The dual personalities of matrix metalloproteinases in inflammation

Frontiers in Bioscience

Volumn 12, Issue 4, 2007, Pages 1475-1487

  Le, Nghia T V ^a   Xue, Meilang ^a   Castelnoble, Laura A ^a   Jackson, Christopher J ^a  

^a UNIVERSITY OF SYDNEY   (Australia)

Author keywords

Arhritis; Cancer; Chemokines; Cytokines; Inflammation; Matrix metalloproteinases; Review; Rheumatoid

Indexed keywords

EID: 34249795455     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/2161     Document Type: Article

References (129)

1. Pei, D., T. Kang & H. Qi: Cysteine array matrix metalloproteinase (CA-MMP)/MMP-23 is a type II transmembrane matrix metalloproteinase regulated by a single cleavage for both secretion and activation. J Biol Chem, 275, 33988-97 (2000)
2. Van Wart, H. E. & H. Birkedal-Hansen: The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci USA, 87, 5578-82 (1990)
3. Rouille, Y., S. J. Duguay, K. Lund, M. Furuta, Q. Gong, G. Lipkind, A. A. Oliva, Jr., S. J. Chan & D. F. Steiner: Proteolytic processing mechanisms in the biosynthesis of neuroendocrine peptides: the subtilisin-like proprotein convertases. Front Neuroendocrinol, 16, 322-61 H 995)
4. Bassi, D. E., H. Mahloogi & A. J. Klein-Szanto: The proprotein convertases furin and PACE4 play a significant role in tumor progression. Mol Carcinog, 28, 63-9 (2000)
5. Gurarajan, R., J. M. Lahti, J. Grenet, J. Easton, I. Gruber, P. F. Ambros & V. J. Kidd: Duplication of a genomic region containing the Cdc2Ll-2 and MMP21-22 genes on human chromosome Ip36.3 and their linkage to D1Z2. Genome Res, 8, 929-39 (1998)
6. Gururajan, R., J. Grenet, J. M. Lahti & V. J. Kidd: Isolation and characterization of two novel metalloproteinase genes linked to the Cdc2L locus on human chromosome Ip36.3. Genomics, 52, 101-6 (1998)
7. Murphy, G. & V. Knauper: Relating matrix metalloproteinase structure to function: why the "hemopexin" domain? Matrix Biol, 15, 511-8 (1997)
8. Roeb, E., K. Schleinkofer, T. Kernebeck, S. Potsch, B. Jansen, I. Behrmann, S. Matem & J. Grotzinger: The matrix metalloproteinase 9 (mmp-9) hemopexin domain is a novel gelatin binding domain and acts as an antagonist. J Biol Chem, 277, 50326-32 (2002)
9. Itoh, Y., A. Takamura, N. Ito, Y. Maru, H. Sato, N. Suenaga, T. Aoki & M. Seiki: Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion. Embo J, 20, 4782-93 (2001)
10. Brooks, P. C., S. Silletti, T. L. von Schalscha, M. Friedlander & D. A. Cheresh: Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity. Cell, 92, 391-400 (1998)
11. Brooks, P. C., S. Stromblad, L. C. Sanders, T. L. von Schalscha, R. T. Aimes, W. G. Stetler-Stevenson, J. P. Quigley & D. A. Cheresh: Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3. Cell, 85, 683-93 0996)
12. Stricker, T. P., J. A. Dumin, S. K. Dickeson, L. Chung, H. Nagase, W. C. Parks & S. A. Santoro: Structural analysis of the alpha (2) integrin I domain/procollagenase-1 (matrix metalloproteinase-1) interaction. J Biol Chem, 276, 29375-81 (2001)
13. Pei, D.: CA-MMP: a matrix metalloproteinase with a novel cysteine array, but without the classic cysteine switch. FEBS Lett, 457, 262-70 (1999)
14. Steffensen, B., U. M. Wallon & C. M. Overall: Extracellular matrix binding properties of recombinant fibronectin type Il-like modules of human 72-kDa gelatinase/type IV collagenase. High affinity binding to native type I collagen but not native type IV collagen. J Biol Chem, 270, 11555-66 (1995)
