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Volumn 27, Issue 3, 2008, Pages 137-175

Long-lasting tissue inflammatory processes trigger autoimmune responses to extracellular matrix molecules

Author keywords

Autoantibodies; Autoimmunity; Cryptic epitopes; Extracellular matrix; Inflammation

Indexed keywords

IMMUNOGLOBULIN A; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M; NITROGEN; PROTEINASE; REACTIVE OXYGEN METABOLITE; SCLEROPROTEIN;

EID: 42549095139     PISSN: 08830185     EISSN: 15635244     Source Type: Journal    
DOI: 10.1080/08830180801939280     Document Type: Review
Times cited : (17)

References (203)
  • 1
    • 0038575444 scopus 로고    scopus 로고
    • Functional structure and composition of extracellular matrix
    • F. Bosman and I. Stamenkovic, Functional structure and composition of extracellular matrix. J. Pathol., 200: 423-428, 2003.
    • (2003) J. Pathol , vol.200 , pp. 423-428
    • Bosman, F.1    Stamenkovic, I.2
  • 2
    • 33748967069 scopus 로고    scopus 로고
    • Of extracellular matrix, scaffolds, and signalling: Tissue architecture regulates development, homeostasis, and cancer
    • C.M. Nelson and M. J. Bissell, Of extracellular matrix, scaffolds, and signalling: tissue architecture regulates development, homeostasis, and cancer. Annu. Rev. Cell. Dev. Biol., 22: 287-309, 2006.
    • (2006) Annu. Rev. Cell. Dev. Biol , vol.22 , pp. 287-309
    • Nelson, C.M.1    Bissell, M.J.2
  • 3
    • 0030962323 scopus 로고    scopus 로고
    • Basement-membrane stromal relationships: Interactions between collagen fibrils and the lamina densa
    • E. Adachi, I. Hopkinson, and T. Hayashi, Basement-membrane stromal relationships: interactions between collagen fibrils and the lamina densa. Int. Rev. Cytol., 173: 73-156, 1997
    • (1997) Int. Rev. Cytol , vol.173 , pp. 73-156
    • Adachi, E.1    Hopkinson, I.2    Hayashi, T.3
  • 4
    • 0026542959 scopus 로고
    • Basement membrane proteins: Structure, assembly, and cellular interactions
    • M. Paulsson, Basement membrane proteins: structure, assembly, and cellular interactions. Crit. Rev. Biochem. Mol. Biol., 27: 93-127, 1992.
    • (1992) Crit. Rev. Biochem. Mol. Biol , vol.27 , pp. 93-127
    • Paulsson, M.1
  • 5
    • 0242710145 scopus 로고    scopus 로고
    • Collagens-structure, function, and biosynthesis
    • K. Gelse, E. Poschl, and T. Aigner, Collagens-structure, function, and biosynthesis. Adv. Drug. Deliv. Rev., 55: 1531-1546, 2003.
    • (2003) Adv. Drug. Deliv. Rev , vol.55 , pp. 1531-1546
    • Gelse, K.1    Poschl, E.2    Aigner, T.3
  • 6
    • 0025778486 scopus 로고
    • Mutations in collagen genes: Causes of rare and some common diseases in humans
    • H. Kuivaniemi, G. Tromp, and D. J. Prockop, Mutations in collagen genes: causes of rare and some common diseases in humans. FASEB J., 5: 2052-2060, 1991.
    • (1991) FASEB J , vol.5 , pp. 2052-2060
    • Kuivaniemi, H.1    Tromp, G.2    Prockop, D.J.3
  • 7
    • 0015187752 scopus 로고
    • The chemistry and structure of collagen
    • W. Traub and K. A. Piez, The chemistry and structure of collagen. Adv. Protein Chem., 25: 243-352, 1971.
    • (1971) Adv. Protein Chem , vol.25 , pp. 243-352
    • Traub, W.1    Piez, K.A.2
  • 8
    • 23444447845 scopus 로고    scopus 로고
    • The collagen superfamily: From the extracellular matrix to the cell membrane
    • S. Ricard-Blum and F. Ruggiero, The collagen superfamily: from the extracellular matrix to the cell membrane. Pathol. Biol. (Paris), 53: 430-442, 2005.
    • (2005) Pathol. Biol. (Paris) , vol.53 , pp. 430-442
    • Ricard-Blum, S.1    Ruggiero, F.2
  • 10
    • 0033037022 scopus 로고    scopus 로고
    • Connective tissues: Matrix composition and its relevance to physical therapy
    • E. M. Culav, C. H. Clark, and M. J. Merrilees, Connective tissues: matrix composition and its relevance to physical therapy. Phys. Ther., 79: 308-319, 1999.
    • (1999) Phys. Ther , vol.79 , pp. 308-319
    • Culav, E.M.1    Clark, C.H.2    Merrilees, M.J.3
  • 11
    • 33748318174 scopus 로고    scopus 로고
    • Approaching the proteoglycome: Molecular interactions of proteoglycans and their functional output
    • S. Cattaruzza and R. Perris, Approaching the proteoglycome: molecular interactions of proteoglycans and their functional output. Macromol. Biosci., 6: 667-680, 2006.
    • (2006) Macromol. Biosci , vol.6 , pp. 667-680
    • Cattaruzza, S.1    Perris, R.2
  • 12
    • 0036166823 scopus 로고    scopus 로고
    • Domain structure and organisation of extracellular matrix proteins
    • E. Hohenester and J. Engel, Domain structure and organisation of extracellular matrix proteins. Matrix Biol., 21: 115-128, 2002.
    • (2002) Matrix Biol , vol.21 , pp. 115-128
    • Hohenester, E.1    Engel, J.2
  • 13
    • 0027939832 scopus 로고
    • The role of extracellular matrix in postinflammatory wound healing and fibrosis
    • R. Raghow, The role of extracellular matrix in postinflammatory wound healing and fibrosis. FASEB J., 8: 823-831, 1994.
    • (1994) FASEB J , vol.8 , pp. 823-831
    • Raghow, R.1
  • 14
    • 22844451608 scopus 로고    scopus 로고
    • Meet the tenascins: Multifunctional and mysterious
    • H. C. Hsia and J. E. Schwarzbauer, Meet the tenascins: multifunctional and mysterious. J. Biol. Chem., 280: 26641-26644, 2005.
    • (2005) J. Biol. Chem , vol.280 , pp. 26641-26644
    • Hsia, H.C.1    Schwarzbauer, J.E.2
  • 15
    • 0037180812 scopus 로고    scopus 로고
    • Points of control in inflammation
    • C. Nathan, Points of control in inflammation. Nature, 420: 846-852, 2002.
    • (2002) Nature , vol.420 , pp. 846-852
    • Nathan, C.1
  • 17
    • 0043201100 scopus 로고    scopus 로고
    • Role of chemokines and chemokine receptors in regulating specific leukocyte trafficking in the immune/inflammatory response
    • A. Manzo, R. Caporali, C. Montecucco, and C. Pitzalis, Role of chemokines and chemokine receptors in regulating specific leukocyte trafficking in the immune/inflammatory response. Clin. Exp. Rheumatol., 21: 501-508, 2003.
    • (2003) Clin. Exp. Rheumatol , vol.21 , pp. 501-508
    • Manzo, A.1    Caporali, R.2    Montecucco, C.3    Pitzalis, C.4
  • 19
    • 2942602599 scopus 로고    scopus 로고
    • T-cell-mediated signalling in immune, inflammatory and angiogenic processes: The cascade of events leading to inflammatory diseases
    • C. Monaco, E. Andreakos, S. Kiriakidis, M. Feldmann, and E. Paleolog, T-cell-mediated signalling in immune, inflammatory and angiogenic processes: the cascade of events leading to inflammatory diseases. Curr. Drug Targets Inflamm. Allergy, 3: 35-42, 2004.
    • (2004) Curr. Drug Targets Inflamm. Allergy , vol.3 , pp. 35-42
    • Monaco, C.1    Andreakos, E.2    Kiriakidis, S.3    Feldmann, M.4    Paleolog, E.5
  • 20
    • 2342437653 scopus 로고    scopus 로고
    • Upregulation of reactive oxygen species generation and phagocytosis, and increased apoptosis in human neutrophils during severe sepsis and septic shock
    • P. S. Martins, E. G. Kallas, M. C. Neto, M. A. Dalboni, S. Blecher, and R. Salomão, Upregulation of reactive oxygen species generation and phagocytosis, and increased apoptosis in human neutrophils during severe sepsis and septic shock. Shock, 20: 208-212, 2003.
    • (2003) Shock , vol.20 , pp. 208-212
    • Martins, P.S.1    Kallas, E.G.2    Neto, M.C.3    Dalboni, M.A.4    Blecher, S.5    Salomão, R.6
  • 22
    • 0030773145 scopus 로고    scopus 로고
    • The interplay between primary and secondary cytokines. Cytokines involved in the regulation of monocyte recruitment
    • A. Mantovani, The interplay between primary and secondary cytokines. Cytokines involved in the regulation of monocyte recruitment. Drugs, 54 (Suppl 1): 15-23, 1997.
