Metalloproteinases and their inhibitors: Regulators of wound healing

International Journal of Biochemistry and Cell Biology

Volumn 40, Issue 6-7, 2008, Pages 1334-1347

  Gill, Sean E ^a   Parks, William C ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

Author keywords

Chemokines; Extracellular matrix; Inflammation; Metalloproteinases; Wound healing

Indexed keywords

CHEMOKINE; GELATINASE A; MATRILYSIN; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 14; MATRIX METALLOPROTEINASE INHIBITOR; STROMELYSIN 2;

CELL MIGRATION; CELL REGENERATION; HUMAN; NONHUMAN; PROTEIN FUNCTION; REVIEW; WOUND HEALING;

ANIMALS; GENE EXPRESSION REGULATION, ENZYMOLOGIC; HUMANS; METALLOPROTEASES; MODELS, BIOLOGICAL; TISSUE INHIBITOR OF METALLOPROTEINASES; WOUND HEALING;

EID: 43049092274     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2007.10.024     Document Type: Review

References (96)

1. Alexander C.M., Howard E.W., Bissell M.J., and Werb Z. Rescue of mammary epithelial cell apoptosis and entactin degradation by a tissue inhibitor of metalloproteinases-1 transgene. J. Cell Biol. 135 6 Pt 1 (1996) 1669-1677
2. Alexander J.S., and Elrod J.W. Extracellular matrix, junctional integrity and matrix metalloproteinase interactions in endothelial permeability regulation. J. Anat. 200 6 (2002) 561-574
3. Amour A., Knight C.G., Webster A., Slocombe P.M., Stephens P.E., Knauper V., et al. The in vitro activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3. FEBS Lett. 473 3 (2000) 275-279
4. Amour A., Slocombe P.M., Webster A., Butler M., Knight C.G., Smith B.J., et al. TNF-alpha converting enzyme (TACE) is inhibited by TIMP-3. FEBS Lett. 435 1 (1998) 39-44
5. Atkinson J.J., Toennies H.M., Holmbeck K., and Senior R.M. Membrane-type 1 matrix metalloproteinase is necessary for distal airway epithelial repair and keratinocyte growth factor receptor expression after acute injury. Am. J. Physiol. Lung Cell Mol. Physiol. 293 (2007) L600-L610
6. Baker A.H., Edwards D.R., and Murphy G. Metalloproteinase inhibitors: biological actions and therapeutic opportunities. J. Cell Sci. 115 Pt 19 (2002) 3719-3727
7. Betsuyaku T., Fukuda Y., Parks W.C., Shipley J.M., and Senior R.M. Gelatinase B is required for alveolar bronchiolization after intratracheal bleomycin. Am. J. Pathol. 157 2 (2000) 525-535
8. Birkedal-Hansen H., Moore W.G., Bodden M.K., Windsor L.J., Birkedal-Hansen B., DeCarlo A., et al. Matrix metalloproteinases: A review. Crit. Rev. Oral Biol. Med. 4 2 (1993) 197-250
9. Black R.A., Rauch C.T., Kozlosky C.J., Peschon J.J., Slack J.L., Wolfson M.F., et al. A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 385 (1997) 729-733
10. Black R.A., and White J.M. ADAMs: Focus on the protease domain. Curr. Opin. Cell. Biol. 10 5 (1998) 654-659
11. Boulday G., Fitau J., Coupel S., Soulillou J.P., and Charreau B. Exogenous tissue inhibitor of metalloproteinase-1 promotes endothelial cell survival through activation of the phosphatidylinositol 3-kinase/Akt pathway. Ann. N. Y. Acad. Sci. 1030 (2004) 28-36
12. Bove P.F., Wesley U.V., Greul A.K., Hristova M., Dostmann W.R., and van der Vliet A. Nitric oxide promotes airway epithelial wound repair through enhanced activation of MMP-9. Am. J. Respir. Cell Mol. Biol. 36 2 (2007) 138-146