15. Allan, J. A., A. J. Docherty, P. J. Barker, N. S. Huskisson, J. J. Reynolds & G. Murphy: Binding of gelatinases A and B to type-I collagen and other matrix components. Biochem J, 309 (Pt 1), 299-306 (1995)
16. Xu, X., Y. Wang, J. L. Lauer-Fields, G. B. Fields & B. Steffensen: Contributions of the MMP-2 collagen binding domain to gelatin cleavage. Substrate binding via the collagen binding domain is required for hydrolysis of gelatin but not short peptides. Matrix Biol, 23, 171-81 (2004)
17. Sakai, T., F. Kambe, H. Mitsuyama, N. Ishiguro, K. Kurokouchi, M. Takigawa, H. Iwata & H. Seo: Tumor necrosis factor alpha induces expression of genes for matrix degradation in human chondrocyte-like HCS-2/8 cells through activation of NF-kappaB: abrogation of the tumor necrosis factor alpha effect by proteasome inhibitors. J Bone Miner Res, 16, 1272-80 (2001)
18. Han, Y. P., T. L. Tuan, M. Hughes, H. Wu & W. L. Garner: Transforming growth factor-beta - and tumor necrosis factor-alpha -mediated induction and proteolytic activation of MMP-9 in human skin. J Biol Chem, 276, 22341-50 (2001)
19. Vincenti, M. P., C. I. Coon & C. E. Brinckerhoff: Nuclear factor kappaB/p50 activates an element in the distal matrix metalloproteinase 1 promoter in interleukin1 beta-stimulated synovial fibroblasts. Arthritis Rheum, 41, 1987-94 (1998)
20. Moon, S. K., B. Y. Cha & C. H. Kim: ERK1/2 mediates TNF-alpha-induced matrix metalloproteinase-9 expression in human vascular smooth muscle cells via the regulation of NF-kappaB and AP-1: Involvement of the ras dependent pathway. J Cell Physiol, 198, 417-27 (2004)
21. Benbow, U. & C. E. Brinckerhoff: The AP-1 site and MMP gene regulation: what is all the fuss about? Matrix Biol, 15, 519-26 (1997)
22. Nagase, H., Y. Itoh & S. Binner: Interaction of alpha 2-macroglobulin with matrix metalloproteinases and its use for identification of their active forms. Ann N Y Acad Sci, 732, 294-302 (1994)
23. Docherty, A. J., A. Lyons, B. J. Smith, E. M. Wright, P. E. Stephens, T. J. Harris, G. Murphy & J. J. Reynolds: Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity. Nature, 318,66-9(1985)
24. Stetler-Stevenson, W. G., H. C. Krutzsch & L. A. Liotta: Tissue inhibitor of metalloproteinase (TIMP-2). A new member of the metalloproteinase inhibitor family. J Biol Chem, 264, 17374-8 (1989)
25. Apte, S. S., B. R. Olsen & G. Murphy: The gene structure of tissue inhibitor of metalloproteinases (TIMP)3 and its inhibitory activities define the distinct TIMP gene family. J Biol Chem, 270, 14313-8 (1995)
26. Greene, J., M. Wang, Y. E. Liu, L. A. Raymond, C. Rosen & Y. E. Shi: Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4. J Biol Chem, 271, 30375-80 (1996)
27. Butler, G. S, H. Will, S. J. Atkinson & G. Murphy: Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases. Eur J Biochem, 244, 653-7 (1997)
28. Stracke, J. O., M. Hutton, M. Stewart, A. M. Pendas, B. Smith, C. Lopez-Otin, G. Murphy & V. Knauper: Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme. J Biol Chem, 275, 14809-16 (2000)
29. Will, H., S. J. Atkinson, G. S. Butler, B. Smith & G. Murphy: The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3. J Biol Chem, 271, 17119-23(1996)