    • (1997) Drugs , vol.54 , Issue.SUPPL. 1 , pp. 15-23
    • Mantovani, A.1
  • 23
    • 0029071643 scopus 로고
    • Chemokines and tissue injury
    • M.B. Furie, and G. J. Randolph, Chemokines and tissue injury. Am. J. Pathol., 146: 1287-1301, 1995.
    • (1995) Am. J. Pathol , vol.146 , pp. 1287-1301
    • Furie, M.B.1    Randolph, G.J.2
  • 27
    • 34147190086 scopus 로고    scopus 로고
    • Chronic inflammation: A failure of resolution?
    • T. Lawrence, and D. W. Gilroy, Chronic inflammation: a failure of resolution? Int. J. Exp. Pathol., 88: 85-94, 2007.
    • (2007) Int. J. Exp. Pathol , vol.88 , pp. 85-94
    • Lawrence, T.1    Gilroy, D.W.2
  • 29
    • 1642521978 scopus 로고    scopus 로고
    • Remnant epitopes generate autoimmunity: From rheumatoid arthritis and multiple sclerosis to diabetes
    • F. J. Descamps, P. E. Van den Steen, I. Nelissen, J. Van Damme, and G. Opdenakker, Remnant epitopes generate autoimmunity: from rheumatoid arthritis and multiple sclerosis to diabetes. Adv. Exp. Med. Biol., 535: 69-77, 2003.
    • (2003) Adv. Exp. Med. Biol , vol.535 , pp. 69-77
    • Descamps, F.J.1    Van den Steen, P.E.2    Nelissen, I.3    Van Damme, J.4    Opdenakker, G.5
  • 30
    • 0036186977 scopus 로고    scopus 로고
    • Cleavage of denatured natural collagen type II by neutrophil gelatinase B reveals enzyme specificity, post-translational modifications in the substrate, and the formation of remnant epitopes in rheumatoid arthritis
    • P. E. Van den Steen, P. Proost, B. Grillet, D. D. Brand, A. H. Kang, J. Van Damme, and G. Opdenakker, Cleavage of denatured natural collagen type II by neutrophil gelatinase B reveals enzyme specificity, post-translational modifications in the substrate, and the formation of remnant epitopes in rheumatoid arthritis. FASEB J., 16: 379-389, 2002.
    • (2002) FASEB J , vol.16 , pp. 379-389
    • Van den Steen, P.E.1    Proost, P.2    Grillet, B.3    Brand, D.D.4    Kang, A.H.5    Van Damme, J.6    Opdenakker, G.7
  • 31
    • 33644838962 scopus 로고    scopus 로고
    • Gelatinase B participates in collagen II degradation and releases glycosylated remnant epitopes in rheumatoid arthritis
    • P. E. Van den Steen, B. Grillet, and G. Opdenakker, Gelatinase B participates in collagen II degradation and releases glycosylated remnant epitopes in rheumatoid arthritis. Adv. Exp. Med. Biol., 564: 45-55, 2005.
    • (2005) Adv. Exp. Med. Biol , vol.564 , pp. 45-55
    • Van den Steen, P.E.1    Grillet, B.2    Opdenakker, G.3
  • 32
    • 20644444567 scopus 로고    scopus 로고
    • Understanding crypticity is the key to revealing the pathogenesis of autoimmunity
    • K. D. Moudgil and E. E. Sercarz, Understanding crypticity is the key to revealing the pathogenesis of autoimmunity. Trends Immunol., 26: 355-359, 2005.
    • (2005) Trends Immunol , vol.26 , pp. 355-359
    • Moudgil, K.D.1    Sercarz, E.E.2
  • 33
    • 25844526684 scopus 로고    scopus 로고
    • Central tolerance: Learning self-control in the thymus
    • K. A. Hogquist, T. A. Baldwin, and S. C. Jameson, Central tolerance: learning self-control in the thymus. Nat. Rev. Immunol, 5: 772-782, 2005.
    • (2005) Nat. Rev. Immunol , vol.5 , pp. 772-782
    • Hogquist, K.A.1    Baldwin, T.A.2    Jameson, S.C.3
  • 34
    • 33745821247 scopus 로고    scopus 로고
    • T-cell avidity and tuning: The flexible connection between tolerance and autoimmunity
    • J. G. van den Boorn, I.C. Le Poole, and R. M. Luiten, T-cell avidity and tuning: the flexible connection between tolerance and autoimmunity. Int. Rev. Immunol., 25: 235-258, 2006.
    • (2006) Int. Rev. Immunol , vol.25 , pp. 235-258
    • van den Boorn, J.G.1    Le Poole, I.C.2    Luiten, R.M.3
  • 35
    • 22244459507 scopus 로고    scopus 로고
    • Neonatal autoimmune disease: Influence of CD4+ CD25+ regulatory T cells
    • Y. Y. Setiady, S. Agersborg, E. T. Samy, J. E. Lewis, and K. S. Tung, Neonatal autoimmune disease: influence of CD4+ CD25+ regulatory T cells. Int. Rev. Immunol., 24: 227-45, 2005.
    • (2005) Int. Rev. Immunol , vol.24 , pp. 227-245
    • Setiady, Y.Y.1    Agersborg, S.2    Samy, E.T.3    Lewis, J.E.4    Tung, K.S.5
  • 36
    • 0029444644 scopus 로고
    • Costimulation in tolerance and autoimmunity
    • S. Guerder and R. A. Flavell, Costimulation in tolerance and autoimmunity. Int. Rev. Immunol., 13: 135-146, 1995.
    • (1995) Int. Rev. Immunol , vol.13 , pp. 135-146
    • Guerder, S.1    Flavell, R.A.2
  • 37
    • 34548536750 scopus 로고    scopus 로고
    • B-cell self-tolerance in humans
    • H. Wardemann and M. C. Nussenzweig, B-cell self-tolerance in humans. Adv. Immunol., 95: 83-110, 2007.
    • (2007) Adv. Immunol , vol.95 , pp. 83-110
    • Wardemann, H.1    Nussenzweig, M.C.2
  • 38
    • 16244405272 scopus 로고    scopus 로고
    • T-cell tolerance and autoimmunity to systemic and tissue-restricted self-antigens
    • J. Lohr, B. Knoechel, V. Nagabhushanam, and A. K. Abbas, T-cell tolerance and autoimmunity to systemic and tissue-restricted self-antigens. Immunol. Rev., 204: 116-27, 2005.
    • (2005) Immunol. Rev , vol.204 , pp. 116-127
    • Lohr, J.1    Knoechel, B.2    Nagabhushanam, V.3    Abbas, A.K.4
  • 39
    • 0036481263 scopus 로고    scopus 로고
    • Epitope spreading in immune-mediated diseases: Implications for immunotherapy
    • C. L. Vanderlugt and S. D. Miller, Epitope spreading in immune-mediated diseases: implications for immunotherapy. Nat. Rev. Immunol., 2: 85-95, 2002.
    • (2002) Nat. Rev. Immunol , vol.2 , pp. 85-95
    • Vanderlugt, C.L.1    Miller, S.D.2
  • 40
    • 0026664422 scopus 로고
    • Spreading of T-cell autoimmunity to cryptic determinants of an autoantigen
    • P. V. Lehmann, T. Forsthuber, A. Miller, and E.E. Sercarz, Spreading of T-cell autoimmunity to cryptic determinants of an autoantigen. Nature, 358: 155-157, 1992.
    • (1992) Nature , vol.358 , pp. 155-157
    • Lehmann, P.V.1    Forsthuber, T.2    Miller, A.3    Sercarz, E.E.4
  • 42
    • 0030028043 scopus 로고    scopus 로고
    • Matrix metalloproteinases in immunity
    • E. J. Goetzl, M. J. Banda, and D. Leppert, Matrix metalloproteinases in immunity. J. Immunol., 156: 1-4, 1996.
    • (1996) J. Immunol , vol.156 , pp. 1-4
    • Goetzl, E.J.1    Banda, M.J.2    Leppert, D.3
  • 43
    • 0026701517 scopus 로고
    • Lymphocyte migration through extracellular matrix
    • S. Ratner, Lymphocyte migration through extracellular matrix. Invasion Metastasis, 12: 82-100, 1992.
    • (1992) Invasion Metastasis , vol.12 , pp. 82-100
    • Ratner, S.1
  • 44
    • 0033773240 scopus 로고    scopus 로고
    • Modulation of leukocyte behavior by an inflamed extracellular matrix
    • H. Schor, G. G. Vaday, and O. Lider, Modulation of leukocyte behavior by an inflamed extracellular matrix. Dev. Immunol., 7: 227-238, 2000.
    • (2000) Dev. Immunol , vol.7 , pp. 227-238
    • Schor, H.1    Vaday, G.G.2    Lider, O.3
  • 45
    • 0028625739 scopus 로고
    • The family of matrix metalloproteinases
    • J. F. Jr Woessner, The family of matrix metalloproteinases. Ann. N. Y. Acad. Sci., 732: 11-21, 1994.
    • (1994) Ann. N. Y. Acad. Sci , vol.732 , pp. 11-21
    • Woessner Jr, J.F.1
  • 46
    • 33646598361 scopus 로고    scopus 로고
    • Matrix metalloproteinases in development and disease
    • Part C
    • V. Lemaitre and J. D'Armiento, Matrix metalloproteinases in development and disease. Birth Defects Res. (Part C), 78: 1-10, 2006.