13. Brew K., Dinakarpandian D., and Nagase H. Tissue inhibitors of metalloproteinases: Evolution, structure and function. Biochim. Biophys. Acta 1477 1/2 (2000) 267-283
14. Brooks P.C., Clark R.A., and Cheresh D.A. Requirement of vascular integrin alpha v beta 3 for angiogenesis. Science 264 5158 (1994) 569-571
15. Brown L.F., Yeo K.T., Berse B., Yeo T.K., Senger D.R., Dvorak H.F., et al. Expression of vascular permeability factor (vascular endothelial growth factor) by epidermal keratinocytes during wound healing. J. Exp. Med. 176 5 (1992) 1375-1379
16. Bullard K.M., Lund L., Mudgett J.S., Mellin T.N., Hunt T.K., Murphy B., et al. Impaired wound contraction in stromelysin-1-deficient mice. Ann. Surg. 230 2 (1999) 260-265
17. Chen P., Farivar A.S., Mulligan M.S., and Madtes D.K. Tissue inhibitor of metalloproteinase-1 deficiency abrogates obliterative airway disease after heterotopic tracheal transplantation. Am. J. Respir. Cell Mol. Biol. 34 4 (2006) 464-472
18. Clark R.A., Quinn J.H., Winn H.J., Lanigan J.M., Dellepella P., and Colvin R.B. Fibronectin is produced by blood vessels in response to injury. J. Exp. Med. 156 2 (1982) 646-651
19. Clark R.A.F., Lanigan J.M., DellaPelle P., Manseau E., Dvorak H.F., and Colvin R.B. Fibronectin and fibrin provide a provisional matrix for epidermal cell migration during wound re-epithelization. J. Invest. Dermatol. 79 (1982) 264-269
20. Clark-Lewis I., Kim K.S., Rajarathnam K., Gong J.H., Dewald B., Moser B., et al. Structure-activity relationships of chemokines. J. Leukoc. Biol. 57 5 (1995) 703-711
21. Coraux C., Martinella-Catusse C., Nawrocki-Raby B., Hajj R., Burlet H., Escotte S., et al. Differential expression of matrix metalloproteinases and interleukin-8 during regeneration of human airway epithelium in vivo. J. Pathol. 206 2 (2005) 160-169
22. Corbel M., Caulet-Maugendre S., Germain N., Molet S., Lagente V., and Boichot E. Inhibition of bleomycin-induced pulmonary fibrosis in mice by the matrix metalloproteinase inhibitor batimastat. J. Pathol. 193 4 (2001) 538-545
23. Corry D.B., Kiss A., Song L.Z., Song L., Xu J., Lee S.H., et al. Overlapping and independent contributions of MMP2 and MMP9 to lung allergic inflammatory cell egression through decreased CC chemokines. FASEB J. 18 (2004) 995-997
24. Corry D.B., Rishi K., Kanellis J., Kiss A., Song L.Z., Xu J., et al. Decreased allergic lung inflammatory cell egression and increased susceptibility to asphyxiation in MMP2-deficiency. Nat. Immunol. 3 (2002) 347-353
25. d'Ortho M.P., Clerici C., Yao P.M., Delacourt C., Delclaux C., Franco-Montoya M.L., et al. Alveolar epithelial cells in vitro produce gelatinases and tissue inhibitor of matrix metalloproteinase-2. Am. J. Physiol. 273 3 Pt 1 (1997) L663-L675
26. Dunsmore S.E., Saarialho-Kere U.K., Roby J.D., Wilson C.L., Matrisian L.M., Welgus H.G., et al. Matrilysin expression and function in airway epithelium. J. Clin. Invest. 102 7 (1998) 1321-1331
27. Egeblad M., and Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat. Rev. Cancer 2 (2002) 161-174
28. Endo K., Takino T., Miyamori H., Kinsen H., Yoshizaki T., Furukawa M., et al. Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration. J. Biol. Chem. 278 42 (2003) 40764-40770
29. Fu X., Parks W.C., and Heinecke J.W. Activation and silencing of matrix metalloproteinases. Semin. Cell Dev. Biol. 19 (2008) 2-13