30. Lee, M. H., M. Rapti & G. Murphy: Unveiling the surface epitopes that render tissue inhibitor of metalloproteinase-1 inactive against membrane type 1-matrix metalloproteinase. J Biol Chem, 278, 40224-30 (2003)
31. Nathan, C.: Points of control in inflammation. Nature, 420, 846-52 (2002)
32. Benoist, C. & D. Mathis: Mast cells in autoimmune disease. Nature, 420, 875-8 (2002)
33. Muller, W. A.: Leukocyte-endothelial cell interactions in the inflammatory response. Lab Invest, 82, 521-33 (2002)
34. Yonekawa, K. & J. M. Harlan: Targeting leukocyte integrins in human diseases. J Leukoc Biol, 77, 129-40 (2005)
35. Masure, S., P. Proost, J. Van Damme & G. Opdenakker: Purification and identification of 91-kDa neutrophil gelatinase. Release by the activating peptide interleukin-8. Eur J Biochem, 198, 391-8 (1991)
36. Borregaard, N., M. Sehested, B. S. Nielsen, H. Sengelov & L. Kjeldsen: Biosynthesis of granule proteins in normal human bone marrow cells. Gelatinase is a marker of terminal neutrophil differentiation. Blood, 85, 812-7 f!995)
37. Opdenakker, G., S. Masure, P. Proost, A. Billiau & J. van Damme: Natural human monocyte gelatinase and its inhibitor. FEBS Lett, 284, 73-8 (1991)
38. Leppert, D., E. Waubant, R. Galardy, N. W. Bunnett & S. L. Hauser: T cell gelatinases mediate basement membrane transmigration in vitro. J Immunol, 154, 4379-89 (1995)
39. Gidday, J. M., Y. G. Gasche, J. C. Copin, A. R. Shah, R. S. Perez, S. D. Shapiro, P. H. Chan & T. S. Park: Leukocyte-derived matrix metalloproteinase-9 mediates blood-brain barrier breakdown and is proinflammatory after transient focal cerebral ischemia. Am J Physiol Heart Circ Physiol, 289, H558-68 (2005)
40. Allport, J. R., Y. C. Lim, J. M. Shipley, R. M. Senior, S. D. Shapiro, N. Matsuyoshi, D. Vestweber & F. W. Luscinskas: Neutrophils from MMP-9- or neutrophil elastase-deficient mice show no defect in transendothelial migration under flow in vitro. J Leukoc Biol, 71, 821-8 (2002)
41. Fernandez-Patron, C., C. Zouki, R. Whittal, J. S. Chan, S. T. Davidge & J. G. Filep: Matrix metalloproteinases regulate neutrophil-endothelial cell adhesion through generation of endothelin-1 (1-32]. Faseb J, 15, 2230-40 (2001)
42. Wiedow, O. & U. Meyer-Hoffert: Neutrophil serine proteases: potential key regulators of cell signalling during inflammation. J Intern Med, 257, 319-28 (2005)
43. Liu, Z., X. Zhou, S. D. Shapiro, J. M. Shipley, S. S. Twining, L. A. Diaz, R. M. Senior & Z. Werb: The serpin alpha 1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 in vivo. Cell, 102, 647-55 (2000)
44. Banda, M. J., A. G. Rice, G. L. Griffin & R. M. Senior: Alpha 1-proteinase inhibitor is aneutrophil chemoattractant after proteolytic inactivation by macrophage elastase. J Biol Chem, 263, 4481-4 (1988)
45. Mast, A. E., J. J. Enghild, H. Nagase, K. Suzuki, S. V. Pizzo & G. Salvesen: Kinetics and physiologic relevance of the inactivation of alpha 1-proteinase inhibitor, alpha 1-antichymotrypsin, and antithrombin III by matrix metalloproteinases-1 (tissue collagenase), -2 (72-kDa gelatinase/type IV collagenase), and -3 (stromelysin). J Biol Chem, 266, 15810-6 (1991)
46. Vilcek, J. & T. H. Lee: Tumor necrosis factor. New insights into the molecular mechanisms of its multiple actions. J Biol Chem, 266, 7313-6 (1991)
