The impact of the extracellular matrix on inflammation

Nature Reviews Immunology

Volumn 10, Issue 10, 2010, Pages 712-723

  Sorokin, Lydia ^a  

^a UNIVERSITY OF MÜNSTER   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BIGLYCAN; COLLAGEN TYPE 4; ELASTASE; ENTACTIN; GAMMA INTERFERON; GELATINASE A; GELATINASE B; HYALURONIC ACID; INTEGRIN; INTERLEUKIN 17; INTERLEUKIN 1BETA; INTERSTITIAL COLLAGENASE; LAMININ; MATRILYSIN; MELATONIN 1 RECEPTOR; OSTEOPONTIN; PROTEINASE; STROMELYSIN; TENASCIN; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 2; TISSUE INHIBITOR OF METALLOPROTEINASE 3; TISSUE INHIBITOR OF METALLOPROTEINASE 4; TRANSFORMING GROWTH FACTOR BETA; TUMOR NECROSIS FACTOR;

CELL ACTIVATION; CELL DIFFERENTIATION; CELL INFILTRATION; CELL MIGRATION; CELL SURVIVAL; DELAYED HYPERSENSITIVITY; EXTRACELLULAR MATRIX; HUMAN; IMMUNE RESPONSE; IMMUNOCOMPETENT CELL; INFLAMMATION; LEUKOCYTE; MULTIPLE SCLEROSIS; NEUTROPHIL; NONHUMAN; PNEUMONIA; PRIORITY JOURNAL; REVIEW; T LYMPHOCYTE; VASCULAR ENDOTHELIUM; ANIMAL; IMMUNOLOGY;

ANIMALS; EXTRACELLULAR MATRIX; HUMANS; INFLAMMATION;

EID: 77957221743     PISSN: 14741733     EISSN: None     Source Type: Journal    
DOI: 10.1038/nri2852     Document Type: Review

References (129)

1. Nourshargh, S., Hordijk, P. L. and Sixt, M. Breaching multiple barriers: leukocyte motility through venular walls and the interstitium. Nature Rev. Mol. Cell Biol. 11, 366-378 (2010).
2. Vestweber, D. Adhesion and signaling molecules controlling the transmigration of leukocytes through endothelium. Immunol. Rev. 218, 178-196 (2007). (Pubitemid 47052303)
3. Alon, R. and Ley, K. Cells on the run: shear-regulated integrin activation in leukocyte rolling and arrest on endothelial cells. Curr. Opin. Cell Biol. 20, 525-532 (2008).
4. Morrison, C. J., Butler, G. S., Rodriguez, D. and Overall, C. M. Matrix metalloproteinase proteomics: substrates, targets, and therapy. Curr. Opin. Cell Biol. 21, 645-653 (2009).
5. Cauwe, B., Van den Steen, P. E. and Opdenakker, G. The biochemical, biological, and pathological kaleidoscope of cell surface substrates processed by matrix metalloproteinases. Crit. Rev. Biochem. Mol. Biol. 42, 113-185 (2007). (Pubitemid 46911962)
6. Struyf, S., Proost, P. and Van Damme, J. Regulation of the immune response by the interaction of chemokines and proteases. Adv. Immunol. 81, 1-44 (2003). (Pubitemid 38009040)
7. Hohenester, E. and Engel, J. Domain structure and organisation in extracellular matrix proteins. Matrix Biol. 21, 115-128 (2002). (Pubitemid 34145238)
8. Hynes, R. O. The extracellular matrix: not just pretty fibrils. Science 326, 1216-1219 (2009).
9. Lokmic, Z. et al. The extracellular matrix of the spleen as a potential organizer of immune cell compartments. Semin. Immunol. 20, 4-13 (2008).
10. Sixt, M. et al. The conduit system transports soluble antigens from the afferent lymph to resident dendritic cells in the T cell area of the lymph node. Immunity 22, 19-29 (2005). (Pubitemid 40143448)
11. Eckes, B., Nischt, R. and Krieg, T. Cell-matrix interactions in dermal repair and scarring. Fibrogenesis Tissue Repair 3, 4 (2010).