30. Gill S.E., Pape M.C., Khokha R., Watson A.J., and Leco K.J. A null mutation for tissue inhibitor of metalloproteinases-3 (Timp-3) impairs murine bronchiole branching morphogenesis. Dev. Biol. 261 2 (2003) 313-323
31. Gill S.E., Pape M.C., and Leco K.J. Tissue inhibitor of metalloproteinases 3 regulates extracellular matrix-cell signaling during bronchiole branching morphogenesis. Dev. Biol. 298 2 (2006) 540-554
32. Huxley-Jones J., Clarke T.K., Beck C., Toubaris G., Robertson D.L., and Boot-Handford R.P. The evolution of the vertebrate metzincins; insights from Ciona intestinalis and Danio rerio. BMC Evol. Biol. 7 (2007) 63
33. Inoue M., Kratz G., Haegerstrand A., and Ståhle-Bäckdahl M. Collagenase expression is rapidly induced in wound-edge keratinocytes after acute injury in human skin, persists during healing, and stops at re-epithelialization. J. Invest. Dermatol. 104 (1995) 479-483
34. Kashiwagi M., Tortorella M., Nagase H., and Brew K. TIMP-3 is a potent inhibitor of aggrecanase 1 (ADAM-TS4) and aggrecanase 2 (ADAM-TS5). J. Biol. Chem. 276 16 (2001) 12501-12504
35. Kheradmand F., and Werb Z. Shedding light on sheddases: Role in growth and development. Bioessays 24 1 (2002) 8-12
36. Kim K.H., Burkhart K., Chen P., Frevert C.W., Randolph-Habecker J., Hackman R.C., et al. Tissue inhibitor of metalloproteinase-1 deficiency amplifies acute lung injury in bleomycin-exposed mice. Am. J. Respir. Cell Mol. Biol. 33 3 (2005) 271-279
37. Krampert M., Bloch W., Sasaki T., Bugnon P., Rulicke T., Wolf E., et al. Activities of the matrix metalloproteinase stromelysin-2 (MMP-10) in matrix degradation and keratinocyte organization in wounded skin. Mol. Biol. Cell 15 12 (2004) 5242-5254
38. Kruidenier L., MacDonald T.T., Collins J.E., Pender S.L., and Sanderson I.R. Myofibroblast matrix metalloproteinases activate the neutrophil chemoattractant CXCL7 from intestinal epithelial cells. Gastroenterology 130 1 (2006) 127-136
39. Leco K.J., Waterhouse P., Sanchez O.H., Gowing K.L., Poole A.R., Wakeham A., et al. Spontaneous air space enlargement in the lungs of mice lacking tissue inhibitor of metalloproteinases-3 (TIMP-3). J. Clin. Invest. 108 6 (2001) 817-829
40. Li Q., Park P.W., Wilson C.L., and Parks W.C. Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury. Cell 111 5 (2002) 635-646
41. Loechel F., Fox J.W., Murphy G., Albrechtsen R., and Wewer U.M. ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3. Biochem. Biophys. Res. Commun. 278 3 (2000) 511-515
42. Lu P.C., Ye H., Maeda M., and Azar D.T. Immunolocalization and gene expression of matrilysin during corneal wound healing. Invest. Ophthalmol. Vis. Sci. 40 1 (1999) 20-27
43. Madlener M., Mauch C., Conca W., Brauchle M., Parks W.C., and Werner S. Growth factor regulation of stromelysin-2 expression by keratinocytes: Implications for normal and imparied wound healing. Biochem. J. 320 (1996) 659-664
44. Madlener M., Parks W.C., and Werner S. Matrix metalloproteinases (MMPs) and their physiological inhibitors (TIMPs) are differentially regulated during excisional skin wound repair in mice. Exp. Cell Res. 242 (1998) 201-211
45. Madtes D.K., Elston A.L., Kaback L.A., and Clark J.G. Selective induction of tissue inhibitor of metalloproteinase-1 in bleomycin-induced pulmonary fibrosis. Am. J. Respir. Cell Mol. Biol. 24 5 (2001) 599-607