    • (2006) Birth Defects Res , vol.78 , pp. 1-10
    • Lemaitre, V.1    D'Armiento, J.2
  • 47
    • 0036516460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: A tail of a frog that became a prince
    • C. E. Brinckerhoff and L. M. Matrisian, Matrix metalloproteinases: a tail of a frog that became a prince. Nat. Rev. Mol. Cell. Biol., 3: 207-214, 2002.
    • (2002) Nat. Rev. Mol. Cell. Biol , vol.3 , pp. 207-214
    • Brinckerhoff, C.E.1    Matrisian, L.M.2
  • 48
    • 0033981473 scopus 로고    scopus 로고
    • The plasminogen activation system in tumor growth, invasion, and metastasis
    • P. A. Andreasen, R. Egelund, and H. H. Petersen, The plasminogen activation system in tumor growth, invasion, and metastasis. CMLS, Cell. Mol. Life Sci., 57: 25-40, 2000.
    • (2000) CMLS, Cell. Mol. Life Sci , vol.57 , pp. 25-40
    • Andreasen, P.A.1    Egelund, R.2    Petersen, H.H.3
  • 49
    • 36849018449 scopus 로고    scopus 로고
    • Activation and silencing of matrix metalloproteinases
    • X. Fu, W. C. Parks, and J. W. Heinecke, Activation and silencing of matrix metalloproteinases. Semin. Cell Dev. Biol., 19: 2-13, 2008.
    • (2008) Semin. Cell Dev. Biol , vol.19 , pp. 2-13
    • Fu, X.1    Parks, W.C.2    Heinecke, J.W.3
  • 50
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Structures, evolution, and diversification
    • I. Massova, L. P. Kotra, R. Fridman, and S. Mobashery, Matrix metalloproteinases: structures, evolution, and diversification. FASEB J., 12: 1075-1095, 1998.
    • (1998) FASEB J , vol.12 , pp. 1075-1095
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 51
    • 0035129903 scopus 로고    scopus 로고
    • a novel family of extracellular matrix proteases
    • ADAMTS
    • B. L. Tang, ADAMTS: a novel family of extracellular matrix proteases. Int. J. Biochem. Cell. Biol., 33: 33-44, 2001.
    • (2001) Int. J. Biochem. Cell. Biol , vol.33 , pp. 33-44
    • Tang, B.L.1
  • 52
    • 1842428713 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases in the lung: Role in protein processing and immunoregulation
    • F. Buhling, N. Waldburg, A. Reisenauer, A. Heimburg, H. Golpon, and T. Welte, Lysosomal cysteine proteases in the lung: role in protein processing and immunoregulation. Eur. Respir. J., 23: 620-628, 2004.
    • (2004) Eur. Respir. J , vol.23 , pp. 620-628
    • Buhling, F.1    Waldburg, N.2    Reisenauer, A.3    Heimburg, A.4    Golpon, H.5    Welte, T.6
  • 53
    • 0036077458 scopus 로고    scopus 로고
    • Cysteine peptidases of mammals: Their biological roles and potential effects in the oral cavity and other tissues in health and disease
    • D. P. Dickinson, Cysteine peptidases of mammals: their biological roles and potential effects in the oral cavity and other tissues in health and disease. Crit. Rev. Oral. Biol. Med., 13: 238-275, 2002.
    • (2002) Crit. Rev. Oral. Biol. Med , vol.13 , pp. 238-275
    • Dickinson, D.P.1
  • 54
    • 1842479065 scopus 로고    scopus 로고
    • A cut above the rest? MMP-8 and liver fibrosis gene therapy
    • J. P. Iredale, A cut above the rest? MMP-8 and liver fibrosis gene therapy. Gastroenterology, 126: 1199-1201, 2004.
    • (2004) Gastroenterology , vol.126 , pp. 1199-1201
    • Iredale, J.P.1
  • 55
    • 32944465075 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Role in arthritis
    • P. S. Burrage, K. S. Mix, and C. E. Brinckerhoff, Matrix metalloproteinases: role in arthritis. Front. Biosci., 11: 529-543, 2006.
    • (2006) Front. Biosci , vol.11 , pp. 529-543
    • Burrage, P.S.1    Mix, K.S.2    Brinckerhoff, C.E.3
  • 56
    • 0033146096 scopus 로고    scopus 로고
    • Matrix metalloproteinases. Matrix degradation and more
    • S. D. Shapiro and R. M. Senior, Matrix metalloproteinases. Matrix degradation and more. Am. J. Respir. Cell. Mol. Biol., 20: 1100-1102, 1999.
    • (1999) Am. J. Respir. Cell. Mol. Biol , vol.20 , pp. 1100-1102
    • Shapiro, S.D.1    Senior, R.M.2
  • 57
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles for cysteine proteases in human biology
    • H. A. Chapman, R. J. Riese, and G. P. Shi, Emerging roles for cysteine proteases in human biology. Annu. Rev, Physiol., 59: 63-88, 1997.
    • (1997) Annu. Rev, Physiol , vol.59 , pp. 63-88
    • Chapman, H.A.1    Riese, R.J.2    Shi, G.P.3
  • 58
    • 33744771928 scopus 로고    scopus 로고
    • The regulation of cathepsin K gene expression
    • B. R. Troen, The regulation of cathepsin K gene expression. Ann. N. Y. Acad. Sci., 1068: 165-172, 2006.
    • (2006) Ann. N. Y. Acad. Sci , vol.1068 , pp. 165-172
    • Troen, B.R.1
  • 59
    • 0026545368 scopus 로고
    • The macrophage capacity for phagocytosis
    • G. J. Cannon and J. A. Swanson, The macrophage capacity for phagocytosis. J. Cell. Sci., 101: 907-913, 1992.
    • (1992) J. Cell. Sci , vol.101 , pp. 907-913
    • Cannon, G.J.1    Swanson, J.A.2
  • 60
    • 0012330613 scopus 로고    scopus 로고
    • Importance of lysosomal cysteine proteases in lung disease
    • P. J. Wolters and H. A. Chapman, Importance of lysosomal cysteine proteases in lung disease. Respir. Res., 1: 170-177, 2000.
    • (2000) Respir. Res , vol.1 , pp. 170-177
    • Wolters, P.J.1    Chapman, H.A.2
  • 62
    • 0036754586 scopus 로고    scopus 로고
    • Degradation of extracellular matrix protein tenascin-C by cathepsin B: An interaction involved in the progression of gliomas
    • J. Mai, M. Sameni, T. Mikkelsen, and B. F. Sloane, Degradation of extracellular matrix protein tenascin-C by cathepsin B: an interaction involved in the progression of gliomas. Biol. Chem., 383: 1407-1413, 2002.
    • (2002) Biol. Chem , vol.383 , pp. 1407-1413
    • Mai, J.1    Sameni, M.2    Mikkelsen, T.3    Sloane, B.F.4
  • 63
    • 0026575258 scopus 로고
    • Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumour tissues
    • M. R. Buck, D. G. Karustis, N. A. Day, K. V. Honn, and B. F. Sloane, Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumour tissues. Biochem. J., 282: 273-278, 1992.
    • (1992) Biochem. J , vol.282 , pp. 273-278
    • Buck, M.R.1    Karustis, D.G.2    Day, N.A.3    Honn, K.V.4    Sloane, B.F.5
  • 64
    • 33847324029 scopus 로고    scopus 로고
    • Critical role of dipeptidyl peptidase I in neutrophil recruitment during the development of experimental abdominal aortic aneurysms
    • M. B. Pagano, M. A. Bartoli, T. L. Ennis, D. Mao, P. M. Simmons, R. W. Thompson, and C. T. Pham, Critical role of dipeptidyl peptidase I in neutrophil recruitment during the development of experimental abdominal aortic aneurysms. Proc. Natl. Acad. Sci. U.S.A, 104: 2855-2860, 2007.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 2855-2860
    • Pagano, M.B.1    Bartoli, M.A.2    Ennis, T.L.3    Mao, D.4    Simmons, P.M.5    Thompson, R.W.6    Pham, C.T.7
  • 65
    • 0017644625 scopus 로고
    • Further studies on the activation of procollagenase, the latent precursor of bone collagenase. Effects of lysosomal cathepsin B, plasmin and kallikrein, and spontaneous activation
    • Y. Eeckhout and G. Vaes, Further studies on the activation of procollagenase, the latent precursor of bone collagenase. Effects of lysosomal cathepsin B, plasmin and kallikrein, and spontaneous activation. Biochem. J., 166: 21-31, 1977.
    • (1977) Biochem. J , vol.166 , pp. 21-31
    • Eeckhout, Y.1    Vaes, G.2
  • 66
    • 0036398446 scopus 로고    scopus 로고
    • The IL-1 family and inflammatory diseases
    • C. A. Dinarello, The IL-1 family and inflammatory diseases. Clin. Exp. Rheumatol., 20(5 Suppl 27): S1-13, 2002.
    • (2002) Clin. Exp. Rheumatol , vol.20 , Issue.5 SUPPL. 27
    • Dinarello, C.A.1
  • 67
    • 0345547431 scopus 로고    scopus 로고
    • Regulation of the expression of inducible nitric oxide synthase
    • H. Kleinert, P. M. Schwarz, and U. Förstermann, Regulation of the expression of inducible nitric oxide synthase. Biol. Chem., 384: 1343-1364, 2003.