12. Engelhardt, B. and Wolburg, H. Mini-review: Transendothelial migration of leukocytes: through the front door or around the side of the house? Eur. J. Immunol. 34, 2955-2963 (2004). (Pubitemid 39549374)
13. Furie, M. B., Naprstek, B. L. and Silverstein, S. C. Migration of neutrophils across monolayers of cultured microvascular endothelial cells. An in vitro model of leucocyte extravasation. J. Cell Sci. 88, 161-175 (1987).
14. Hurley, J. V. An electron microscopic study of leucocytic emigration and vascular permeability in rat skin. Aust. J. Exp. Biol. Med. Sci. 41, 171-186 (1963).
15. Marchesi, V. T. and Florey, H. W. Electron micrographic observations on the emigration of leucocytes. Q. J. Exp. Physiol. Cogn. Med. Sci. 45, 343-348 (1960).
16. Ohashi, K. L., Tung, D. K., Wilson, J., Zweifach, B. W. and Schmid-Schonbein, G. W. Transvascular and interstitial migration of neutrophils in rat mesentery. Microcirculation 3, 199-210 (1996).
17. Hoshi, O. and Ushiki, T. Neutrophil extravasation in rat mesenteric venules induced by the chemotactic peptide N-formyl-methionyl- luecylphenylalanine (fMLP), with special attention to a barrier function of the vascular basal lamina for neutrophil migration. Arch. Histol. Cytol. 67, 107-114 (2004). (Pubitemid 38508687)
18. Wang, S. et al. Venular basement membranes contain specific matrix protein low expression regions that act as exit points for emigrating neutrophils. J. Exp. Med. 203, 1519-1532 (2006). (Pubitemid 43877612)
19. Bartholomaus, I. et al. Effector T cell interactions with meningeal vascular structures in nascent autoimmune CNS lesions. Nature 462, 94-98 (2009).
20. Muller, W. A. Mechanisms of transendothelial migration of leukocytes. Circ. Res. 105, 223-230 (2009).
21. Schenkel, A. R., Dufour, E. M., Chew, T. W., Sorg, E. and Muller, W. A. The murine CD99-related molecule CD99-like 2 (CD99L2) is an adhesion molecule involved in the inflammatory response. Cell Commun. Adhes. 14, 227-237 (2007).
22. Bixel, M. G. et al. A CD99-related antigen on endothelial cells mediates neutrophil but not lymphocyte extravasation in vivo. Blood 109, 5327-5336 (2007).
23. Bixel, G. et al. CD99 and CD99L act at the same site as, but independently of, PECAM-1 during leukocyte diapedesis. Blood 116, 1172-1184 (2010).
24. Lou, O., Alcaide, P., Luscinskas, F. W. and Muller, W. A. CD99 is a key mediator of the transendothelial migration of neutrophils. J. Immunol. 178, 1136-1143 (2007). (Pubitemid 46095186)
25. Wakelin, M. W. et al. An anti-platelet-endothelial cell adhesion molecule-1 antibody inhibits leukocyte extravasation from mesenteric microvessels in vivo by blocking the passage through the basement membrane. J. Exp. Med. 184, 229-239 (1996).
26. Dangerfield, J., Larbi, K. Y., Huang, M. T., Dewar, A. and Nourshargh, S. PECAM-1 (CD31) homophilic interaction up-regulates ?6?1 on transmigrated neutrophils in vivo and plays a functional role in the ability of ?6 integrins to mediate leukocyte migration through the perivascular basement membrane. J. Exp. Med. 196, 1201-1211 (2002). (Pubitemid 35304186)
27. Yurchenco, P. D. and Patton, B. L. Developmental and pathogenic mechanisms of basement membrane assembly. Curr. Pharm. Des. 15, 1277-1294 (2009).
28. Poschl, E. et al. Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development. Development 131, 1619-1628 (2004). (Pubitemid 38559288)
29. Li, S. et al. Matrix assembly, regulation, and survival functions of laminin and its receptors in embryonic stem cell differentiation. J. Cell Biol. 157, 1279-1290 (2002). (Pubitemid 34847796)
30. McKee, K. K., Harrison, D., Capizzi, S. and Yurchenco, P. D. Role of laminin terminal globular domains in basement membrane assembly. J. Biol. Chem. 282, 21437-21447 (2007). (Pubitemid 47099937)
31. Koch, M. et al. A novel member of the netrin family, β-netrin, shares homology with the γ chain of laminin: identification, expression, and functional characterization. J. Cell Biol. 151, 221-234 (2000).
