References
- Krouse JH. Endoscopic treatment of inverted papilloma: safety and efficacy. Am J Otolaryngol. 2001;22(2):87–99. doi:10.1053/ajot.2001.22563
- Lane AP, Bolger WE. Endoscopic management of inverted papilloma. Curr Opin Otolaryngol Head Neck Surg. 2006;14(1):14–18. doi:10.1097/01.moo.0000193175.54450.1f
- Kristensen S, Vorre P, Elbrond O, Sogaard H. Nasal Schneiderian papillomas: a study of 83 cases. Clin Otolaryngol Allied Sci. 1985;10(3):125–134. doi:10.1111/j.1365-2273.1985.tb01181.x
- Mirza S, Bradley PJ, Acharya A, Stacey M, Jones NS. Sinonasal inverted papillomas: recurrence, and synchronous and metachronous malignancy. J Laryngol Otol. 2007;121(9):857–864.
- Zhao L, Li CW, Jin P, et al. Histopathological features of sinonasal inverted papillomas in Chinese patients. Laryngoscope. 2016;126(4):E141–E147. doi:10.1002/lary.25694
- Reynoso J, Davis RE, Daniels WW, Awad ZT, Gatalica Z, Filipi CJ. Esophageal papillomatosis complicated by squamous cell carcinoma in situ. Dis Esophagus. 2004;17(4):345–347. doi:10.1111/j.1442-2050.2004.00438.x
- Zhao Y, Li N, Gong X, Yu L, Jin X. Clinicopathologic features of intraductal papillary neoplasm of breast: analyses of three cases. Int J Clin Exp Pathol. 2017;10(9):9575–9582.
- Jang HH, Kim HW, Kim SJ, et al. Gastric squamous papilloma in a 52-year-old female patient. Clin Endosc. 2014;47(6):571–574. doi:10.5946/ce.2014.47.6.571
- Vandenbroucke RE, Libert C. Is there new hope for therapeutic matrix metalloproteinase inhibition? Nat Rev Drug Discov. 2014;13(12):904–927.
- Kessenbrock K, Plaks V, Werb Z. Matrix metalloproteinases: regulators of the tumor microenvironment. Cell. 2010;141(1):52–67. doi:10.1016/j.cell.2010.03.015
- Gross J, Lapiere CM. Collagenolytic activity in amphibian tissues: a tissue culture assay. Proc Natl Acad Sci U S A. 1962;48:1014–1022. doi:10.1073/pnas.48.6.1014
- Page-McCaw A, Ewald AJ, Werb Z. Matrix metalloproteinases and the regulation of tissue remodelling. Nat Rev Mol Cell Biol. 2007;8(3):221–233. doi:10.1038/nrm2125
- Parks WC, Wilson CL, Lopez-Boado YS. Matrix metalloproteinases as modulators of inflammation and innate immunity. Nat Rev Immunol. 2004;4(8):617–629. doi:10.1038/nri1418
- Deryugina EI, Quigley JP. Matrix metalloproteinases and tumor metastasis. Cancer Metastasis Rev. 2006;25(1):9–34. doi:10.1007/s10555-006-7886-9
- Fanjul-Fernandez M, Folgueras AR, Cabrera S, Lopez-Otin C. Matrix metalloproteinases: evolution, gene regulation and functional analysis in mouse models. Biochim Biophys Acta. 2010;1803(1):3–19. doi:10.1016/j.bbamcr.2009.07.004
- Aimes RT, Quigley JP. Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments. J Biol Chem. 1995;270(11):5872–5876. doi:10.1074/jbc.270.11.5872
- Mackay AR, Hartzler JL, Pelina MD, Thorgeirsson UP. Studies on the ability of 65-kDa and 92-kDa tumor cell gelatinases to degrade type IV collagen. J Biol Chem. 1990;265(35):21929–21934. doi:10.1016/S0021-9258(18)45827-9
- Keck T, Balcom JH, Fernandez-del Castillo C, Antoniu BA, Warshaw AL. Matrix metalloproteinase-9 promotes neutrophil migration and alveolar capillary leakage in pancreatitis-associated lung injury in the rat. Gastroenterology. 2002;122(1):188–201. doi:10.1053/gast.2002.30348
- Chabot V, Reverdiau P, Iochmann S, et al. CCL5-enhanced human immature dendritic cell migration through the basement membrane in vitro depends on matrix metalloproteinase-9. J Leukoc Biol. 2006;79(4):767–778. doi:10.1189/jlb.0804464
- Okada S, Kita H, George TJ, Gleich GJ, Leiferman KM. Migration of eosinophils through basement membrane components in vitro: role of matrix metalloproteinase-9. Am J Respir Cell Mol Biol. 1997;17(4):519–528. doi:10.1165/ajrcmb.17.4.2877
- Papon JF, Lechapt-Zalcman E, Abina M, et al. Matrix metalloproteinase-2 and −9 expression in sinonasal inverted papilloma. Rhinology. 2006;44(3):211–215.