    • (2003) Biol. Chem , vol.384 , pp. 1343-1364
    • Kleinert, H.1    Schwarz, P.M.2    Förstermann, U.3
  • 68
    • 0036751127 scopus 로고    scopus 로고
    • Physiological mechanisms regulating the expression of endothelial-type NO synthase
    • H. Li, T. Wallerath, and U. Förstermann, Physiological mechanisms regulating the expression of endothelial-type NO synthase. Nitric Oxide, 7: 132-147, 2002.
    • (2002) Nitric Oxide , vol.7 , pp. 132-147
    • Li, H.1    Wallerath, T.2    Förstermann, U.3
  • 69
    • 0028335587 scopus 로고
    • Peroxynitrite-mediated oxidation of albumin to the protein-thiyl free radical
    • R. M. Gatti, R. Radi, and O. Augusto, Peroxynitrite-mediated oxidation of albumin to the protein-thiyl free radical. FEBS Lett., 348: 287-290, 1994.
    • (1994) FEBS Lett , vol.348 , pp. 287-290
    • Gatti, R.M.1    Radi, R.2    Augusto, O.3
  • 70
    • 33746018989 scopus 로고    scopus 로고
    • Free radical theory of autoimmunity
    • S. Kannan, Free radical theory of autoimmunity. Theor. Biol. Med. Model, 3: 22-36, 2006.
    • (2006) Theor. Biol. Med. Model , vol.3 , pp. 22-36
    • Kannan, S.1
  • 72
    • 33947511182 scopus 로고    scopus 로고
    • Endogenous production of reactive oxygen species is required for stimulation of human articular chondrocyte matrix metalloproteinase production by fibronectin fragments
    • M. Del Carlo, D. Schwartz, E. A. Erickson, and R. F. Loeser, Endogenous production of reactive oxygen species is required for stimulation of human articular chondrocyte matrix metalloproteinase production by fibronectin fragments. Free Radic. Biol. Med., 42: 1350-1358, 2007.
    • (2007) Free Radic. Biol. Med , vol.42 , pp. 1350-1358
    • Del Carlo, M.1    Schwartz, D.2    Erickson, E.A.3    Loeser, R.F.4
  • 73
    • 26844522332 scopus 로고    scopus 로고
    • Oxidative stress augments the production of matrix metalloproteinase-1, cyclooxygenase-2, and prostaglandin E2 through enhancement of NF-kappa B activity in lipopolysaccharide-activated human primary monocytes
    • Y. Lu and L. M. Wahl, Oxidative stress augments the production of matrix metalloproteinase-1, cyclooxygenase-2, and prostaglandin E2 through enhancement of NF-kappa B activity in lipopolysaccharide-activated human primary monocytes. J. Immunol., 175: 5423-5429, 2005.
    • (2005) J. Immunol , vol.175 , pp. 5423-5429
    • Lu, Y.1    Wahl, L.M.2
  • 74
    • 4043161974 scopus 로고    scopus 로고
    • Mitochondrial redox control of matrix metalloproteinases
    • K. K. Nelson and J. A. Melendez, Mitochondrial redox control of matrix metalloproteinases. Free Radic. Biol. Med., 37: 768-784, 2004.
    • (2004) Free Radic. Biol. Med , vol.37 , pp. 768-784
    • Nelson, K.K.1    Melendez, J.A.2
  • 76
    • 0030614809 scopus 로고    scopus 로고
    • Hydrogen peroxide (H2O2) increases the steady-state mRNA levels of collagenase/MMP-1 in human dermal fibroblasts
    • P. Brenneisen, K. Briviba, M. Wlaschek, J. Wenk, and K. Scharffetter-Kochanek, Hydrogen peroxide (H2O2) increases the steady-state mRNA levels of collagenase/MMP-1 in human dermal fibroblasts. Free Radic. Biol. Med., 22: 515-524, 1997.
    • (1997) Free Radic. Biol. Med , vol.22 , pp. 515-524
    • Brenneisen, P.1    Briviba, K.2    Wlaschek, M.3    Wenk, J.4    Scharffetter-Kochanek, K.5
  • 77
    • 0025106479 scopus 로고
    • Activation of latent human neutrophil collagenase by reactive oxygen species and serine proteases
    • H. Saari, K. Suomalainen, O. Lindy, Y. T. Konttinen, and T. Sorsa, Activation of latent human neutrophil collagenase by reactive oxygen species and serine proteases. Biochem. Biophys. Res. Commun., 171: 979-987, 1990.
    • (1990) Biochem. Biophys. Res. Commun , vol.171 , pp. 979-987
    • Saari, H.1    Suomalainen, K.2    Lindy, O.3    Konttinen, Y.T.4    Sorsa, T.5
  • 79
    • 33644995821 scopus 로고    scopus 로고
    • Mechanism of nitrite oxidation by eosinophil peroxidase: Implications for oxidant production and nitration by eosinophils
    • C. J. van Dalen, C. C. Winterbourn, and A. J. Kettle, Mechanism of nitrite oxidation by eosinophil peroxidase: implications for oxidant production and nitration by eosinophils. Biochem. J., 394: 707-713, 2006.
    • (2006) Biochem. J , vol.394 , pp. 707-713
    • van Dalen, C.J.1    Winterbourn, C.C.2    Kettle, A.J.3
  • 80
    • 0035890333 scopus 로고    scopus 로고
    • Hypochlorite- and hypobromite-mediated radical formation and its role in cell lysis
    • C. L. Hawkins, B. E. Brown, and M. J. Davies, Hypochlorite- and hypobromite-mediated radical formation and its role in cell lysis. Arch. Biochem. Biophys., 395: 137-145, 2001.
    • (2001) Arch. Biochem. Biophys , vol.395 , pp. 137-145
    • Hawkins, C.L.1    Brown, B.E.2    Davies, M.J.3
  • 81
    • 33846531190 scopus 로고    scopus 로고
    • Degradation of extracellular matrix and its components by hypobromous acid
    • M. D. Rees, T. N. McNiven, and M. J. Davies, Degradation of extracellular matrix and its components by hypobromous acid. Biochem. J., 401: 587-596, 2007.
    • (2007) Biochem. J , vol.401 , pp. 587-596
    • Rees, M.D.1    McNiven, T.N.2    Davies, M.J.3
  • 82
    • 3142736372 scopus 로고    scopus 로고
    • Hypochlorite and superoxide radicals can act synergistically to induce fragmentation of hyaluronan and chondroitin sulphates
    • M. D. Rees, C. L. Hawkins, and M. J. Davies, Hypochlorite and superoxide radicals can act synergistically to induce fragmentation of hyaluronan and chondroitin sulphates. Biochem. J., 381: 175-184, 2004.
    • (2004) Biochem. J , vol.381 , pp. 175-184
    • Rees, M.D.1    Hawkins, C.L.2    Davies, M.J.3
  • 83
    • 33947246924 scopus 로고    scopus 로고
    • Degradation of matrix glycosaminoglycans by peroxynitrite/peroxynitrous acid: Evidence for a hydroxyl-radical-like mechanism
    • E. C. Kennett and M. J. Davies, Degradation of matrix glycosaminoglycans by peroxynitrite/peroxynitrous acid: evidence for a hydroxyl-radical-like mechanism. Free Radic. Biol. Med., 42: 1278-1289, 2007.
    • (2007) Free Radic. Biol. Med , vol.42 , pp. 1278-1289
    • Kennett, E.C.1    Davies, M.J.2
  • 84
    • 0024949751 scopus 로고
    • Non-proteolytic activation of latent human neutrophil collagenase and its role in matrix destruction in periodontal diseases
    • T. Sorsa, H. Saari, Y.T. Konttinen, K. Suomalainen, S. Lindy, and V.J. Uitto, Non-proteolytic activation of latent human neutrophil collagenase and its role in matrix destruction in periodontal diseases. Int. J. Tissue. React., 11: 153-159, 1989.
    • (1989) Int. J. Tissue. React , vol.11 , pp. 153-159
    • Sorsa, T.1    Saari, H.2    Konttinen, Y.T.3    Suomalainen, K.4    Lindy, S.5    Uitto, V.J.6
  • 85
    • 34948897918 scopus 로고    scopus 로고
    • Oxidative damage pathways in relation to normal tissue injury
    • W. Zhao, D. I. Diz, and M. E. Robbins, Oxidative damage pathways in relation to normal tissue injury. Br. J. Radiol., 80(Spec No 1): S23-31, 2007.
    • (2007) Br. J. Radiol , vol.80 , Issue.SPEC 1
    • Zhao, W.1    Diz, D.I.2    Robbins, M.E.3
  • 87
    • 0033869778 scopus 로고    scopus 로고
    • Pathogenesis of liver fibrosis: Role of oxidative stress
    • G. Poli, Pathogenesis of liver fibrosis: role of oxidative stress. Mol. Aspects Med., 21: 49-98, 2000.
    • (2000) Mol. Aspects Med , vol.21 , pp. 49-98
    • Poli, G.1
  • 88
    • 0029859861 scopus 로고    scopus 로고
    • Oxidative damage and fibrogenesis
    • G. Poli and M. Parola, Oxidative damage and fibrogenesis. Free Radic. Biol. Med., 22: 287-305, 1997.