46. Martin E.L., Moyer B.Z., Pape M.C., Starcher B., Leco K.J., and Veldhuizen R.A. Negative impact of tissue inhibitor of metalloproteinase-3 null mutation on lung structure and function in response to sepsis. Am. J. Physiol. Lung Cell Mol. Physiol. 285 6 (2003) L1222-L1232
47. Martin P. Wound healing-aiming for perfect skin regeneration. Science 276 (1997) 75-81
48. Martin P., and Leibovich S.J. Inflammatory cells during wound repair: the good, the bad and the ugly. Trends Cell Biol. 15 11 (2005) 599-607
49. McCawley L.J., and Matrisian L.M. Matrix metalloproteinases: they're not just for matrix anymore!. Curr. Opin. Cell Biol. 13 (2001) 534-540
50. McCawley L.J., O'Brien P., and Hudson L.G. Epidermal growth factor (EGF)- and scatter factor/hepatocyte growth factor (SF/HGF)- mediated keratinocyte migration is coincident with induction of matrix metalloproteinase (MMP)-9. J. Cell Physiol. 176 2 (1998) 255-265
51. McGuire J.K., Li Q., and Parks W.C. Matrilysin (matrix metalloproteinase-7) mediates E-cadherin ectodomain shedding in injured lung epithelium. Am. J. Pathol. 162 6 (2003) 1831-1843
52. McMillan S.J., Kearley J., Campbell J.D., Zhu X.W., Larbi K.Y., Shipley J.M., et al. Matrix metalloproteinase-9 deficiency results in enhanced allergen-induced airway inflammation. J. Immunol. 172 4 (2004) 2586-2594
53. McQuibban G.A., Butler G.S., Gong J.H., Bendall L., Power C., Clark-Lewis I., et al. Matrix metalloproteinase activity inactivates the CXC chemokine stromal cell-derived factor-1. J. Biol. Chem. 276 47 (2001) 43503-43508
54. McQuibban G.A., Gong J.H., Tam E.M., McCulloch C.A., Clark-Lewis I., and Overall C.M. Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. Science 289 5482 (2000) 1202-1206
55. McQuibban G.A., Gong J.H., Wong J.P., Wallace J.L., Clark-Lewis I., and Overall C.M. Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo. Blood 100 4 (2002) 1160-1167
56. Mirastschijski U., Haaksma C.J., Tomasek J.J., and Ågren M.S. Matrix metalloproteinase inhibitor GM 6001 attenuates keratinocyte migration, contraction and myofibroblast formation in skin wounds. Exp. Cell Res. 299 2 (2004) 465-475
57. Mohammed F.F., Smookler D.S., Taylor S.E., Fingleton B., Kassiri Z., Sanchez O.H., et al. Abnormal TNF activity in Timp3-/- mice leads to chronic hepatic inflammation and failure of liver regeneration. Nat. Genet. 36 9 (2004) 969-977
58. Moss M.L., and Bartsch J.W. Therapeutic benefits from targeting of ADAM family members. Biochemistry 43 23 (2004) 7227-7235
59. Mott J.D., and Werb Z. Regulation of matrix biology by matrix metalloproteinases. Curr. Opin. Cell Biol. 16 5 (2004) 558-564
60. Mulholland B., Tuft S.J., and Khaw P.T. Matrix metalloproteinase distribution during early corneal wound healing. Eye 19 5 (2005) 584-588
61. Nguyen J., Gogusev J., Knapnougel P., and Bauvois B. Protein tyrosine kinase and p38 MAP kinase pathways are involved in stimulation of matrix metalloproteinase-9 by TNF-alpha in human monocytes. Immunol. Lett. 106 (2007) 34-41
62. Parks W.C. Matrix metalloproteinases in repair. Wound Repair. Regen. 7 (1999) 423-432
63. Parks W.C., Wilson C.L., and Lopez-Boado Y.S. Matrix metalloproteinases as modulators of inflammation and innate immunity. Nat. Rev. Immunol. 4 8 (2004) 617-629
