Associations of MMP-7 and OPN gene polymorphisms with risk of coal workers’ pneumoconiosis in a Chinese population: a case-control study

References

• Agnihotri R, Crawford HC, Haro H, et al. (2001). Osteopontin, a novel substrate for matrix metalloproteinase-3 (stromelysin-1) and matrix metalloproteinase-7 (matrilysin). J Biol Chem 276:28261–7
   PubMed Web of Science ®Google Scholar
• Ashkar S, Weber GF, Panoutsakopoulou V, et al. (2000). Eta-1 (osteopontin): an early component of type-1 (cell-mediated) immunity. Science 287:860–4
   PubMed Web of Science ®Google Scholar
• Berman JS, Serlin D, Li X, et al. (2004). Altered bleomycin-induced lung fibrosis in osteopontin-deficient mice. Am J Physiol Lung Cell Mol Physiol 286:L1311–18
   PubMed Web of Science ®Google Scholar
• Brabletz T, Jung A, Dag S, et al. (1999). beta-catenin regulates the expression of the matrix metalloproteinase-7 in human colorectal cancer. Am J Pathol 155:1033–8
   PubMed Web of Science ®Google Scholar
• Chen W, Liu Y, Wang H, et al. (2012). Long-term exposure to silica dust and risk of total and cause-specific mortality in Chinese workers: a cohort study. PLoS Med 9:e1001206
   PubMed Web of Science ®Google Scholar
• Chilosi M, Poletti V, Zamò A, et al. (2003). Aberrant Wnt/beta-catenin pathway activation in idiopathic pulmonary fibrosis. Am J Pathol 162:1495–502
   PubMed Web of Science ®Google Scholar
• Crystal RG, Bitterman PB, Mossman B, et al. (2002). Future research directions in idiopathic pulmonary fibrosis: summary of a National Heart, Lung, and Blood Institute working group. Am J Respir Crit Care Med 166:236–46
   PubMed Web of Science ®Google Scholar
• Denhardt DT, Noda M, O’Regan AW, et al. (2001). Osteopontin as a means to cope with environmental insults: regulation of inflammation, tissue remodeling, and cell survival. J Clin Invest 107:1055–61
   PubMed Web of Science ®Google Scholar
• Desai B, Rogers MJ, Chellaiah MA. (2007). Mechanisms of osteopontin and CD44 as metastatic principles in prostate cancer cells. Mol Cancer 6:18
   PubMed Web of Science ®Google Scholar
• Dunsmore SE, Saarialho-Kere UK, Roby JD, et al. (1998). Matrilysin expression and function in airway epithelium. J Clin Invest 102:1321–31
   PubMed Web of Science ®Google Scholar
• El-Tanani M, Platt-Higgins A, Rudland PS, Campbell FC. (2004). Ets gene PEA3 cooperates with beta-catenin-Lef-1 and c-Jun in regulation of osteopontin transcription. J Biol Chem 279:20794–806
   PubMed Web of Science ®Google Scholar
• Fagenholz PJ, Warren SM, Greenwald JA, et al. (2001). Osteoblast gene expression is differentially regulated by TGF-beta isoforms. J Craniofac Surg 12:183–90
   PubMed Web of Science ®Google Scholar
• Fine A, Janssen-Heininger Y, Soultanakis RP, et al. (2000). Apoptosis in lung pathophysiology. Am J Physiol Lung Cell Mol Physiol 279:L423–7
   PubMed Web of Science ®Google Scholar
• Franks TJ, Galvin JR. (2015). Smoking-Related “Interstitial” Lung Disease. Arch Pathol Lab Med 139:974–7
   Google Scholar
• Fujishima S, Shiomi T, Yamashita S, et al. (2010). Production and activation of matrix metalloproteinase 7 (matrilysin 1) in the lungs of patients with idiopathic pulmonary fibrosis. Arch Pathol Lab Med 134:1136–42
   PubMed Web of Science ®Google Scholar
