Genetic polymorphisms of matrix metalloproteinases: Functional importance in the development of chronic obstructive pulmonary disease?

American Journal of PharmacoGenomics

Volumn 2, Issue 3, 2002, Pages 167-175

  Wallace, Alison M ^a   Sandford, Andrew J ^a  

^a ST PAUL S HOSPITAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

GELATINASE B; INTERSTITIAL COLLAGENASE; MACROPHAGE ELASTASE;

CHRONIC OBSTRUCTIVE LUNG DISEASE; ENZYME ACTIVITY; ENZYME POLYMORPHISM; GENETIC RISK; GENETIC SUSCEPTIBILITY; HUMAN; LUNG EMPHYSEMA; LUNG FUNCTION; PRIORITY JOURNAL; REVIEW; RISK FACTOR; SMOKING;

EID: 0036395964     PISSN: 11752203     EISSN: None     Source Type: Journal    
DOI: 10.2165/00129785-200202030-00002     Document Type: Review

References (77)

1. Pauwels RA, Buist AS, Calverley PM, et al. Global strategy for the diagnosis, management, and prevention of chronic obstructive pulmonary disease: NHLBI/WHO Global Initiative for Chronic Obstructive Lung Disease (GOLD) Workshop summary. Am J Respir Crit Care Med 2001; 163: 1256-76
2. World Health Organization. World health report [online]. Geneva: WHO, 2000. Available from URL: http://www.who.int/whr/2000/en/statistics.htm [Accessed 2002 Feb 3]
3. Canadian Lung Association [online]. Available from URL: http://www.lung.ca [Accessed 2001 Nov 20]
4. Peto R, Chen ZM, Boreham J. Tobacco: the growing epidemic. Nat Med 1999; 5: 15-7
5. Beck GJ, Doyle CA, Schachter EN. Smoking and lung function. Am Rev Respir Dis 1981; 123: 149-55
6. Givelber RJ, Couropmitree NN, Gottlieb DJ, et al. Segregation analysis of pulmonary function among families in the Framingham Study. Am J Respir Crit Care Med 1998; 157: 1445-51
7. Redline S, Tishler PV, Lewitter FI, et al. Assessment of genetic and nongenetic influences on pulmonary function: a twin study. Am Rev Respir Dis 1987; 135: 217-22
8. Nakamura Y, Leppert M, O'Connell P, et al. Variable number of tandem repeat (VNTR) markers for human gene mapping. Science 1987; 235: 1616-22
9. Lander ES, Linton LM, Birren B, et al. Initial sequencing and analysis of the human genome. Nature 2001; 409 (6822): 860-921
10. Halushka MK, Fan JB, Bentley K, et al. Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet 1999; 22: 239-47
11. Eriksson S. Studies in alpha 1-antitrypsin deficiency. Acta Med Scand Suppl 1965; 432: 1-85
12. Larsson C. Natural history and life expectancy in severe alpha1-antitrypsin deficiency, Pi Z. Acta Med Scand 1978; 204: 345-51
13. Piitulainen E, Eriksson S. Decline in FEV1 related to smoking status in individuals with severe alpha1-antitrypsin deficiency (PiZZ). Eur Respir J 1999; 13: 247-51
14. Silverman EK, Province MA, Campbell EJ, et al. Biochemical intermediates in alpha1-antitrypsin deficiency: residual family resemblance for total alpha1-antitrypsin, oxidised alpha1-antitrypsin, and immunoglobulin E after adjustment for the effect of the Pi locus. Genet Epidemiol 1989; 7: 137-49
15. Sandford AJ, Pare PD. Genetic risk factors for chronic obstructive pulmonary disease. Clin Chest Med 2000; 21: 633-43
16. Silverman EK, Chapman H, Drazen JM, et al. Severe, early-onset COPD: linkage analysis of chromosomes 5q and 12q [abstract]. Am J Respir Crit Care Med 1999; 159: A802