47. Kriegler, M., C. Perez, K. DeFay, I. Albert & S. D. Lu: A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: ramifications for the complex physiology of TNF. Cell, 53, 45-53 (1988)
48. Gearing, A. J., P. Beckett, M. Christodoulou, M. Churchill, J. Clements, A. H. Davidson, A. H. Drummond, W. A. Galloway, R. Gilbert, J. L. Gordon & et al.: Processing of tumour necrosis factor-alpha precursor by metalloproteinases. Nature, 370, 555-7 (1994)
49. Mohan, M. J., T. Seaton, J. Mitchell, A. Howe, K. Blackburn, W. Burkhart, M. Moyer, I. Patel, G. M. Waitt, J. D. Becherer, M. L. Moss & M. E. Milla: The tumor necrosis factor-alpha converting enzyme (TAGE): a unique metalloproteinase with highly defined substrate selectivity. Biochemistry, 41, 9462-9 (2002)
50. Haro, H., H. C. Crawford, B. Fingleton, K. Shinomiya, D. M. Spengler & L. M. Matrisian: Matrix metalloproteinase-7-dependent release of tumor necrosis factor-alpha in a model of herniated disc resorption. J Clin Invest, 105, 143-50 (2000)
51. Tam, E. M., C. J. Morrison, Y. I. Wu, M. S. Stack & C. M. Overall: Membrane protease proteomics: Isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates. Proc Natl Acad Sci USA, 101, 6917-22 (2004)
52. English, W. R., X. S. Puente, J. M. Freije, V. Knauper, A. Amour, A. Merryweather, C. Lopez-Otin & G. Murphy: Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor-alpha convertase activity but does not activate pro-MMP2. J Biol Chem, 275, 14046-55 (2000)
53. Williams, L. M., D. L. Gibbons, A. Gearing, R. N. Maini, M. Feldmann & F. M. Brennan: Paradoxical effects of a synthetic metalloproteinase inhibitor that blocks both p55 and p75 TNF receptor shedding and TNF alpha processing in RA synovial membrane cell cultures. J Clin Invest, 97, 2833-41 1996)
54. Catrina, A. I., J. Lampa, S. Ernestam, E. af Klint, J. Bratt, L. Klareskog & A. K. Ulfgren: Anti-tumour necrosis factor (TNF)-alpha therapy (etanercept) down-regulates serum matrix metalloproteinase (MMP)-3 and MMP-1 in rheumatoid arthritis. Rheumatology (Oxford), 41, 484-9 (2002)
55. Ito, A., A. Mukaiyama, Y. Itoh, H. Nagase, I. B. Thogersen, J. J. Enghild, Y. Sasaguri & Y. Mori: Degradation of interleukin Ibeta by matrix metalloproteinases. JBiol Chem, 271, 14657-60 (1996)
56. Schonbeck, U., F. Mach & P. Libby: Generation of biologically active IL-1 beta by matrix metalloproteinases: a novel caspase-1-independent pathway of IL-1 beta processing. J Immunol, 161, 3340-6 (1998)
57. Schmidt-Weber, C. B. & K. Blaser: Regulation and role of transforming growth factor-beta in immune tolerance induction and inflammation. Curr Opin Immunol, 16, 709-16 (2004)
58. Javelaud, D. & A. Mauviel: Mammalian transforming growth factor-betas: Smad signaling and physio-pathological roles. Int J Biochem Cell Biol, 36, 1161-5 (2004)
59. Maeda, S., D. D. Dean, R. Gomez, Z. Schwartz & B. D. Boyan: The first stage of transforming growth factor betal activation is release of the large latent complex from the extracellular matrix of growth plate chondrocytes by matrix vesicle stromelysin-1 (MMP-3). Calcif Tissue Int, 70, 54-65 (2002)
60. Yu, Q. & I. Stamenkovic: Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev, 14, 163-76 (2000)