32. Timpl, R., Sasaki, T., Kostka, G. and Chu, M. L. Fibulins: a versatile family of extracellular matrix proteins. Nature Rev. Mol. Cell Biol. 4, 479-489 (2003). (Pubitemid 36648593)
33. Brekken, R. A. and Sage, E. H. SPARC, a matricellular protein: at the crossroads of cell-matrix. Matrix Biol. 19, 569-580 (2000).
34. Sasaki, T. et al. Endostatins derived from collagens XV and XVIII differ in structural and binding properties, tissue distribution and anti-angiogenic activity. J. Mol. Biol. 301, 1179-1190 (2000).
35. Hallmann, R. et al. Expression and function of laminins in the embryonic and mature vasculature. Physiol. Rev. 85, 979-1000 (2005). (Pubitemid 40885221)
36. Burns, A. R., Smith, C. W. and Walker, D. C. Unique structural features that influence neutrophil emigration into the lung. Physiol. Rev. 83, 309-336 (2003).
37. Sixt, M. et al. Endothelial cell laminin isoforms, laminin 8 and 10, play decisive roles in in T-cell recruitment across the blood-brain-barrier in an experimental autoimmune encephalitis model (EAE). J. Cell Biol. 153, 933-945 (2001). (Pubitemid 34289234)
38. Wu, C. et al. Endothelial basement membrane laminin ?5 selectively inhibits T lymphocyte extravasation into the brain. Nature Med. 15, 519-527 (2009).
39. Frieser, M. et al. Cloning of the mouse laminin β4 cDNA. Expression in a subset of endothelium. Eur. J. Biochem. 246, 727-735 (1997). (Pubitemid 27252916)
40. Khoshnoodi, J., Pedchenko, V. and Hudson, B. G. Mammalian collagen IV. Microsc. Res. Tech. 71, 357-370 (2008). (Pubitemid 351620858)
41. Iozzo, R. V. Basement membrane proteoglycans: from cellar to ceiling. Nature Rev. Mol. Cell Biol. 6, 646-656 (2005).
42. Bader, B. L. et al. Compound genetic ablation of nidogen 1 and 2 causes basement membrane defects and perinatal lethality in mice. Mol. Cell Biol. 25, 6846-6856 (2005).
43. Sorokin, L. M. et al. Developmental regulation of laminin β5 suggests a role in epithelial and endothelial cell maturation. Dev. Biol. 189, 285-300 (1997).
44. Brachvogel, B. et al. Isolated Anxa5+/Sca-1+ perivascular cells from mouse meningeal vasculature retain their perivascular phenotype in vitro and in vivo. Exp. Cell Res. 313, 2730-2743 (2007). (Pubitemid 46977343)
45. Stratman, A. N., Malotte, K. M., Mahan, R. D., Davis, M. J. and Davis, G. E. Pericyte recruitment during vasculogenic tube assembly stimulates endothelial basement membrane matrix formation. Blood 114, 5091-5101 (2009).
46. Abramsson, A. et al. Defective N-sulfation of heparan sulfate proteoglycans limits PDGF-BB binding and pericyte recruitment in vascular development. Genes Dev. 21, 316-331 (2007). (Pubitemid 46246780)
47. Kalamajski, S. and Oldberg, A. The role of small leucinerich proteoglycans in collagen fibrillogenesis. Matrix Biol. 29, 248-253 (2010).
48. Rowe, R. G. and Weiss, S. J. Breaching the basement membrane: who, when and how? Trends Cell Biol. 18, 560-574 (2008).
49. Senior, R. M., Gresham, H. D., Griffin, G. L., Brown, E. J. and Chung, A. E. Entactin stimulates neutrophil adhesion and chemotaxis through interactions between its Arg-Gly-Asp (RGD) domain and the leukocyte response integrin. J. Clin. Invest. 90, 2251-2257 (1992).