    • (1997) Free Radic. Biol. Med , vol.22 , pp. 287-305
    • Poli, G.1    Parola, M.2
  • 89
    • 0029729982 scopus 로고    scopus 로고
    • Molecular variants of fibronectin and laminin: Structure, physiological occurrence and histopathological aspects
    • H. Kosmehl, A. Berndt, and D. Katenkamp, Molecular variants of fibronectin and laminin: structure, physiological occurrence and histopathological aspects. Virchows Arch., 429: 311-322, 1996.
    • (1996) Virchows Arch , vol.429 , pp. 311-322
    • Kosmehl, H.1    Berndt, A.2    Katenkamp, D.3
  • 91
    • 0038771156 scopus 로고    scopus 로고
    • Tales from the crypt[ic] sites of the extracellular matrix
    • S. Schenk and V. Quaranta, Tales from the crypt[ic] sites of the extracellular matrix. Trends Cell. Biol., 13: 366-375, 2003.
    • (2003) Trends Cell. Biol , vol.13 , pp. 366-375
    • Schenk, S.1    Quaranta, V.2
  • 92
    • 0028147777 scopus 로고
    • Fibrogenic cytokines and connective tissue production
    • E. J. Kovacs and L. A. DiPietro, Fibrogenic cytokines and connective tissue production. FASEB J., 8: 854-861, 1994.
    • (1994) FASEB J , vol.8 , pp. 854-861
    • Kovacs, E.J.1    DiPietro, L.A.2
  • 93
    • 0031431637 scopus 로고    scopus 로고
    • Cryptic T-cell epitopes and their role in the pathogenesis of autoimmune diseases
    • M. G. Warnock and J. A. Goodacre, Cryptic T-cell epitopes and their role in the pathogenesis of autoimmune diseases. Br. J. Rheumatol., 36: 1144-1150, 1997.
    • (1997) Br. J. Rheumatol , vol.36 , pp. 1144-1150
    • Warnock, M.G.1    Goodacre, J.A.2
  • 94
    • 0029006389 scopus 로고
    • How can cryptic epitopes trigger autoimmunity?
    • A. Lanzavecchia, How can cryptic epitopes trigger autoimmunity? J. Exp. Med., 181: 1945-1948, 1995.
    • (1995) J. Exp. Med , vol.181 , pp. 1945-1948
    • Lanzavecchia, A.1
  • 95
    • 0031106106 scopus 로고    scopus 로고
    • Antigen processing by proteasomes: Insights into themolecular basis of crypticity
    • H. Djaballah, Antigen processing by proteasomes: insights into themolecular basis of crypticity. Mol. Biol. Rep., 24: 63-67, 1997.
    • (1997) Mol. Biol. Rep , vol.24 , pp. 63-67
    • Djaballah, H.1
  • 96
    • 0033847622 scopus 로고    scopus 로고
    • Regulation of tissue injury responses by the exposure of matricryptic sites within extracellular matrix molecules
    • G. E. Davis, K. J. Bayless, M. J. Davis, and G. A. Meininger, Regulation of tissue injury responses by the exposure of matricryptic sites within extracellular matrix molecules. Am. J. Pathol., 156: 1489-1498, 2000.
    • (2000) Am. J. Pathol , vol.156 , pp. 1489-1498
    • Davis, G.E.1    Bayless, K.J.2    Davis, M.J.3    Meininger, G.A.4
  • 97
  • 98
    • 0035802109 scopus 로고    scopus 로고
    • Proteolytic exposure of a cryptic site within collagen type IV is required for angiogenesis and tumor growth in vivo
    • J. Xu, D. Rodriguez, E. Petitclerc, J. J. Kim, M. Hangai, Y. S. Moon, G. E. Davis, and P. C. Brooks, Proteolytic exposure of a cryptic site within collagen type IV is required for angiogenesis and tumor growth in vivo. J. Cell Biol., 154: 1069-1079, 2001.
    • (2001) J. Cell Biol , vol.154 , pp. 1069-1079
    • Xu, J.1    Rodriguez, D.2    Petitclerc, E.3    Kim, J.J.4    Hangai, M.5    Moon, Y.S.6    Davis, G.E.7    Brooks, P.C.8
  • 99
    • 3142655415 scopus 로고    scopus 로고
    • Localization of a cryptic binding site for tenascin on fibronectin
    • K. C. Ingham, S. A. Brew, and H. P. Erickson, Localization of a cryptic binding site for tenascin on fibronectin. J. Biol. Chem., 279: 28132-28135, 2004.
    • (2004) J. Biol. Chem , vol.279 , pp. 28132-28135
    • Ingham, K.C.1    Brew, S.A.2    Erickson, H.P.3
  • 100
    • 0037134487 scopus 로고    scopus 로고
    • Exposure of cryptic domains in the alpha 1-chain of laminin-1 by elastase stimulates macrophages urokinase and matrix metalloproteinase-9 expression
    • K. M. Faisal Khan, G. W. Laurie, T. A. McCaffrey, and D. J. Falcone, Exposure of cryptic domains in the alpha 1-chain of laminin-1 by elastase stimulates macrophages urokinase and matrix metalloproteinase-9 expression. J. Biol. Chem., 277: 13778-13786, 2002.
    • (2002) J. Biol. Chem , vol.277 , pp. 13778-13786
    • Faisal Khan, K.M.1    Laurie, G.W.2    McCaffrey, T.A.3    Falcone, D.J.4
  • 101
    • 0029090299 scopus 로고
    • Release of biological activities from quiescent fibronectin by a conformational change and limited proteolysis by matrix metalloproteinases
    • F. Fukai, M. Ohtaki, N. Fujii, H. Yajima, T. Ishii, Y. Nishizawa, K. Miyazaki, and T. Katayama, Release of biological activities from quiescent fibronectin by a conformational change and limited proteolysis by matrix metalloproteinases. Biochemistry, 34: 11453-11459, 1995.
    • (1995) Biochemistry , vol.34 , pp. 11453-11459
    • Fukai, F.1    Ohtaki, M.2    Fujii, N.3    Yajima, H.4    Ishii, T.5    Nishizawa, Y.6    Miyazaki, K.7    Katayama, T.8
  • 102
    • 29144482654 scopus 로고    scopus 로고
    • Generation of neoantigenic epitopes after posttranslational modification of type II collagen by factors present within the inflamed joint
    • A. Nissim, P.G. Winyard, V. Corrigall, R. Fatah, D. Perrett, G. Panayi, and Y. Chernajovsky, Generation of neoantigenic epitopes after posttranslational modification of type II collagen by factors present within the inflamed joint. Arthritis Rheum., 52: 3829-3838, 2005.
    • (2005) Arthritis Rheum , vol.52 , pp. 3829-3838
    • Nissim, A.1    Winyard, P.G.2    Corrigall, V.3    Fatah, R.4    Perrett, D.5    Panayi, G.6    Chernajovsky, Y.7
  • 104
    • 18844386764 scopus 로고    scopus 로고
    • Humoral immune response to citrullinated collagen type II determinants in early rheumatoid arthritis
    • H. Burkhardt, B. Sehnert, R. Bockermann, A. Engström, J. R. Kalden, and R. Holmdahl, Humoral immune response to citrullinated collagen type II determinants in early rheumatoid arthritis. Eur. J. Immunol., 35: 1643-1652, 2005.
    • (2005) Eur. J. Immunol , vol.35 , pp. 1643-1652
    • Burkhardt, H.1    Sehnert, B.2    Bockermann, R.3    Engström, A.4    Kalden, J.R.5    Holmdahl, R.6
  • 107
    • 4444304939 scopus 로고    scopus 로고
    • Regulation of matrix biology by matrix metalloproteinases
    • J. D. Mott and Z. Werb, Regulation of matrix biology by matrix metalloproteinases. Curr. Opin. Cell Biol., 16: 558-564, 2004.
    • (2004) Curr. Opin. Cell Biol , vol.16 , pp. 558-564
    • Mott, J.D.1    Werb, Z.2
  • 108
    • 0031006421 scopus 로고    scopus 로고
    • Cytokines and the hepatic acute phase response
    • H. Moshage, Cytokines and the hepatic acute phase response. J. Pathol., 18: 257-266, 1997.
    • (1997) J. Pathol , vol.18 , pp. 257-266
    • Moshage, H.1
  • 109
    • 1442301501 scopus 로고    scopus 로고
    • V. Leroy, F. Monier, S. Bottari, C. Trocme, N. Sturm, M. N. Hilleret, F. Morel, and J. P. Zarski, Circulating matrix metalloproteinases 1, 2, 9 and their inhibitors TIMP-1 and TIMP-2 as serum markers of liver fibrosis in patients with chronic hepatitis C: comparison with PIIINP and hyaluronic acid. Am. J. Gastroenterol., 99: 271-279, 2004.
    • V. Leroy, F. Monier, S. Bottari, C. Trocme, N. Sturm, M. N. Hilleret, F. Morel, and J. P. Zarski, Circulating matrix metalloproteinases 1, 2, 9 and their inhibitors TIMP-1 and TIMP-2 as serum markers of liver fibrosis in patients with chronic hepatitis C: comparison with PIIINP and hyaluronic acid. Am. J. Gastroenterol., 99: 271-279, 2004.