61. Maeda, S., D. D. Dean, I. Gay, Z. Schwartz & B. D. Boyan: Activation of latent transforming growth factor betal by stromelysin 1 in extracts of growth plate chondrocyte-derived matrix vesicles. J Bone Miner Res, 16, 1281-90 (2001)
62. Karsdal, M. A., L. Larsen, M. T. Engsig, H. Lou, M. Ferreras, A. Lochter, J. M. Delaisse & N. T. Foged: Matrix metalloproteinase-dependent activation of latent transforming growth factor-beta controls the conversion of osteoblasts into osteocytes by blocking osteoblast apoptosis. J Biol Chem, 277, 44061-7 (2002)
63. Karsdal, M. A., M. S. Fjording, N. T. Foged, J. M. Delaisse & A. Lochter: Transforming growth factor-beta-induced osteoblast elongation regulates osteoclastic bone résorption through a p38 mitogen-activated protein kinaseand matrix metalloproteinase-dependent pathway. J Biol Chem, 276, 39350-8 (2001)
64. Moser, B. & K. Willimann: Chemokines: role in inflammation and immune surveillance. Ann Rheum Dis, 63 Suppl 2, ii84-ii89 (2004)
65. Mackay, C. R.: Chemokines: immunology's high impact factors. Nat Immunol, 2, 95-101 (2001)
66. Rollins, B. J.: Chemokines. Blood, 90, 909-28 (1997)
67. Fernandez, E. J. & E. Lolis: Structure, function, and inhibition of chemokines. Anna Rev Pharmacol Toxicol, 42, 469-99 (2002)
68. Murphy, P. M.: International Union of Pharmacology. XXX. Update on chemokine receptor nomenclature. Pharmacol Rev, 54, 227-9 (2002)
69. Van den Steen, P. E., P. Proost, A. Wuyts, J. Van Damme & G. Opdenakker: Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact. Blood, 96, 2673-81 (2000)
70. Chakrabarti, S. & K. D. Patel: Regulation of matrix metalloproteinase-9 release from IL-8-stimulated human neutrophils. J Leukoc Biol, 78, 279-88 (2005)
71. Van Den Steen, P. E., A. Wuyts, S. J. Husson, P. Proost, J. Van Damme & G. Opdenakker: Gelatinase B/MMP-9 and neutrophil collagenase/MMP-8 process the chemokines human GCP-2/CXCL6, ENA-78/CXCL5 and mouse GCP-2/LIX and modulate their physiological activities. Eur J Biochem, 270, 3739-49 (2003)
72. McQuibban, G. A., J. H. Gong, E. M. Tam, C. A. McCulloch, I. dark-Lewis & C. M. Overall: Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. Science, 289, 1202-6 (2000)
73. Xu, L. L., D. W. McVicar, A. Ben-Baruch, D. B. Kuhns, J. Johnston, J. J. Oppenheim & J. M. Wang: Monocyte chemotactic protein-3 (MCP3) interacts with multiple leukocyte receptors: binding and signaling of MCP3 through shared as well as unique receptors on monocytes and neutrophils. Eur J Immunol, 25, 2612-7 (1995)
74. Loetscher, P., M. Seitz, I. dark-Lewis, M. Baggiolini & B. Moser: Monocyte chemotactic proteins MCP-1, MCP-2, and MCP-3 are major attractants for human CD4+ and CD8+ T lymphocytes. Faseb J, 8, 1055-60 (1994)
75. McQuibban, G. A., J. H. Gong, J. P. Wong, J. L. Wallace, I. dark-Lewis & C. M. Overall: Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo. Blood, 100, 1160-7 2002)
76. Giannelli, G., R. Erriquez, F. lannone, F. Marinosci, G. Lapadula & S. Antonaci: MMP-2, MMP-9, TIMP-1 and TIMP-2 levels in patients with rheumatoid arthritis and psoriatic arthritis. Clin Exp Rheumatol, 22, 335-8 (2004)
77. Itoh, T., H. Matsuda, M. Tanioka, K. Kuwabara, S. Itohara & R. Suzuki: The role of matrix metalloproteinase-2 and matrix metalloproteinase-9 in antibody-induced arthritis. J Immunol, 169, 2643-7 (2002)