• Gao YA, Agnihotri R, Vary CP, Liaw L. (2004). Expression and characterization of recombinant osteopontin peptides representing matrix metalloproteinase proteolytic fragments. Matrix Biol 23:457–66
   PubMed Web of Science ®Google Scholar
• Gearing AJ, Beckett P, Christodoulou M, et al. (1995). Matrix metalloproteinases and processing of pro-TNF-alpha. J Leukoc Biol 57:774–7
   PubMed Web of Science ®Google Scholar
• Giachelli CM, Steitz S. (2000). Osteopontin: a versatile regulator of inflammation and biomineralization. Matrix Biol 19:615–22
   PubMed Web of Science ®Google Scholar
• Hemers E, Duval C, McCaig C, et al. (2005). Insulin-like growth factor binding protein-5 is a target of matrix metalloproteinase-7: implications for epithelial-mesenchymal signaling. Cancer Res 65:7363–9
   PubMed Web of Science ®Google Scholar
• Kadota J, Mizunoe S, Mito K, et al. (2005). High plasma concentrations of osteopontin in patients with interstitial pneumonia. Respir Med 99:111–17
   PubMed Web of Science ®Google Scholar
• Kastelijn EA, van Moorsel CH, Ruven HJ, et al. (2010). Genetic polymorphisms in MMP7 and reduced serum levels associate with the development of bronchiolitis obliterans syndrome after lung transplantation. J Heart Lung Transplant 29:680–6
   PubMed Web of Science ®Google Scholar
• Katzenstein AL. (2014). Republished: smoking-related interstitial fibrosis (SRIF): pathologic findings and distinction from other chronic fibrosing lung diseases. Postgrad Med J 90:597–602
   PubMed Web of Science ®Google Scholar
• Koh A, da Silva AP, Bansal AK, et al. (2007). Role of osteopontin in neutrophil function. Immunology 122:466–75
   PubMed Web of Science ®Google Scholar
• Konishi K, Gibson KF, Lindell KO, et al. (2009). Gene expression profiles of acute exacerbations of idiopathic pulmonary fibrosis. Am J Respir Crit Care Med 180:167–75
   PubMed Web of Science ®Google Scholar
• Kuwano K, Hagimoto N, Kawasaki M, et al. (1999). Essential roles of the Fas-Fas ligand pathway in the development of pulmonary fibrosis. J Clin Invest 104:13–19
   PubMed Web of Science ®Google Scholar
• Kuwano K, Kawasaki M, Maeyama T, et al. (2000). Soluble form of fas and fas ligand in BAL fluid from patients with pulmonary fibrosis and bronchiolitis obliterans organizing pneumonia. Chest 118:451–8
   PubMed Web of Science ®Google Scholar
• Lenga Y, Koh A, Perera AS, et al. (2008). Osteopontin expression is required for myofibroblast differentiation. Circ Res 102:319–27
   PubMed Web of Science ®Google Scholar
• Li Q, Park PW, Wilson CL, Parks WC. (2002). Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury. Cell 111:635–46
   PubMed Web of Science ®Google Scholar
• Liaw L, Skinner MP, Raines EW, et al. (1995). The adhesive and migratory effects of osteopontin are mediated via distinct cell surface integrins. Role of alpha v beta 3 in smooth muscle cell migration to osteopontin in vitro. J Clin Invest 95:713–24
   PubMed Web of Science ®Google Scholar
• Liu FD, Pan ZQ, Liu SL, et al. (2007). The estimation of the number of underground coal miners and the annual dose to coal miners in China. Health Phys 93:127–32
   PubMed Web of Science ®Google Scholar
• López B, González A, Lindner D, et al. (2013). Osteopontin-mediated myocardial fibrosis in heart failure: a role for lysyl oxidase? Cardiovasc Res 99:111–20