50. Adair-Kirk, T. L. et al. A site on laminin β5, AQARSAASKVKVSMKF, induces inflammatory cell production of matrix metalloproteinase-9 and chemotaxis. J. Immunol. 171, 398-406 (2003).
51. Pipoly, D. J. and Crouch, E. C. Degradation of native type IV procollagen by human neutrophil elastase. Implications for leukocyte-mediated degradation of basement membranes. Biochemistry 26, 5748-5754 (1987).
52. Heck, L. W., Blackburn, W. D., Irwin, M. H. and Abrahamson, D. R. Degradation of basement membrane laminin by human neutrophil elastase and cathepsin G. Am. J. Pathol. 136, 1267-1274 (1990). (Pubitemid 20210325)
53. Steadman, R. et al. Laminin cleavage by activated human neutrophils yields proteolytic fragments with selective migratory properties. J. Leukoc. Biol. 53, 354-365 (1993). (Pubitemid 23159876)
54. Huber, A. R. and Weiss, S. J. Disruption of the subendothelial basement membrane during neutrophil diapedesis in an in vitro construct of a blood vessel wall. J. Clin. Invest. 83, 1122-1136 (1989).
55. Agrawal, S. et al. Dystroglycan is selectively cleaved at the parenchymal basement membrane at sites of leukocyte extravasation in experimental autoimmune encephalomyelitis. J. Exp. Med. 203, 1007-1019 (2006).
56. Huber, A. R., Kunkel, S. L., Todd, R. F., 3rd and Weiss, S. J. Regulation of transendothelial neutrophil migration by endogenous interleukin-8. Science 254, 99-102 (1991).
57. Marchesi, V. T. The site of leucocyte emigration during inflammation. Q. J. Exp. Physiol. Cogn. Med. Sci. 46, 115-118 (1961).
58. Steadman, R. et al. Human neutrophils do not degrade major basement membrane components during chemotactic migration. Int. J. Biochem. Cell Biol. 29, 993-1004 (1997). (Pubitemid 27478885)
59. Pham, C. T. Neutrophil serine proteases: specific regulators of inflammation. Nature Rev. Immunol. 6, 541-550 (2006).
60. Walker, D. C., Behzad, A. R. and Chu, F. Neutrophil migration through preexisting holes in the basal laminae of alveolar capillaries and epithelium during streptococcal pneumonia. Microvasc. Res. 50, 397-416 (1995).
61. Abrams, G. A., Goodman, S. L., Nealey, P. F., Franco, M. and Murphy, C. J. Nanoscale topography of the basement membrane underlying the corneal epithelium of the rhesus macaque. Cell Tissue Res. 299, 39-46 (2000). (Pubitemid 30028721)
62. Candiello, J. et al. Biomechanical properties of native basement membranes. FEBS J. 274, 2897-2908 (2007). (Pubitemid 46800555)
63. Last, J. A., Liliensiek, S. J., Nealey, P. F. and Murphy, C. J. Determining the mechanical properties of human corneal basement membranes with atomic force microscopy. J. Struct. Biol. 167, 19-24 (2009).
64. Kenne, E. et al. Immune cell recruitment to inflammatory loci is impaired in mice deficient in basement membrane protein laminin ?4. J. Leukoc. Biol. 29 Apr 2010 (doi:10.1189/jlb.0110043).
65. Engelhardt, B. and Sorokin, L. The blood-brain and the blood-cerebrospinal fluid barriers: function and dysfunction. Semin. Immunopathol. 31, 497-511 (2009).
66. Wekerle, H. Lessons from multiple sclerosis: models, concepts, observations. Ann. Rheum. Dis. 67, 56-60 (2008).
67. Thyboll, J. et al. Deletion of the laminin ?4 chain leads to impaired microvessel maturation. Mol. Cell Biol. 22, 1194-1202 (2002). (Pubitemid 34094855)
68. Moore, S. A. et al. Deletion of brain dystroglycan recapitulates aspects of congenital muscular dystrophy. Nature 418, 422-425 (2002).