78. Gjertsson, I., M. Innocenta, L. M. Matrisian & A. Tarkowski: Metalloproteinase-7 contributes to joint destruction in Staphylococcus aureus induced arthritis. Microb Pathog, 38, 97-105 (2005)
79. Li, Q., P. W. Park, C. L. Wilson & W. C. Parks: Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury. Cell, 111, 635-46 (2002)
80. Wojtowicz-Praga, S., J. Tom, M. Johnson, V. Steen, J. Marshall, E. Ness, R. Dickson, M. Sale, H. S. Rasmussen, T. A. Chiodo & M. J. Hawkins: Phase I trial of Marimastat, a novel matrix metalloproteinase inhibitor, administered orally to patients with advanced lung cancer. J Clin Oncol, 16, 2150-6 (1998)
81. Hemmings, F. J., M. Farhan, J. Rowland, L. Banken & R. Jain: Tolerability and pharmacokinetics of the collagenase-selective inhibitor Trocade in patients with rheumatoid arthritis. Rheumatology (Oxford), 40, 537-43 (2001)
82. Jackson, C., M. Nguyen, J. Arkell & P. Sambrook: Selective matrix metalloproteinase (MMP) inhibition in rheumatoid arthritis-targetting gelatinase A activation. InflammRes, 50, 183-6 (2001)
83. Close, D. R.: Matrix metalloproteinase inhibitors in rheumatic diseases. Ann Rheum Dis, 60 Suppl 3, iii62-7 (2001)
84. Philip, M., D. A. Rowley & H. Schreiber: Inflammation as a tumor promoter in cancer induction. Semin Cancer Biol, 14,433-9(2004)
85. Farrow, B. & B. M. Evers: Inflammation and the development of pancreatic cancer. Surg Oncol, 10, 153-69 (2002)
86. Freedman, R. S., M. Deavers, J. Liu & E. Wang: Peritoneal inflammation - A microenvironment for Epithelial Ovarian Cancer (EOC). J Transi Med, 1, 23 (2004)
87. Itzkowitz, S. H. & X. Yio: Inflammation and cancer IV. Colorectal cancer in inflammatory bowel disease: the role of inflammation. Am J Physiol Gastrointest Liver Physiol, 287, 07-17 (2004)
88. Mignogna, M. D., S. Fedele, L. Lo Russo, L. Lo Muzio & E. Bucci: Immune activation and chronic inflammation as the cause of malignancy in oral lichen planus: is there any evidence ? Oral Oncol, 40, 120-30 (2004)
89. Kinzler, K. W. & B. Vogelstein: Landscaping the cancer terrain. Science, 280, 1036-7 (1998)
90. Macarthur, M., G. L. Hold & E. M. El-Omar: Inflammation and Cancer II. Role of chronic inflammation and cytokine gene polymorphisms in the pathogenesis ofgastrointestinal malignancy. Am J Physiol Gastrointest Liver Physiol, 286, G515-20 (2004)
91. Friess, H., X. Z. Guo, B. C. Nan, O. Kleeff & M. W. Buchler: Growth factors and cytokines in pancreatic carcinogenesis. Ann N Y Acad Sci, 880, 110-21 (1999)
92. Kuper, H., H. O. Adami & D. Trichopoulos: Infections as a major preventable cause of human cancer. J Intern Med, 248, 171-83(2000)
93. Le, X., Q. Shi, B. Wang, Q. Xiong, C. Qian, Z. Peng, X. C. Li, H. Tang, J. L. Abbruzzese & K. Xie: Molecular regulation of constitutive expression of interleukin-8 in human pancreatic adenocarcinoma. J Interferon Cytokine Res, 20, 935-46 (2000)
94. Kulbe, H., N. R. Levinson, F. Balkwill & J. L. Wilson: The chemokine network in cancer-much more than directing cell movement. Int J Dev Biol, 48, 489-96 (2004)
95. Egeblad, M. & Z. Werb: New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer, 2,161-74(2002)
96. Me Donnell, S., V. Chaudhry, J. Mansilla-Soto, Z. S. Zeng, W. P. Shu & J. G. Guillem: Metastatic and non-metastatic colorectal cancer (CRC) cells induce host metalloproteinase production in vivo. Clin Exp Metastasis, 17, 341-9 (1999)