   PubMed Web of Science ®Google Scholar
• Marcondes MC, Poling M, Watry DD, et al. (2008). In vivo osteopontin-induced macrophage accumulation is dependent on CD44 expression. Cell Immunol 254:56–62
   PubMed Web of Science ®Google Scholar
• Mazzali M, Kipari T, Ophascharoensuk V, et al. (2002). Osteopontin – a molecule for all seasons. QJM 95:3–13
   PubMed Web of Science ®Google Scholar
• McCunney RJ, Morfeld P, Payne S. (2009). What component of coal causes coal workers' pneumoconiosis? J Occup Environ Med 51:462–71
   PubMed Web of Science ®Google Scholar
• McGuire JK, Li Q, Parks WC. (2003). Matrilysin (matrix metalloproteinase-7) mediates E-cadherin ectodomain shedding in injured lung epithelium. Am J Pathol 162:1831–43
   PubMed Web of Science ®Google Scholar
• Miyamoto S, Yano K, Sugimoto S, et al. (2004). Matrix metalloproteinase-7 facilitates insulin-like growth factor bioavailability through its proteinase activity on insulin-like growth factor binding protein 3. Cancer Res 64:665–71
   PubMed Web of Science ®Google Scholar
• Mo J, Wang L, Au W, Su M. (2014). Prevalence of coal workers' pneumoconiosis in China: a systematic analysis of 2001-2011 studies. Int J Hyg Environ Health 217:46–51
   PubMed Web of Science ®Google Scholar
• Morimoto J, Kon S, Matsui Y, Uede T. (2010). Osteopontin; as a target molecule for the treatment of inflammatory diseases. Curr Drug Targets 11:494–505
   PubMed Web of Science ®Google Scholar
• Nkyimbeng T, Ruppert C, Shiomi T, et al. (2013). Pivotal role of matrix metalloproteinase 13 in extracellular matrix turnover in idiopathic pulmonary fibrosis. PLoS One 8:e73279
   PubMed Web of Science ®Google Scholar
• O’Regan A, Berman JS. (2000). Osteopontin: a key cytokine in cell-mediated and granulomatous inflammation. Int J Exp Pathol 81:373–90
   PubMed Web of Science ®Google Scholar
• O’Regan AW, Chupp GL, Lowry JA, et al. (1999). Osteopontin is associated with T cells in sarcoid granulomas and has T cell adhesive and cytokine-like properties in vitro. J Immunol 162:1024–31
   PubMed Web of Science ®Google Scholar
• O’Regan AW, Nau GJ, Chupp GL, Berman JS. (2000). Osteopontin (Eta-1) in cell-mediated immunity: teaching an old dog new tricks. Immunol Today 21:475–8
   PubMedGoogle Scholar
• Oldberg A, Franzén A, Heinegård D. (1986). Cloning and sequence analysis of rat bone sialoprotein (osteopontin) cDNA reveals an Arg-Gly-Asp cell-binding sequence. Proc Natl Acad Sci U S A 83:8819–23
   PubMed Web of Science ®Google Scholar
• Pardo A, Gibson K, Cisneros J, et al. (2005). Up-regulation and profibrotic role of osteopontin in human idiopathic pulmonary fibrosis. PLoS Med 2:e251
   PubMed Web of Science ®Google Scholar
• Pardo A, Selman M. (2006). Matrix metalloproteases in aberrant fibrotic tissue remodeling. Proc Am Thorac Soc 3:383–8
   PubMedGoogle Scholar
• Pardo A, Selman M, Kaminski N. (2008). Approaching the degradome in idiopathic pulmonary fibrosis. Int J Biochem Cell Biol 40:1141–55
   PubMed Web of Science ®Google Scholar
• Philip S, Kundu GC. (2003). Osteopontin induces nuclear factor kappa B-mediated promatrix metalloproteinase-2 activation through I kappa B alpha/IKK signaling pathways, and curcumin (diferulolylmethane) down-regulates these pathways. J Biol Chem 278:14487–97
   PubMed Web of Science ®Google Scholar