69. Lammermann, T. et al. Rapid leukocyte migration by integrin-independent flowing and squeezing. Nature 453, 51-55 (2008). (Pubitemid 351630331)
70. Wolf, K., Muller, R., Borgmann, S., Brocker, E. B. and Friedl, P. Amoeboid shape change and contact guidance: T-lymphocyte crawling through fibrillar collagen is independent of matrix remodeling by MMPs and other proteases. Blood 102, 3269-3269 (2003). (Pubitemid 37314765)
71. Friedl, P. and Wolf, K. Proteolytic and non-proteolytic migration of tumour cells and leucocytes. Biochem. Soc. Symp. 70, 277-285 (2003). (Pubitemid 38497233)
72. Sabeh, F., Li, X. Y., Saunders, T. L., Rowe, R. G. and Weiss, S. J. Secreted versus membrane-anchored collagenases: relative roles in fibroblast-dependent collagenolysis and invasion. J. Biol. Chem. 284, 23001-23011 (2009).
73. Sabeh, F., Shimizu-Hirota, R. and Weiss, S. J. Proteasedependent versus -independent cancer cell invasion programs: three-dimensional amoeboid movement revisited. J. Cell Biol. 185, 11-19 (2009).
74. Rabodzey, A., Alcaide, P., Luscinskas, F. W. and Ladoux, B. Mechanical forces induced by the transendothelial migration of human neutrophils. Biophys. J. 95, 1428-1438 (2008).
75. Oakes, P. W. et al. Neutrophil morphology and migration are affected by substrate elasticity. Blood 114, 1387-1395 (2009).
76. Shulman, Z. et al. Lymphocyte crawling and transendothelial migration require chemokine triggering of high-affinity LFA-1 integrin. Immunity 30, 384-396 (2009).
77. Voisin, M. B., Woodfin, A. and Nourshargh, S. Monocytes and neutrophils exhibit both distinct and common mechanisms in penetrating the vascular basement membrane in vivo. Arterioscler. Thromb. Vasc. Biol. 29, 1193-1199 (2009).
78. Weathington, N. M. et al. A novel peptide CXCR ligand derived from extracellular matrix degradation during airway inflammation. Nature Med. 12, 317-323 (2006). (Pubitemid 43355080)
79. Gaggar, A. et al. A novel proteolytic cascade generates an extracellular matrix-derived chemoattractant in chronic neutrophilic inflammation. J. Immunol. 180, 5662-5669 (2008).
80. OReilly, P. J. et al. Neutrophils contain prolyl endopeptidase and generate the chemotactic peptide, PGP, from collagen. J. Neuroimmunol. 217, 51-54 (2009).
81. Senior, R. M., Griffin, G. L. and Mecham, R. P. Chemotactic activity of elastin-derived peptides. J. Clin. Invest. 66, 859-862 (1980).
82. Hunninghake, G. W. et al. Elastin fragments attract macrophage precursors to diseased sites in pulmonary emphysema. Science 212, 925-927 (1981).
83. Houghton, A. M. et al. Elastin fragments drive disease progression in a murine model of emphysema. J. Clin. Invest. 116, 753-759 (2006).
84. Ospelt, C. and Gay, S. TLRs and chronic inflammation. Int. J. Biochem. Cell Biol. 42, 495-505 (2010).
85. Oldberg, A., Franzen, A. and Heinegard, D. Cloning and sequence analysis of rat bone sialoprotein (osteopontin) cDNA reveals an Arg-Gly-Asp cell-binding sequence. Proc. Natl Acad. Sci. USA 83, 8819-8823 (1986). (Pubitemid 17223492)
86. Wong, C. K., Lit, L. C., Tam, L. S., Li, E. K. and Lam, C. W. Elevation of plasma osteopontin concentration is correlated with disease activity in patients with systemic lupus erythematosus. Rheumatology (Oxford) 44, 602-606 (2005). (Pubitemid 41487227)
87. Xu, G. et al. Role of osteopontin in amplification and perpetuation of rheumatoid synovitis. J. Clin. Invest. 115, 1060-1067 (2005). (Pubitemid 40489411)
88. Sato, T. et al. Osteopontin/Eta-1 upregulated in Crohns disease regulates the Th1 immune response. Gut 54, 1254-1262 (2005). (Pubitemid 41192483)
89. Chabas, D. et al. The influence of the proinflammatory cytokine, osteopontin, on autoimmune demyelinating disease. Science 294, 1731-1735 (2001).