17. Gross P, Pfitzer E, Tolker E, et al. Experimental emphysema: its production with papain in normal and silicotic rats. Arch Environ Health 1965; 11: 50-8
18. Laurell CB, Eriksson S. The electrophoretic alpha1-globulin pattern of serum in alpha1-antitrypsin deficiency. Scand J Clin Lab Invest 1963; 15: 132-40
19. Barrett AJ. Classification of peptidases. Methods Enzymol 1994; 244: 1-15
20. Matrisian LM. Metalloproteinases and their inhibitors in matrix remodeling. Trends Genet 1990; 6: 121-5
21. Birkedal-Hansen H, Moore WG, Bodden MK, et al. Matrix metalloproteinases: a review. Crit Rev Oral Biol Med 1993; 4: 197-250
22. Woessner Jr JF. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J 1991; 5: 2145-54
23. Opdenakker G, Van den Steen PE, Dubois B, et al. Gelatinase B functions as regulator and effector in leukocyte biology. J Leukoc Biol 2001; 69: 851-9
24. Murphy G, Willenbrock F, Crabbe T, et al. Regulation of matrix metalloproteinase activity. Ann N Y Acad Sci 1994; 732: 31-41
25. Nagase H. Activation mechanisms of matrix metalloproteinases. Biol Chem 1997; 378: 151-60
26. Gomez DE, Alonso DF, Yoshiji H, et al. Tissue inhibitors of metalloproteinases: structure, regulation and biological functions. Eur J Cell Biol 1997; 74: 111-22
27. Woessner Jr JF. Matrix metalloproteinase inhibition: from the Jurassic to the third millennium. Ann N Y Acad Sci 1999; 878: 388-403
28. Mignatti P, Robbins E, Rifkin DB. Tumor invasion through the human amniotic membrane: requirement for a proteinase cascade. Cell 1986; 47: 487-98
29. Khokha R, Waterhouse P, Yagel S, et al. Antisense RNA-induced reduction in murine TIMP levels confers oncogenicity on Swiss 3T3 cells. Science 1989; 243: 947-50
30. McCachren SS. Expression of metalloproteinases and metalloproteinase inhibitor in human arthritic synovium. Arthritis Rheum 1991; 34: 1085-93
31. Dean DD, Martel-Pelletier J, Pelletier JP, et al. Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage. J Clin Invest 1989; 84: 678-85
32. Henney AM, Wakeley PR, Davies MJ, et al. Localization of stromelysin gene expression in atherosclerotic plaques by in situ hybridization. Proc Natl Acad Sci U S A 1991; 88: 8154-8
33. Brophy CM, Reilly JM, Smith GJ, et al. The role of inflammation in nonspecific abdominal aortic aneurysm disease. Ann Vasc Surg 1991; 5: 229-33
34. Pozzi A, LeVine WF, Gardner HA. Low plasma levels of matrix metalloproteinase 9 permit increased tumor angiogenesis. Oncogene 2002 Jan 10; 21: 272-81
35. Zhu Y, Spitz MR, Lei L, et al. A single nucleotide polymorphism in the matrix metalloproteinase-1 promoter enhances lung cancer susceptibility. Cancer Res 2001 Nov 1; 61: 7825-9
36. Rutter JL, Mitchell TI, Buttice G, et al. A single nucleotide polymorphism in the matrix metalloproteinase-1 promoter creates an Ets binding site and augments transcription. Cancer Res 1998; 58: 5321-5
37. Kanamori Y, Matsushima M, Minaguchi T, et al. Correlation between expression of the matrix metalloproteinase-1 gene in ovarian cancers and an insertion/deletion polymorphism in its promoter region. Cancer Res 1999; 59: 4225-7
38. Nishioka Y, Kobayashi K, Sagae S, et al. A single nucleotide polymorphism in the matrix metalloproteinase-1 promoter in endometrial carcinomas. Jpn J Cancer Res 2000 Jun; 91: 612-5