97. Mook, O. R., W. M. Frederiks & C. J. Van Noorden: The role of gelatinases in colorectal cancer progression and metastasis. Biochim Biophys Acta, 1705, 69-89 (2004)
98. Segain, J. P., J. Harb, M. Grégoire, K. Meflah & J. Menanteau: Induction of fibroblast gelatinase B expression by direct contact with cell lines derived from primary tumor but not from metastases. Cancer Res, 56, 5506-12 (1996)
99. van den Oord, J. J., L. Paemen, G. Opdenakker & C. de Wolf-Peeters: Expression of gelatinase B and the extracellular matrix metalloproteinase inducer EMMPRIN in benign and malignant pigment cell lesions of the skin. Am J Pathol, 151, 665-70 (1997)
100. Li, B. H., P. Zhao, S. Z. Liu, Y. M. Yu, M. Han & J. K. Wen: Matrix metalloproteinase-2 and tissue inhibitor of metallo-proteinase-2 in colorectal carcinoma invasion and metastasis. World J Gastroenterol, 11, 3046-50 (2005)
101. Watson, S. A., T. M. Morris, H. M. Collins, L. J. Bawden, K. Hawkins & E. A. Bone: Inhibition of tumour growth by marimastat in a human xenograft model of gastric cancer: relationship with levels of circulating CEA. Br J Cancer, 81, 19-23 (1999)
102. Bloomston, M., E. E. Zervos & A. S. Rosemurgy, 2nd: Matrix metalloproteinases and their role in pancreatic cancer: a review of preclinical studies and clinical trials. Ann Surg Oncol, 9, 668-74 (2002)
103. Kessler, T. A., A. Pfeifer, S. Silletti, R. M. Mesters, W. E. Berdel, I. Verrna & D. Cheresh: Matrix metalloproteinase/integrin interactions as target for antiangiogenic treatment strategies. Ann Hematol, 81 Suppl 2, S69-70 (2002)
104. Pluderi, M., V. Lucini, D. Caronzolo, M. Pannacci, F. Costa, G. Carrabba, C. Giussani, S. Grosso, F. Colleoni, F. Scaglione, R. Villani, A. Bikfalvi & L. Bello: Long-term inhibition of glioma growth by systemic administration of human PEX. J Neurosurg Sci, 47,69-78 (2003)
105. Lee, H. Y., K. S. Park, M. K. Kim, T. Lee, S. H. Ryu, K. J. Woo, T. K. Kwon & Y. S. Bae: A small compound that inhibits tumor necrosis factor-alpha-induced matrix metalloproteinase-9 upregulation. Biochem Biophys Res Commun (2005)
106. Singer, A. J. & R. A. Clark: Cutaneous wound healing. NEngl J Med, 341, 738-46 (1999)
107. Smith, J. A.: Neutrophils, host defense, and inflammation: a double-edged sword. J Leukoc Biol, 56, 672-86 (1994)
108. Mollinedo, F., N. Borregaard & L. A. Boxer: Novel trends in neutrophil structure, function and development. Immunol Today, 20, 535-7 (1999)
109. Garner, W. L., J. L. Rodriguez, C. G. Miller, G. O. Till, R. S. Rees, D. J. Smith & D. G. Remick: Acute skin injury releases neutrophil chemoattractants. Surgery, 116, 42-8 (1994)
110. Parks, W. C.: Matrix metalloproteinases in repair. Wound Repair Regen, 7, 423-32 (1999)
111. Agren, M. S.: Matrix metalloproteinases (MMPs) are required for re-epithelialization of cutaneous wounds. Arch DermatolRes, 291, 583-90 (1999)
112. Ravanti, L. & V. M. Kahari: Matrix metalloproteinases in wound repair (review). Int J Mol Med, 6, 391-407 (2000)
113. Cornelius, L. A., L. C. Nehring, J. D. Roby, W. C. Parks & H. G. Welgus: Human dermal microvascular endothelial cells produce matrix metalloproteinases in response to angiogenic factors and migration. J Invest Dermatol, 105, 170-6(1995)