90. Comabella, M. et al. Plasma osteopontin levels in multiple sclerosis. J. Neuroimmunol. 158, 231-239 (2005). (Pubitemid 39626091)
91. Hur, E. M. et al. Osteopontin-induced relapse and progression of autoimmune brain disease through enhanced survival of activated T cells. Nature Immunol. 8, 74-83 (2007).
92. Steinman, L. A molecular trio in relapse and remission in multiple sclerosis. Nature Rev. Immunol. 9, 440-447 (2009).
93. Ashkar, S. et al. Eta-1 (osteopontin): an early component of type-1 (cell-mediated) immunity. Science 287, 860-864 (2000). (Pubitemid 30084330)
94. Adler, B., Ashkar, S., Cantor, H. and Weber, G. F. Costimulation by extracellular matrix proteins determines the response to TCR ligation. Cell. Immunol. 210, 30-40 (2001). (Pubitemid 32756939)
95. Pender, M. P., Nguyen, K. B., McCombe, P. A. and Kerr, J. F. Apoptosis in the nervous system in experimental allergic encephalomyelitis. J. Neurol. Sci. 104, 81-87 (1991).
96. Gold, R., Hartung, H. P. and Lassmann, H. T-cell apoptosis in autoimmune diseases: termination of inflammation in the nervous system and other sites with specialized immune-defense mechanisms. Trends Neurosci. 20, 399-404 (1997). (Pubitemid 27364510)
97. Hocking, A. M., Shinomura, T. and McQuillan, D. J. Leucine-rich repeat glycoproteins of the extracellular matrix. Matrix Biol. 17, 1-19 (1998). (Pubitemid 28206020)
98. Okamura, Y. et al. The extra domain A of fibronectin activates Toll-like receptor 4. J. Biol. Chem. 276, 10229-10233 (2001). (Pubitemid 37391934)
99. Stern, R., Asari, A. A. and Sugahara, K. N. Hyaluronan fragments: an information-rich system. Eur. J. Cell Biol. 85, 699-715 (2006). (Pubitemid 44070579)
100. Johnson, G. B., Brunn, G. J., Kodaira, Y. and Platt, J. L. Receptor-mediated monitoring of tissue well-being via detection of soluble heparan sulfate by Toll-like receptor. J. Immunol. 168, 5233-5239 (2002). (Pubitemid 34495991)
101. Taylor, K. R. and Gallo, R. L. Glycosaminoglycans and their proteoglycans: host-associated molecular patterns for initiation and modulation of inflammation. FASEB J. 20, 9-22 (2006).
102. Midwood, K. et al. Tenascin-C is an endogenous activator of Toll-like receptor 4 that is essential for maintaining inflammation in arthritic joint disease. Nature Med. 15, 774-780 (2009).
103. Schaefer, L. et al. The matrix component biglycan is proinflammatory and signals through Toll-like receptors 4 and 2 in macrophages. J. Clin. Invest. 115, 2223-2233 (2005). (Pubitemid 41134165)
104. Schaefer, L. Extracellular matrix molecules: endogenous danger signals as new drug targets in kidney diseases. Curr. Opin. Pharmacol. 10, 185-190 (2010).
105. Jiang, D. et al. Regulation of lung injury and repair by Toll-like receptors and hyaluronan. Nature Med. 11, 1173-1179 (2005). (Pubitemid 43093664)
106. Noble, P. W. Hyaluronan and its catabolic products in tissue injury and repair. Matrix Biol. 21, 25-29 (2002).
107. McKee, C. M. et al. Hyaluronan (HA) fragments induce chemokine gene expression in alveolar macrophages. The role of HA size and CD44. J. Clin. Invest. 98, 2403-2413 (1996).
108. Mummert, M. E. et al. Synthesis and surface expression of hyaluronan by dendritic cells and its potential role in antigen presentation. J. Immunol. 169, 4322-4331 (2002).