  • 111
    • 33847363203 scopus 로고    scopus 로고
    • Model of liver fibrosis: Exploring the dynamic nature of inflammation and repair in a solid organ
    • J. P. Iredale, Model of liver fibrosis: exploring the dynamic nature of inflammation and repair in a solid organ. J. Clin. Invest., 117: 539-548, 2007.
    • (2007) J. Clin. Invest , vol.117 , pp. 539-548
    • Iredale, J.P.1
  • 112
    • 3843109060 scopus 로고    scopus 로고
    • Chronic autoimmune thyroiditis and rheumatic manifestations
    • L. Punzi and C. Betterle, Chronic autoimmune thyroiditis and rheumatic manifestations. Joint Bone Spine. 71: 275-283, 2004.
    • (2004) Joint Bone Spine , vol.71 , pp. 275-283
    • Punzi, L.1    Betterle, C.2
  • 113
    • 0029896946 scopus 로고    scopus 로고
    • Chronic autoimmune thyroiditis
    • C. M. Dayan and G. H. Daniels, Chronic autoimmune thyroiditis. New Engl. J. Med., 335: 99-105. 1996.
    • (1996) New Engl. J. Med , vol.335 , pp. 99-105
    • Dayan, C.M.1    Daniels, G.H.2
  • 114
    • 0036884263 scopus 로고    scopus 로고
    • Inhibition of TGFbeta1 by anti-TGFbeta1 antibody or lisinopril reduces thyroid fibrosis in granulomatous experimental autoimmune thyroiditis
    • K. Chen, Y. Wei, G. C. Sharp, and H. Braley-Mullen, Inhibition of TGFbeta1 by anti-TGFbeta1 antibody or lisinopril reduces thyroid fibrosis in granulomatous experimental autoimmune thyroiditis. J. Immunol., 169: 6530-6538, 2002.
    • (2002) J. Immunol , vol.169 , pp. 6530-6538
    • Chen, K.1    Wei, Y.2    Sharp, G.C.3    Braley-Mullen, H.4
  • 115
    • 39649098520 scopus 로고    scopus 로고
    • Recent advances on pathogenesis and therapies in systemic sclerosis
    • N. Yazawa, M. Fujimoto, and K. Tamaki, Recent advances on pathogenesis and therapies in systemic sclerosis. Clin. Rev. Allergy Immunol. 33: 107-112, 2007.
    • (2007) Clin. Rev. Allergy Immunol , vol.33 , pp. 107-112
    • Yazawa, N.1    Fujimoto, M.2    Tamaki, K.3
  • 116
    • 0028876751 scopus 로고
    • Modulation of collagen gene expression: Its relation to fibrosis in systemic sclerosis and other disorders
    • J. Varga and S. A. Jimenez, Modulation of collagen gene expression: its relation to fibrosis in systemic sclerosis and other disorders. Annals Int. Med., 122: 60-62, 1995.
    • (1995) Annals Int. Med , vol.122 , pp. 60-62
    • Varga, J.1    Jimenez, S.A.2
  • 117
    • 28444477739 scopus 로고    scopus 로고
    • Scleroderma: From cell and molecular mechanisms to disease models
    • D. J. Abraham and J. Varga, Scleroderma: from cell and molecular mechanisms to disease models. Trends Immunol., 26: 587-595, 2005.
    • (2005) Trends Immunol , vol.26 , pp. 587-595
    • Abraham, D.J.1    Varga, J.2
  • 118
    • 33747626518 scopus 로고    scopus 로고
    • Role of matrix metalloproteinases in intestinal inflammation
    • C. Medina and M. W. Radomski, Role of matrix metalloproteinases in intestinal inflammation. J. Pharmacol. Exp. Ther. 318: 933-938, 2006.
    • (2006) J. Pharmacol. Exp. Ther , vol.318 , pp. 933-938
    • Medina, C.1    Radomski, M.W.2
  • 119
    • 24044432964 scopus 로고    scopus 로고
    • Role of matrix metalloproteinases in inflammatory bowel disease
    • Y. Naito and T. Yoshikawa, Role of matrix metalloproteinases in inflammatory bowel disease. Mol. Aspects Med., 26: 379-390, 2005.
    • (2005) Mol. Aspects Med , vol.26 , pp. 379-390
    • Naito, Y.1    Yoshikawa, T.2
  • 120
    • 0033933804 scopus 로고    scopus 로고
    • Differential expression of matrix metalloproteinases and their tissue inhibitors in colon mucosa of patients with inflammatory bowel disease
    • B. von Lampe, B. Barthel, S. E. Coupland, E. O. Riecken, and S. Rosewicz, Differential expression of matrix metalloproteinases and their tissue inhibitors in colon mucosa of patients with inflammatory bowel disease. Gut, 47: 63-73, 2000.
    • (2000) Gut , vol.47 , pp. 63-73
    • von Lampe, B.1    Barthel, B.2    Coupland, S.E.3    Riecken, E.O.4    Rosewicz, S.5
  • 121
    • 33748710916 scopus 로고    scopus 로고
    • K. Menzel, M. Hausmann, E. Obermeier, K. Schreiter, N. Dunger, F. Bataille, W. Falk, J. Scholmerich, H. Herfarth, and G. Rogler, Cathepsins B, L and D in inflammatory bowel disease macrophages and potential therapeutic effects of cathepsin inhibition in vivo. Clin. Exp. Immunol., 146: 169-180, 2006.
    • K. Menzel, M. Hausmann, E. Obermeier, K. Schreiter, N. Dunger, F. Bataille, W. Falk, J. Scholmerich, H. Herfarth, and G. Rogler, Cathepsins B, L and D in inflammatory bowel disease macrophages and potential therapeutic effects of cathepsin inhibition in vivo. Clin. Exp. Immunol., 146: 169-180, 2006.
  • 122
    • 14944377055 scopus 로고    scopus 로고
    • Reduced expression of collagen type I and increased expression of matrix metalloproteinases 1 in patients with Crohn's disease
    • M. Stumpf, W. Cao, U. Klinge, B. Klosterhalfen, K. Junge, C. J. Krones, and V. Schumpelick, Reduced expression of collagen type I and increased expression of matrix metalloproteinases 1 in patients with Crohn's disease. J. Invest. Surg., 18: 33-38, 2005.
    • (2005) J. Invest. Surg , vol.18 , pp. 33-38
    • Stumpf, M.1    Cao, W.2    Klinge, U.3    Klosterhalfen, B.4    Junge, K.5    Krones, C.J.6    Schumpelick, V.7
  • 123
    • 0041885455 scopus 로고    scopus 로고
    • Interleukin 1beta induces gastric epithelial cellmatrixmetalloproteinase secretion and activation during Helicobacter pylori infection
    • M. Gööz, M. Shaker, P. Gööz, and A. J. Smolka, Interleukin 1beta induces gastric epithelial cellmatrixmetalloproteinase secretion and activation during Helicobacter pylori infection. Gut, 52: 1250-1256, 2003.
    • (2003) Gut , vol.52 , pp. 1250-1256
    • Gööz, M.1    Shaker, M.2    Gööz, P.3    Smolka, A.J.4
  • 126
    • 28444463303 scopus 로고    scopus 로고
    • Inflammatory mediators in chronic obstructive pulmonary disease
    • K. F. Chung. Inflammatory mediators in chronic obstructive pulmonary disease. Curr. Drug. Targets Inflamm. Allergy, 4: 619-625, 2005.
    • (2005) Curr. Drug. Targets Inflamm. Allergy , vol.4 , pp. 619-625
    • Chung, K.F.1
  • 127
    • 33749992653 scopus 로고    scopus 로고
    • The missing link: Chemokine receptors and tissue matrix breakdown in COPD
    • J. J. Smit and N. W. Lukacs, The missing link: chemokine receptors and tissue matrix breakdown in COPD. Trends Pharmacol., 27: 555-557, 2006.
    • (2006) Trends Pharmacol , vol.27 , pp. 555-557
    • Smit, J.J.1    Lukacs, N.W.2
  • 128
    • 0027176277 scopus 로고
    • Cathepsin L activity is increased in alveolar macrophages and bronchoalveolar lavage fluid of smokers
    • H. Takahashi, K. Ishidoh, D. Muno, A. Ohwada, T. Nukiwa, E. Kominami, and S. Kira, Cathepsin L activity is increased in alveolar macrophages and bronchoalveolar lavage fluid of smokers. Am. Rev. Respir. Dis., 147: 1562-1568, 1993.
    • (1993) Am. Rev. Respir. Dis , vol.147 , pp. 1562-1568
    • Takahashi, H.1    Ishidoh, K.2    Muno, D.3    Ohwada, A.4    Nukiwa, T.5    Kominami, E.6    Kira, S.7
  • 129
    • 0031280307 scopus 로고    scopus 로고
    • Increased release of matrix metalloproteinase-9 in bronchoalveolar lavage fluid and by alveolar macrophages of asthmatics
    • G. Mautino, N. Oliver, P. Chanez, J. Bousquet, and F. Capony, Increased release of matrix metalloproteinase-9 in bronchoalveolar lavage fluid and by alveolar macrophages of asthmatics, Am. J. Respir. Cell Mol. Biol., 17: 583-591, 1997.