64. Pilcher B.K., Dumin J.A., Sudbeck B.D., Krane S.M., Welgus H.G., and Parks W.C. The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix. J. Cell Biol. 137 (1997) 1445-1457
65. Pilcher B.K., Sudbeck B.D., Dumin J.A., Welgus H.G., and Parks W.C. Collagenase-1 and collagen in epidermal repair. Arch. Dermatol. Res. 290 Suppl (1998) S37-S46
66. Pilcher B.K., Wang M., Qin X.J., Parks W.C., Senior R.M., and Welgus H.G. Role of matrix metalloproteinases and their inhibition in cutaneous wound healing and allergic contact hypersensitivity. Ann. N. Y. Acad. Sci. 878 (1999) 12-24
67. Qi J.H., Ebrahem Q., Moore N., Murphy G., Claesson-Welsh L., Bond M., et al. A novel function for tissue inhibitor of metalloproteinases-3 (TIMP3): Inhibition of angiogenesis by blockage of VEGF binding to VEGF receptor-2. Nat. Med. 9 4 (2003) 407-415
68. Roberts C.M., Tani P.H., Bridges L.C., Laszik Z., and Bowditch R.D. MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytes. J. Biol. Chem. 274 41 (1999) 29251-29259
69. Saarialho-Kere U., Kerkela E., Jahkola T., Suomela S., Keski-Oja J., and Lohi J. Epilysin (MMP-28) expression is associated with cell proliferation during epithelial repair. J. Invest. Dermatol. 119 1 (2002) 14-21
70. Saarialho-Kere U.K., Crouch E.C., and Parks W.C. Matrix metalloproteinase matrilysin is constitutively expressed in adult human exocrine epithelium. J. Invest. Dermatol. 105 2 (1995) 190-196
71. Saarialho-Kere U.K., Vaalamo M., Airola K., Niemi K.-M., Oikarinen A.I., and Parks W.C. Interstitial collagenase is expressed by keratinocytes which are actively involved in re-epithelialization in blistering skin diseases. J. Invest. Dermatol. 104 (1995) 982-988
72. Salmela M.T., Pender S.L., Karjalainen-Lindsberg M.L., Puolakkainen P., Macdonald T.T., and Saarialho-Kere U. Collagenase-1 (MMP-1), matrilysin-1 (MMP-7), and stromelysin-2 (MMP-10) are expressed by migrating enterocytes during intestinal wound healing. Scand. J. Gastroenterol. 39 11 (2004) 1095-1104
73. Sawicki G., Marcoux Y., Sarkhosh K., Tredget E.E., and Ghahary A. Interaction of keratinocytes and fibroblasts modulates the expression of matrix metalloproteinases-2 and -9 and their inhibitors. Mol. Cell. Biochem. 269 1/2 (2005) 209-216
74. Scholz F., Schulte A., Adamski F., Hundhausen C., Mittag J., Schwarz A., et al. Constitutive expression and regulated release of the transmembrane chemokine CXCL16 in human and murine skin. J. Invest. Dermatol. 127 6 (2007) 1444-1455
75. Seals D.F., and Courtneidge S.A. The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev. 17 1 (2003) 7-30
76. Shimoda M., Hashimoto G., Mochizuki S., Ikeda E., Nagai N., Ishida S., et al. Binding of ADAM28 to P-selectin glycoprotein ligand-1 enhances P-selectin-mediated leukocyte adhesion to endothelial cells. J. Biol. Chem. 282 35 (2007) 25864-25874
77. Sigurdson L., Sen T., Hall III L., Rubenfeld A., Hard R., Gardella J., et al. Possible impedance of luminal reepithelialization by tracheal cartilage metalloproteinases. Arch. Otolaryngol. Head Neck Surg. 129 2 (2003) 197-200
78. Singer A.J., and Clark R.A. Cutaneous wound healing. N. Engl. J. Med. 341 10 (1999) 738-746
79. Singh R.J., Mason J.C., Lidington E.A., Edwards D.R., Nuttall R.K., Khokha R., et al. Cytokine stimulated vascular cell adhesion molecule-1 (VCAM-1) ectodomain release is regulated by TIMP-3. Cardiovasc. Res. 67 1 (2005) 39-49