109. Termeer, C. et al. Oligosaccharides of hyaluronan activate dendritic cells via Toll-like receptor 4. J. Exp. Med. 195, 99-111 (2002). (Pubitemid 34074500)
110. Overall, C. M. and Blobel, C. P. In search of partners: linking extracellular proteases to substrates. Nature Rev. Mol. Cell Biol. 8, 245-257 (2007). (Pubitemid 46316033)
111. Vanacore, R. M. et al. The ?1.?2 network of collagen IV. Reinforced stabilization of the noncollagenous domain-1 by noncovalent forces and the absence of Met-Lys cross-links. J. Biol. Chem. 279, 44723-44730 (2004).
112. Nagase, H., Visse, R. and Murphy, G. Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc. Res. 69, 562-573 (2006). (Pubitemid 43139720)
113. Di Girolamo, N. et al. Human mast cell-derived gelatinase B (matrix metalloproteinase-9) is regulated by inflammatory cytokines: role in cell migration. J. Immunol. 177, 2638-2650 (2006). (Pubitemid 44201023)
114. Qiu, Z. et al. Interleukin-17 regulates chemokine and gelatinase B expression in fibroblasts to recruit both neutrophils and monocytes. Immunobiology 214, 835-842 (2009).
115. Hu, J., Van den Steen, P. E., Sang, Q. X. and Opdenakker, G. Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases. Nature Rev. Drug Discov. 6, 480-498 (2007). (Pubitemid 47064570)
116. Overall, C. M., McQuibban, G. A. and Clark-Lewis, I. Discovery of chemokine substrates for matrix metalloproteinases by exosite scanning: a new tool for degradomics. Biol. Chem. 383, 1059-1066 (2002). (Pubitemid 35215050)
117. Van den Steen, P. E., Proost, P., Wuyts, A., Van Damme, J. and Opdenakker, G. Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-? and leaves RANTES and MCP-2 intact. Blood 96, 2673-2681 (2000).
118. McQuibban, G. A. et al. Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. Science 289, 1202-1206 (2000).
119. Van Den Steen, P. E. et al. 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, 3739-3749 (2003).
120. Gearing, A. J. et al. Processing of tumour necrosis factor-γ precursor by metalloproteinases. Nature 370, 555-557 (1994). (Pubitemid 24264920)
121. Ito, A. et al. Degradation of interleukin 1β by matrix metalloproteinases. J. Biol. Chem. 271, 14657-14660 (1996).
122. Schonbeck, U., Mach, F. and Libby, P. Generation of biologically active IL-1β by matrix metalloproteinases: a novel caspase-1-independent pathway of IL-1β processing. J. Immunol. 161, 3340-3346 (1998). (Pubitemid 128470627)
123. Redondo-Munoz, J. et al. Matrix metalloproteinase-9 promotes chronic lymphocytic leukemia B cell survival through its hemopexin domain. Cancer Cell 17, 160-172 (2010).
124. Denhardt, D. T., Noda, M., ORegan, A. W., Pavlin, D. and Berman, J. S. Osteopontin as a means to cope with environmental insults: regulation of inflammation, tissue remodeling, and cell survival. J. Clin. Invest. 107, 1055-1061 (2001). (Pubitemid 32422899)
125. Leask, A. and Abraham, D. J. TGF-β signaling and the fibrotic response. FASEB J. 18, 816-827 (2004).
126. Hu, X. and Ivashkiv, L. B. Cross-regulation of signaling pathways by interferon-β: implications for immune responses and autoimmune diseases. Immunity 31, 539-550 (2009).
127. McQuibban, G. A. et al. Matrix metalloproteinase activity inactivates the CXC chemokine stromal cellderived factor-1. J. Biol. Chem. 276, 43503-43508 (2001). (Pubitemid 37383907)
128. McQuibban, G. A. et al. Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo. Blood 100, 1160-1167 (2002).
129. Hayashida, K., Parks, W. C. and Park, P. W. Syndecan-1 shedding facilitates the resolution of neutrophilic inflammation by removing sequestered CXC chemokines. Blood 114, 3033-3043 (2009).