• Powell WC, Fingleton B, Wilson CL, et al. (1999). The metalloproteinase matrilysin proteolytically generates active soluble Fas ligand and potentiates epithelial cell apoptosis. Curr Biol 9:1441–7
   PubMed Web of Science ®Google Scholar
• Rangaswami H, Kundu GC. (2007). Osteopontin stimulates melanoma growth and lung metastasis through NIK/MEKK1-dependent MMP-9 activation pathways. Oncol Rep 18:909–15
   PubMed Web of Science ®Google Scholar
• Richards TJ, Kaminski N, Baribaud F, et al. (2012). Peripheral blood proteins predict mortality in idiopathic pulmonary fibrosis. Am J Respir Crit Care Med 185:67–76
   PubMed Web of Science ®Google Scholar
• Rom WN. (1990). Basic mechanisms leading to focal emphysema in coal workers' pneumoconiosis. Environ Res 53:16–28
   PubMed Web of Science ®Google Scholar
• Rosas IO, Richards TJ, Konishi K, et al. (2008). MMP1 and MMP7 as potential peripheral blood biomarkers in idiopathic pulmonary fibrosis. PLoS Med 5:e93
   PubMed Web of Science ®Google Scholar
• Schins RP, Borm PJ. (1999). Mechanisms and mediators in coal dust induced toxicity: a review. Ann Occup Hyg 43:7–33
   PubMed Web of Science ®Google Scholar
• Selman M, Pardo A, Barrera L, et al. (2006). Gene expression profiles distinguish idiopathic pulmonary fibrosis from hypersensitivity pneumonitis. Am J Respir Crit Care Med 173:188–98
   PubMed Web of Science ®Google Scholar
• Suga M, Iyonaga K, Okamoto T, et al. (2000). Characteristic elevation of matrix metalloproteinase activity in idiopathic interstitial pneumonias. Am J Respir Crit Care Med 162:1949–56
   PubMed Web of Science ®Google Scholar
• Takahashi F, Takahashi K, Okazaki T, et al. (2001). Role of osteopontin in the pathogenesis of bleomycin-induced pulmonary fibrosis. Am J Respir Cell Mol Biol 24:264–71
   PubMed Web of Science ®Google Scholar
• Trueblood NA, Xie Z, Communal C, et al. (2001). Exaggerated left ventricular dilation and reduced collagen deposition after myocardial infarction in mice lacking osteopontin. Circ Res 88:1080–7
   PubMed Web of Science ®Google Scholar
• Tsukui T, Ueha S, Abe J, et al. (2013). Qualitative rather than quantitative changes are hallmarks of fibroblasts in bleomycin-induced pulmonary fibrosis. Am J Pathol 183:758–73
   PubMed Web of Science ®Google Scholar
• Vargo-Gogola T, Crawford HC, Fingleton B, Matrisian LM. (2002). Identification of novel matrix metalloproteinase-7 (matrilysin) cleavage sites in murine and human Fas ligand. Arch Biochem Biophys 408:155–61
   PubMed Web of Science ®Google Scholar
• Wang M, Wang S, Song Z, et al. (2011). Associations of IL-4, IL-4R, and IL-13 gene polymorphisms in coal workers' pneumoconiosis in China: a case-control study. PLoS One 6:e22624
   PubMed Web of Science ®Google Scholar
• Wang M, Ye Y, Qian H, et al. (2010). Common genetic variants in pre-microRNAs are associated with risk of coal workers’ pneumoconiosis. J Hum Genet 55:13–17
   PubMed Web of Science ®Google Scholar
• Yucesoy B, Luster MI. (2007). Genetic susceptibility in pneumoconiosis. Toxicol Lett 168:249–54
   PubMed Web of Science ®Google Scholar
• Zuo F, Kaminski N, Eugui E, et al. (2002). Gene expression analysis reveals matrilysin as a key regulator of pulmonary fibrosis in mice and humans. Proc Natl Acad Sci U S A 99:6292–7
   PubMed Web of Science ®Google Scholar