114. Nwomeh, B. C., H. X. Liang, R. F. Diegelmann, I. K. Cohen & D. R. Yager: Dynamics of the matrix metalloproteinases MMP-1 and MMP-8 in acute open human dermal wounds. Wound Repair Regen, 6, 127-34 (1998)
115. Yager, D. R., L. Y. Zhang, H. X. Liang, R. F. Diegelmann & I. K. Cohen: Wound fluids from human pressure ulcers contain elevated matrix metalloproteinase levels and activity compared to surgical wound fluids. J Invest Dermatol, 107, 743-8 (1996)
116. Trengove, N. J., M. C. Stacey, S. MacAuley, N. Bennett, J. Gibson, F. Burslem, G. Murphy & G. Schultz: Analysis of the acute and chronic wound environments: the role of proteases and their inhibitors. Wound Repair Regen, 1, 442-52 (1999)
117. Ladwig, G. P., M. C. Robson, R. Liu, M. A. Kühn, D. F. Muir & G. S. Schultz: Ratios of activated matrix metalloproteinase-9 to tissue inhibitor of matrix metalloproteinase-1 in wound fluids are inversely correlated with healing of pressure ulcers. Wound Repair Regen, 10,26-37(2002)
118. Weckroth, M., A. Vaheri, J. Lauharanta, T. Sorsa & Y. T. Konttinen: Matrix metalloproteinases, gelatinase and collagenase, in chronic leg ulcers. J Invest Dermatol, 106, 1119-24 (1996)
119. Lobmann, R., A. Ambrosch, G. Schultz, K. Waldmann, S. Schiweck & H. Lehnert: Expression of matrix-metalloproteinases and their inhibitors in the wounds of diabetic and non-diabetic patients. Diabetologia, 45, 1011-6(2002)
120. Esmon, C. T.: The regulation of natural anticoagulant pathways. Science, 235, 1348-52 (1987)
121. Nguyen, M., J. Arkell & C. J. Jackson: Activated protein C directly activates human endothelial gelatinase A. JBiol Chem, 275, 9095-8 (2000)
122. Xue, M., P. Thompson, I. Kelso & C. Jackson: Activated protein C stimulates proliferation, migration and wound closure, inhibits apoptosis and upregulates MMP-2 activity in cultured human keratinocytes. Exp Cell Res, 299,119-27(2004)
123. Makela, M., H. Larjava, E. Pirila, P. Maisi, T. Salo, T. Sorsa & V. J. Uitto: Matrix metalloproteinase 2 (gelatinase A) is related to migration of keratinocytes. Exp Cell Res, 251,67-78(1999)
124. Singh, S., U. P. Singh, J. K. Stiles, W. E. Grizzle & J. W. Lillard, Jr.: Expression and functional role of CCR9 in prostate cancer cell migration and invasion. Clin Cancer Res, 10, 8743-50 (2004)
125. Singh, S., U. P. Singh, W. E. Grizzle & J. W. Lillard, Jr.: CXCL12-CXCR4 interactions modulate prostate cancer cell migration, metalloproteinase expression and invasion. Lab Invest, 84, 1666-76 (2004)
126. Campbell, A. S., D. Albo, T. F. Kimsey, S. L. White & T. N. Wang: Macrophage inflammatory protein-3alpha promotes pancreatic cancer cell invasion. J Surg Res, 123, 96-101 (2005)
127. Masuko-Hongo, K., T. Sato & K. Nishioka: Chemokines differentially induce matrix metalloproteinase3 and prostaglandin E2 in human articular chondrocytes. Clin Exp Rheumatol, 23, 57-62 (2005)
128. Galvez, B. G., L. Genis, S. Matias-Roman, S. A. Oblander, K. Tryggvason, S. S. Apte & A. G. Arroyo: Membrane type 1-matrix metalloproteinase is regulated by chemokines monocyte-chemoattractant protein-l/ccl2 and interleukin-8/CXCL8 in endothelial cells during angiogenesis. J Biol Chem, 280, 1292-8 (2005)
129. Zhang, J., S. Sarkar & V. W. Yong: The chemokine stromal cell derived factor-1 (CXCL12) promotes glioma invasiveness through MT2-matrix metalloproteinase. Carcinogenesis (2005)