    • (1997) Am. J. Respir. Cell Mol. Biol , vol.17 , pp. 583-591
    • Mautino, G.1    Oliver, N.2    Chanez, P.3    Bousquet, J.4    Capony, F.5
  • 130
    • 0000692136 scopus 로고    scopus 로고
    • Serum matrix metalloproteinase-9: Tissue inhibitor of metalloproteinase-1 ratio correlates with steroid responsiveness in moderate to severe asthma
    • M. Bosse, J. Chakir, M. Rouabhia, L. P. Boulet, M. Audette, and M. Laviolette, Serum matrix metalloproteinase-9: tissue inhibitor of metalloproteinase-1 ratio correlates with steroid responsiveness in moderate to severe asthma. Am. J. Respir. Crit. Care Med., 159: 596-602, 1999.
    • (1999) Am. J. Respir. Crit. Care Med , vol.159 , pp. 596-602
    • Bosse, M.1    Chakir, J.2    Rouabhia, M.3    Boulet, L.P.4    Audette, M.5    Laviolette, M.6
  • 131
    • 0036077458 scopus 로고    scopus 로고
    • Cysteine peptidases of mammals: Their biological roles and potential effects in the oral cavity and other tissues in health and disease
    • D. P. Dickinson, Cysteine peptidases of mammals: their biological roles and potential effects in the oral cavity and other tissues in health and disease. Crit. Rev. Oral. Biol. Med., 13: 238-275, 2002.
    • (2002) Crit. Rev. Oral. Biol. Med , vol.13 , pp. 238-275
    • Dickinson, D.P.1
  • 132
    • 0028476829 scopus 로고
    • Connective tissue degradation in health and periodontal disease and the roles of matrix metalloproteinases and their natural inhibitors
    • J. J. Reynolds, R. M. Hembry, and M. C. Meikle, Connective tissue degradation in health and periodontal disease and the roles of matrix metalloproteinases and their natural inhibitors. Adv. Dent. Res., 8: 312-319, 1994.
    • (1994) Adv. Dent. Res , vol.8 , pp. 312-319
    • Reynolds, J.J.1    Hembry, R.M.2    Meikle, M.C.3
  • 133
    • 25844460542 scopus 로고    scopus 로고
    • Host response modulation in the management of periodontal diseases
    • G. E. Salvi and N. P. Lang, Host response modulation in the management of periodontal diseases. J. Clin. Periodontol., 32(Suppl 6): 108-129, 2005.
    • (2005) J. Clin. Periodontol , vol.32 , Issue.SUPPL. 6 , pp. 108-129
    • Salvi, G.E.1    Lang, N.P.2
  • 134
    • 0032837039 scopus 로고    scopus 로고
    • Clinical trials of a matrix metalloproteinase inhibitor in human periodontal disease. SDD Clinical Research Team
    • R. A. Ashley, Clinical trials of a matrix metalloproteinase inhibitor in human periodontal disease. SDD Clinical Research Team. Ann. N. Y. Acad. Sci., 878: 335-346, 1999.
    • (1999) Ann. N. Y. Acad. Sci , vol.878 , pp. 335-346
    • Ashley, R.A.1
  • 136
    • 0142218538 scopus 로고    scopus 로고
    • Metalloproteinases, inflammation, and rheumatoid arthritis
    • F. F. Mohammed, D. S. Smookler, and R. Khokha, Metalloproteinases, inflammation, and rheumatoid arthritis. Ann. Rheum. Dis., 62: 43-47, 2003.
    • (2003) Ann. Rheum. Dis , vol.62 , pp. 43-47
    • Mohammed, F.F.1    Smookler, D.S.2    Khokha, R.3
  • 137
    • 33646557000 scopus 로고    scopus 로고
    • Aspect of extracellular matrix remodeling in development and disease
    • K. Holmbeck and L. Szabova, Aspect of extracellular matrix remodeling in development and disease. Birth Defects Res. (part C), 78: 11-23, 2006.
    • (2006) Birth Defects Res , vol.78 , Issue.PART C , pp. 11-23
    • Holmbeck, K.1    Szabova, L.2
  • 138
    • 40449132187 scopus 로고    scopus 로고
    • ADAM-15: A metalloprotease that mediates inflammation
    • L. Charrier-Hisamuddin, C. L. Laboisse, and D. Merlin, ADAM-15: a metalloprotease that mediates inflammation. FASEB J., 22: 641-653, 2008.
    • (2008) FASEB J , vol.22 , pp. 641-653
    • Charrier-Hisamuddin, L.1    Laboisse, C.L.2    Merlin, D.3
  • 139
    • 0035174308 scopus 로고    scopus 로고
    • Articular cartilage and changes in arthritis: Matrix degradation
    • J. S. Mort and C. J. Billington, Articular cartilage and changes in arthritis: matrix degradation. Arthritis Res., 3: 337-341, 2001.
    • (2001) Arthritis Res , vol.3 , pp. 337-341
    • Mort, J.S.1    Billington, C.J.2
  • 140
    • 0025061478 scopus 로고
    • Susceptibility of the cartilage collagens type II, IX and XI to degradation by the cysteine proteinases, cathepsins B and L
    • R. A. Maciewicz, S. F. Wotton, D. J. Etherington, and V. C. Duance, Susceptibility of the cartilage collagens type II, IX and XI to degradation by the cysteine proteinases, cathepsins B and L. FEBS, 269: 189-193, 1990.
    • (1990) FEBS , vol.269 , pp. 189-193
    • Maciewicz, R.A.1    Wotton, S.F.2    Etherington, D.J.3    Duance, V.C.4
  • 141
    • 0025945608 scopus 로고
    • Characterization of the changes in matrix molecules at the dermoepidermal junction in lupus erythematosus
    • E. Mooney, W. R. Gammon, and J. C. Jennette, Characterization of the changes in matrix molecules at the dermoepidermal junction in lupus erythematosus. J. Cutan. Pathol., 18: 417-422, 1991.
    • (1991) J. Cutan. Pathol , vol.18 , pp. 417-422
    • Mooney, E.1    Gammon, W.R.2    Jennette, J.C.3
  • 142
    • 0346336050 scopus 로고    scopus 로고
    • Pathogenesis of Goodpasture syndrome: A molecular perspective
    • D. B. Borza, E. G. Neilson, and B. G. Hudson, Pathogenesis of Goodpasture syndrome: a molecular perspective. Semin. Nephrol., 23: 522-531, 2003.
    • (2003) Semin. Nephrol , vol.23 , pp. 522-531
    • Borza, D.B.1    Neilson, E.G.2    Hudson, B.G.3
  • 143
    • 34447117525 scopus 로고    scopus 로고
    • Autoepitopes and alloepitopes of type IV collagen: Role in the molecular pathogenesis of anti-GBM antibody glomerulonephritis
    • D. B. Borza, Autoepitopes and alloepitopes of type IV collagen: role in the molecular pathogenesis of anti-GBM antibody glomerulonephritis. Nephron Exp. Nephrol., 106: e37-e43, 2007.
    • (2007) Nephron Exp. Nephrol , vol.106
    • Borza, D.B.1
  • 145
    • 18244376353 scopus 로고    scopus 로고
    • Evidence that anti-type VII collagen antibodies are pathogenic and responsible for the clinical, histological, and immunological features of epidermolysis bullosa acquisita
    • D. T. Woodley, C. Chang, P. Saadat, R. Ram, Z. Liu, and M. Chen, Evidence that anti-type VII collagen antibodies are pathogenic and responsible for the clinical, histological, and immunological features of epidermolysis bullosa acquisita. J. Invest. Dermatol., 124: 958-964, 2005.
    • (2005) J. Invest. Dermatol , vol.124 , pp. 958-964
    • Woodley, D.T.1    Chang, C.2    Saadat, P.3    Ram, R.4    Liu, Z.5    Chen, M.6
  • 146
    • 0023879341 scopus 로고    scopus 로고
    • E. KK Choi, P. A. Gatenby, N. W. McGill, J. F. Bateman, W. G. Cole, and J. R. York, Autoantibodies to type II collagen: occurrence in rheumatoid arthritis, other arthritides, autoimmune connective tissue diseases and chronic inflammatory syndromes. Ann. Rheum. Dis., 47: 313-322, 1988.
    • E. KK Choi, P. A. Gatenby, N. W. McGill, J. F. Bateman, W. G. Cole, and J. R. York, Autoantibodies to type II collagen: occurrence in rheumatoid arthritis, other arthritides, autoimmune connective tissue diseases and chronic inflammatory syndromes. Ann. Rheum. Dis., 47: 313-322, 1988.
  • 147
    • 0018817811 scopus 로고
    • Incidence of serum antibodies to native type I and type II collagens in patients with inflammatory arthritis
    • R. B. Clague, M. J. Shaw, and P.J. Lennox Holt, Incidence of serum antibodies to native type I and type II collagens in patients with inflammatory arthritis. Annals Rheum. Dis., 39: 201-206, 1980.
    • (1980) Annals Rheum. Dis , vol.39 , pp. 201-206
    • Clague, R.B.1    Shaw, M.J.2    Lennox Holt, P.J.3
  • 148
    • 0026728407 scopus 로고
    • The diagnostic significance of anti-type II collagen antibody assay in rheumatoid arthritis
    • K. Fujii, M. Tsujii, A. Kitamura, and K. Murota, The diagnostic significance of anti-type II collagen antibody assay in rheumatoid arthritis. Int. Orthop., 16: 272-276, 1992.