- Katori H, Nozawa A, Tsukuda M. Increased expression of matrix metalloproteinase-2 and 9 and human papilloma virus infection are associated with malignant transformation of sinonasal inverted papilloma. J Surg Oncol. 2006;93(1):80–85. doi:10.1002/jso.20386
- Ong CWM, Fox K, Ettorre A, Elkington PT, Friedland JS. Hypoxia increases neutrophil-driven matrix destruction after exposure to Mycobacterium tuberculosis. Sci Rep. 2018;8(1):11475. doi:10.1038/s41598-018-29659-1
- Mortaz E, Alipoor SD, Adcock IM, Mumby S, Koenderman L. Update on neutrophil function in severe inflammation. Front Immunol. 2018;9:2171. doi:10.3389/fimmu.2018.02171
- Chung KF, Adcock IM. Multifaceted mechanisms in COPD: inflammation, immunity, and tissue repair and destruction. Eur Respir J. 2008;31(6):1334–1356. doi:10.1183/09031936.00018908
- Kettritz R, Xu YX, Kerren T, et al. Extracellular matrix regulates apoptosis in human neutrophils. Kidney Int. 1999;55(2):562–571. doi:10.1046/j.1523-1755.1999.00280.x
- Kobayashi SD, Voyich JM, Burlak C, DeLeo FR. Neutrophils in the innate immune response. Arch Immunol Ther Exp. 2005;53(6):505–517.
- Zijlstra A, Seandel M, Kupriyanova TA, et al. Proangiogenic role of neutrophil-like inflammatory heterophils during neovascularization induced by growth factors and human tumor cells. Blood. 2006;107(1):317–327. doi:10.1182/blood-2005-04-1458
- Liu Y, Zhang H, Yan L, et al. MMP-2 and MMP-9 contribute to the angiogenic effect produced by hypoxia/15-HETE in pulmonary endothelial cells. J Mol Cell Cardiol. 2018;121:36–50. doi:10.1016/j.yjmcc.2018.06.006
- McGuire JK, Li Q, Parks WC. Matrilysin (matrix metalloproteinase-7) mediates E-cadherin ectodomain shedding in injured lung epithelium. Am J Pathol. 2003;162(6):1831–1843. doi:10.1016/S0002-9440(10)64318-0
- Ichikawa Y, Ishikawa T, Momiyama N, et al. Matrilysin (MMP-7) degrades VE-cadherin and accelerates accumulation of beta-catenin in the nucleus of human umbilical vein endothelial cells. Oncol Rep. 2006;15(2):311–315.
- Herrera I, Cisneros J, Maldonado M, et al. Matrix metalloproteinase (MMP)-1 induces lung alveolar epithelial cell migration and proliferation, protects from apoptosis, and represses mitochondrial oxygen consumption. J Biol Chem. 2013;288(36):25964–25975. doi:10.1074/jbc.M113.459784