39. Murray GI, Duncan ME, O'Neil P, et al. Matrix metalloproteinase-1 is associated with poor prognosis in colorectal cancer. Nat Med 1996; 2: 461-2
40. Murray GI, Duncan ME, O'Neil P, et al. Matrix metalloproteinase-1 is associated with poor prognosis in oesophageal cancer. J Pathol 1998; 185: 256-61
41. Hewitt RE, Leach IH, Powe DG, et al. Distribution of collagenase and tissue inhibitor of metalloproteinases (TIMP) in colorectal tumours. Int J Cancer 1991; 49: 666-72
42. Chambers AF, Matrisian LM. Changing views of the role of matrix metalloproteinases in metastasis. J Natl Cancer Inst 1997; 89: 1260-70
43. Joos L, He JQ, Shepherdson MB, et al. The role of matrix metalloproteinase polymorphisms in the rate of decline in lung function. Hum Mol Genet 2002; 11: 569-76
44. Zhang B, Henney A, Eriksson P, et al. Genetic variation at the matrix metalloproteinase-9 locus on chromosome 20q12.2-13.1. Hum Genet 1999; 105: 418-23
45. Zhang B, Ye S, Herrmann SM, et al. Functional polymorphism in the regulatory region of gelatinase B gene in relation to severity of coronary atherosclerosis. Circulation 1999; 99: 1788-94
46. Shimajiri S, Arima N, Tanimoto A, et al. Shortened microsatellite d(CA)21 sequence down-regulates promoter activity of matrix metalloproteinase 9 gene. FEBS Lett 1999; 455: 70-4
47. Comings DE. Polygenic inheritance and micro/minisatellites. Mol Psychiatry 1998; 3: 21-31
48. Jormsjo S, Ye S, Moritz J, et al. Allele-specific regulation of matrix metalloproteinase-12 gene activity is associated with coronary artery luminal dimensions in diabetic patients with manifest coronary artery disease. Circ Res 2000 May 12; 86: 998-1003
49. D'Armiento J, Dalal SS, Okada Y, et al. Collagenase expression in the lungs of transgenic mice causes pulmonary emphysema. Cell 1992; 71: 955-61
50. Hautamaki RD, Kobayashi DK, Senior RM, et al. Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice. Science 1997; 277: 2002-4
51. Gerhard DS, Jones C, Bauer EA, et al. Human collagenase gene is located on 11q [abstract]. Cytogenet Cell Genet 1987; 46: 619
52. Buttice G, Duterque-Coquillaud M, Basuyaux JP, et al. Erg, an Ets-family member, differentially regulates human collagenase1 (MMP1) and stromelysin1 (MMP3) gene expression by physically interacting with the Fos/Jun complex. Oncogene 1996; 13: 2297-306
53. Finlay GA, Russell KJ, McMahon KJ, et al. Elevated levels of matrix metalloproteinases in bronchoalveolar lavage fluid of emphysematous patients. Thorax 1997; 52: 502-6
54. Finlay GA, O'Driscoll LR, Russell KJ, et al. Matrix metalloproteinase expression and production by alveolar macrophages in emphysema. Am J Respir Crit Care Med 1997; 156: 240-7
55. Segura-Valdez L, Pardo A, Gaxiola M, et al. Upregulation of gelatinases A and B, collagenases 1 and 2, and increased parenchymal cell death in COPD. Chest 2000 Mar; 117: 684-94
56. Imai K, Dalal SS, Chen ES, et al. Human collagenase (matrix metalloproteinase-1) expression in the lungs of patients with emphysema. Am J Respir Crit Care Med 2001 Mar; 163: 786-91
57. Wilhelm SM, Collier IE, Marmer BL, et al. SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages. J Biol Chem 1989; 264: 17213-21
58. Huhtala P, Tuuttila A, Chow LT, et al. Complete structure of the human gene for 92-kDa type IV collagenase: divergent regulation of expression for the 92- and 72-kilodalton enzyme genes in HT-1080 cells. J Biol Chem 1991; 266: 16485-90