80. Smookler D.S., Mohammed F.F., Kassiri Z., Duncan G.S., Mak T.W., and Khokha R. Tissue inhibitor of metalloproteinase 3 regulates TNF-dependent systemic inflammation. J. Immunol. 176 2 (2006) 721-725
81. Spradling K.D., McDaniel A.E., Lohi J., and Pilcher B.K. Epsin 3 is a novel extracellular matrix-induced transcript specific to wounded epithelia. J. Biol. Chem. 276 31 (2001) 29257-29267
82. Surendran K., Simon T.C., Liapis H., and McGuire J.K. Matrilysin (MMP-7) expression in renal tubular damage: Association with Wnt4. Kidney Int. 65 6 (2004) 2212-2222
83. Tam E.M., Morrison C.J., Wu Y.I., Stack M.S., and Overall C.M. Membrane protease proteomics: Isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates. Proc. Natl. Acad. Sci. U.S.A. 101 18 (2004) 6917-6922
84. Terasaki K., Kanzaki T., Aoki T., Iwata K., and Saiki I. Effects of recombinant human tissue inhibitor of metalloproteinases-2 (rh-TIMP-2) on migration of epidermal keratinocytes in vitro and wound healing in vivo. J. Dermatol. 30 3 (2003) 165-172
85. Tester A.M., Cox J.H., Connor A.R., Starr A.E., Dean R.A., Puente X.S., et al. LPS responsiveness and neutrophil chemotaxis in vivo require PMN MMP-8 activity. PLoS ONE 2 (2007) e312
86. 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-alpha and leaves RANTES and MCP-2 intact. Blood 96 8 (2000) 2673-2681
87. Van den Steen P.E., Wuyts A., Husson S.J., Proost P., Van Damme J., and Opdenakker G. 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 18 (2003) 3739-3749
88. Warner R.L., Bhagavathula N., Nerusu K.C., Lateef H., Younkin E., Johnson K.J., et al. Matrix metalloproteinases in acute inflammation: induction of MMP-3 and MMP-9 in fibroblasts and epithelial cells following exposure to pro-inflammatory mediators in vitro. Exp. Mol. Pathol. 76 3 (2004) 189-195
89. Welch M.P., Odland G.F., and Clark R.A. Temporal relationships of F-actin bundle formation, collagen and fibronectin matrix assembly, and fibronectin receptor expression to wound contraction. J. Cell Biol. 110 1 (1990) 133-145
90. Werner S., Smola H., Liao X., Longaker M.T., Krieg T., Hofschneider P.H., et al. The function of KGF in morphogenesis of epithelium and reepithelialization of wounds. Science 266 (1994) 819-822
91. Xu J., and Clark R.A. Extracellular matrix alters PDGF regulation of fibroblast integrins. J. Cell Biol. 132 1/2 (1996) 239-249
92. Yao P.M., Delclaux C., D'Ortho M.P., Maitre B., Harf A., and Lafuma C. Cell-matrix interactions modulate 92-kD gelatinase expression by human bronchial epithelial cells. Am. J. Respir. Cell Mol. Biol. 18 (1998) 812-822
93. Yong V.W. Metalloproteinases: mediators of pathology and regeneration in the CNS. Nat. Rev. Neurosci. 6 12 (2005) 931-944
94. Zhang K., McQuibban G.A., Silva C., Butler G.S., Johnston J.B., Holden J., et al. HIV-induced metalloproteinase processing of the chemokine stromal cell derived factor-1 causes neurodegeneration. Nat. Neurosci. 6 10 (2003) 1064-1071
95. Zhou M., Zhang Y., Ardans J.A., and Wahl L.M. Interferon-gamma differentially regulates monocyte matrix metalloproteinase-1 and -9 through tumor necrosis factor-alpha and caspase 8. J. Biol. Chem. 278 46 (2003) 45406-45413
96. Zlotnik A., Yoshie O., and Nomiyama H. The chemokine and chemokine receptor superfamilies and their molecular evolution. Genome Biol. 7 12 (2006) 243