: 10.1016/s0013-9351(05)80127-6. [DOI] [PubMed] [Google Scholar]
  15. Shapiro S. D., Senior R. M. Matrix metalloproteinases. Matrix degradation and more. Am J Respir Cell Mol Biol. 1999 Jun;20(6):1100–1102. doi: 10.1165/ajrcmb.20.6.f151. [DOI] [PubMed] [Google Scholar]
  16. Soleilhac J. M., Lafuma C., Porcher J. M., Auburtin G., Roques B. P. Characterization of a soluble form of neutral endopeptidase-24.11 (EC 3.4.24.11) in human serum: enhancement of its activity in serum of underground miners exposed to coal dust particles. Eur J Clin Invest. 1996 Nov;26(11):1011–1017. doi: 10.1046/j.1365-2362.1996.2420580.x. [DOI] [PubMed] [Google Scholar]
  17. Suzuki K., Kan C. C., Hung W., Gehring M. R., Brew K., Nagase H. Expression of human pro-matrix metalloproteinase 3 that lacks the N-terminal 34 residues in Escherichia coli: autoactivation and interaction with tissue inhibitor of metalloproteinase 1 (TIMP-1). Biol Chem. 1998 Feb;379(2):185–191. doi: 10.1515/bchm.1998.379.2.185. [DOI] [PubMed] [Google Scholar]
  18. Vaillant P., Menard O., Vignaud J. M., Martinet N., Martinet Y. The role of cytokines in human lung fibrosis. Monaldi Arch Chest Dis. 1996 Apr;51(2):145–152. [PubMed] [Google Scholar]
  19. Visse Robert, Nagase Hideaki. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ Res. 2003 May 2;92(8):827–839. doi: 10.1161/01.RES.0000070112.80711.3D. [DOI] [PubMed] [Google Scholar]
  20. Woessner J. F., Jr The family of matrix metalloproteinases. Ann N Y Acad Sci. 1994 Sep 6;732:11–21. doi: 10.1111/j.1749-6632.1994.tb24720.x. [DOI] [PubMed] [Google Scholar]
  21. Yin L., Morita A., Tsuji T. Alterations of extracellular matrix induced by tobacco smoke extract. Arch Dermatol Res. 2000 Apr;292(4):188–194. doi: 10.1007/s004030050476. [DOI] [PubMed] [Google Scholar]

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