59. Okada Y, Nagase H, Harris Jr ED. A metalloproteinase from human rheumatoid synovial fibroblasts that digests connective tissue matrix components: purification and characterization. J Biol Chem 1986; 261: 14245-55
60. Liotta LA, Tryggvason K, Garbisa S, et al. Metastatic potential correlates with enzymatic degradation of basement membrane collagen. Nature 1980; 284: 67-8
61. Nordheim A, Rich A. The sequence (dC-dA)n X (dG-dT)n forms left-handed Z-DNA in negatively supercoiled plasmids. Proc Natl Acad Sci U S A 1983; 80: 1821-5
62. Haniford DB, Pulleyblank DE. Facile transition of poly[d(TG) x d(CA)] into a left-handed helix in physiological conditions. Nature 1983; 302: 632-4
63. Boone TC, Johnson MJ, De Clerck YA, et al. cDna cloning and expression of a metalloproteinase inhibitor related to tissue inhibitor of metalloproteinases. Proc Natl Acad Sci U S A 1990; 87: 2800-4
64. Carmichael DF, Sommer A, Thompson RC, et al. Primary structure and cDNA cloning of human fibroblast collagenase inhibitor. Proc Natl Acad Sci U S A 1986; 83: 2407-11
65. Greene J, Wang M, Liu YE, et al. Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4. J Biol Chem 1996; 271: 30375-80
66. Leco KJ, Khokha R, Pavloff N, et al. Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues. J Biol Chem 1994; 269: 9352-60
67. Shapiro SD. Elastolytic metalloproteinases produced by human mononuclear phagocytes: potential roles in destructive lung disease. Am J Respir Crit Care Med 1994; 150: S160-4
68. Vignola AM, Riccobono L, Mirabella A, et al. Sputum metalloproteinase-9/tissue inhibitor of metalloproteinase-1 ratio correlates with airflow obstruction in asthma and chronic bronchitis. Am J Respir Crit Care Med 1998; 158: 1945-50
69. Ohnishi K, Takagi M, Kurokawa Y, et al. Matrix metalloproteinase-mediated extracellular matrix protein degradation in human pulmonary emphysema. Lab Invest 1998; 78: 1077-87
70. Belaaouaj A, Shipley JM, Kobayashi DK, et al. Human macrophage metalloelastase: genomic organization, chromosomal location, gene linkage, and tissue-specific expression. J Biol Chem 1995; 270: 14568-75
71. Shapiro SD, Kobayashi DK, Ley TJ. Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages. J Biol Chem 1993; 268: 23824-9
72. Werb Z, Gordon S. Elastase secretion by stimulated macrophages: characterization and regulation. J Exp Med 1975; 142: 361-77
73. Banda MJ, Werb Z. Mouse macrophage elastase: purification and characterization as a metalloproteinase. Biochem J 1981; 193: 589-605
74. Murphy G, Cockett MI, Ward RV, et al. Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan: a quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP). Biochem J 1991; 277: 277-9
75. Senior RM, Griffin GL, Fliszar CJ, et al. Human 92- and 72-kilodalton type IV collagenases are elastases. J Biol Chem 1991; 266: 7870-5
76. Anthonisen NR, Connett JE, Kiley JP, et al. Effects of smoking intervention and the use of an inhaled anticholinergic bronchodilator on the rate of decline of FEV1; the Lung Health Study. JAMA 1994; 272: 1497-505
77. Minematsu N, Nakamura H, Tateno H, et al. Genetic polymorphism in matrix metalloproteinase-9 and pulmonary emphysema. Biochem Biophys Res Commun 2001 Nov 23; 289: 116-9