    • (1992) Int. Orthop , vol.16 , pp. 272-276
    • Fujii, K.1    Tsujii, M.2    Kitamura, A.3    Murota, K.4
  • 149
    • 0030721587 scopus 로고    scopus 로고
    • IgG subclasses of antibodies to type II collagen in rheumatoid arthritis differ from those in systemic lupus erythematosus and other connective tissue diseases
    • A. D. Cook, I. R. Mackay, F. M. Cicuttini, and M. J. Rowley, IgG subclasses of antibodies to type II collagen in rheumatoid arthritis differ from those in systemic lupus erythematosus and other connective tissue diseases. J. Rheumatol., 24: 2090-2096, 1997.
    • (1997) J. Rheumatol , vol.24 , pp. 2090-2096
    • Cook, A.D.1    Mackay, I.R.2    Cicuttini, F.M.3    Rowley, M.J.4
  • 151
    • 20744458153 scopus 로고    scopus 로고
    • Antibodies against the CB10 fragment of type II collagen in rheumatoid arthritis
    • A. D. Cook, R. Gray, J. Ramshaw, I. R. Mackay, and M. J. Rowley, Antibodies against the CB10 fragment of type II collagen in rheumatoid arthritis. Arthritis Res. Ther., 6: R477-483, 2004.
    • (2004) Arthritis Res. Ther , vol.6
    • Cook, A.D.1    Gray, R.2    Ramshaw, J.3    Mackay, I.R.4    Rowley, M.J.5
  • 152
    • 0023546380 scopus 로고
    • Incidence of antibodies to native and denatured cartilage collagens (type II, IX and XI) and to type I collagen in rheumatoid arthritis
    • K. Morgan, R. B. Clague, I. Collins, S. Ayad, S. D. Phinn, and P. J. L. Holt, Incidence of antibodies to native and denatured cartilage collagens (type II, IX and XI) and to type I collagen in rheumatoid arthritis. Annals Rheum. Dis., 46: 902-907, 1987.
    • (1987) Annals Rheum. Dis , vol.46 , pp. 902-907
    • Morgan, K.1    Clague, R.B.2    Collins, I.3    Ayad, S.4    Phinn, S.D.5    Holt, P.J.L.6
  • 153
    • 0028796036 scopus 로고
    • Investigation of the prevalence and clinical associations of antibodies to human fibronectin in systemic lupus erythematosus
    • M. S. Atta, K. L. Lim, D. A. Ala'deen, R. J. Powell, and I. Todd, Investigation of the prevalence and clinical associations of antibodies to human fibronectin in systemic lupus erythematosus. Ann. Rheum. Dis., 54: 117-124, 1995.
    • (1995) Ann. Rheum. Dis , vol.54 , pp. 117-124
    • Atta, M.S.1    Lim, K.L.2    Ala'deen, D.A.3    Powell, R.J.4    Todd, I.5
  • 155
    • 0030898795 scopus 로고    scopus 로고
    • Autoantibodies to collagens in Japanese patients with ankylosing spondylitis
    • Y. Tani, H. Sato, and S. Hukuda, Autoantibodies to collagens in Japanese patients with ankylosing spondylitis. Clin. Exp. Rheumatol, 15: 295-297, 1997.
    • (1997) Clin. Exp. Rheumatol , vol.15 , pp. 295-297
    • Tani, Y.1    Sato, H.2    Hukuda, S.3
  • 156
    • 0035146630 scopus 로고    scopus 로고
    • Correlation between the immune responses to collagens type I, III, IV and V and Klebsiella pneumoniae in patients with Crohn's disease and ankylosing spondylitis
    • H. Tiwana, R. S. Natt, R. Benitez-Brito, S. Shah, C. Wilson, S. Bridger, M. Harbord, M. Sarner, and A. Ebringer, Correlation between the immune responses to collagens type I, III, IV and V and Klebsiella pneumoniae in patients with Crohn's disease and ankylosing spondylitis. Rheumatology (Oxford), 40: 15-23, 2001.
    • (2001) Rheumatology (Oxford) , vol.40 , pp. 15-23
    • Tiwana, H.1    Natt, R.S.2    Benitez-Brito, R.3    Shah, S.4    Wilson, C.5    Bridger, S.6    Harbord, M.7    Sarner, M.8    Ebringer, A.9
  • 157
    • 0025781486 scopus 로고
    • Collagen autoantibodies in patients with vasculitis and systemic lupus erythematosus
    • L. W. Moreland, R. E. Gay, and S. Gay, Collagen autoantibodies in patients with vasculitis and systemic lupus erythematosus. Clin. Immunol. Immunopathol., 60: 412-418, 1991.
    • (1991) Clin. Immunol. Immunopathol , vol.60 , pp. 412-418
    • Moreland, L.W.1    Gay, R.E.2    Gay, S.3
  • 158
    • 0022450313 scopus 로고
    • Antibodies to type IV collagen in rheumatic diseases
    • R. E. Petty, D. W. Hunt, and A. M. Rosenberg, Antibodies to type IV collagen in rheumatic diseases. J. Rheumatol., 13: 246-253, 1986.
    • (1986) J. Rheumatol , vol.13 , pp. 246-253
    • Petty, R.E.1    Hunt, D.W.2    Rosenberg, A.M.3
  • 159
    • 0028223883 scopus 로고
    • Autoantibodies against endothelial cells, extracellular matrix, and human collagen type IV in patients with systemic vasculitis
    • H. Direskeneli, D. D'Cruz, M. A. Khamashta, and G. R. Hughes, Autoantibodies against endothelial cells, extracellular matrix, and human collagen type IV in patients with systemic vasculitis. Clin. Immunol. Immunopathol., 70: 206-210, 1994.
    • (1994) Clin. Immunol. Immunopathol , vol.70 , pp. 206-210
    • Direskeneli, H.1    D'Cruz, D.2    Khamashta, M.A.3    Hughes, G.R.4
  • 160
    • 0024268992 scopus 로고
    • A retrospective study of antibodies against basement membrane antigens (type IV collagen and laminin) in patients with primary and secondary Raynaud's phenomenon
    • A. Gabrielli, M. Montroni, S. Rupoli, M. L. Caniglia, F. DeLustro, and G. Danieli, A retrospective study of antibodies against basement membrane antigens (type IV collagen and laminin) in patients with primary and secondary Raynaud's phenomenon. Arthritis Rheum., 31: 1432-1436, 1988.
    • (1988) Arthritis Rheum , vol.31 , pp. 1432-1436
    • Gabrielli, A.1    Montroni, M.2    Rupoli, S.3    Caniglia, M.L.4    DeLustro, F.5    Danieli, G.6
  • 161
    • 0030849380 scopus 로고    scopus 로고
    • Humoral and cellular immune response to elastin in patients with systemic sclerosis
    • M. Daskalova, H. Taskov, E. Dimitrova, and S. Baydanoff, Humoral and cellular immune response to elastin in patients with systemic sclerosis. Autoimmunity, 25: 233-241, 1997.
    • (1997) Autoimmunity , vol.25 , pp. 233-241
    • Daskalova, M.1    Taskov, H.2    Dimitrova, E.3    Baydanoff, S.4
  • 162
    • 0026505737 scopus 로고
    • Antibodies to native type III collagen in the serum of patients with Kawasaki disease
    • S. Kobayashi, N. Wada, and M. Kubo, Antibodies to native type III collagen in the serum of patients with Kawasaki disease. Eur. J. Pediatr., 151: 183-187, 1992.
    • (1992) Eur. J. Pediatr , vol.151 , pp. 183-187
    • Kobayashi, S.1    Wada, N.2    Kubo, M.3
  • 163
    • 0028173471 scopus 로고
    • Significance of anti-entactin antibodies in patients with systemic lupus erythematosus and related disorders
    • R. Saxena, G. Sturfelt, O. Nived, and J. Wieslander, Significance of anti-entactin antibodies in patients with systemic lupus erythematosus and related disorders. Ann. Rheum. Dis., 53: 659-665, 1994.
    • (1994) Ann. Rheum. Dis , vol.53 , pp. 659-665
    • Saxena, R.1    Sturfelt, G.2    Nived, O.3    Wieslander, J.4
  • 166
    • 0037379343 scopus 로고    scopus 로고
    • Function blocking autoantibodies against matrix metalloproteinase-1 in patients with systemic sclerosis
    • S. Sato, I. Hayakawa, M. Hasegawa, M. Fujimoto, and K. Takehara, Function blocking autoantibodies against matrix metalloproteinase-1 in patients with systemic sclerosis. J. Invest. Dermatol., 120: 542-547, 2003.
    • (2003) J. Invest. Dermatol , vol.120 , pp. 542-547
    • Sato, S.1    Hayakawa, I.2    Hasegawa, M.3    Fujimoto, M.4    Takehara, K.5
  • 169
    • 33846412669 scopus 로고    scopus 로고
    • Study of serum antibodies against three eye muscle antigens and the connective tissue antigen collagen XIII in patients with Graves' disease with and without ophthalmopathy: Correlation with clinical features
    • B. Gopinath, R. Musselman, C. L. Adams, J. Tani, N. Beard, and J. R. Wall, Study of serum antibodies against three eye muscle antigens and the connective tissue antigen collagen XIII in patients with Graves' disease with and without ophthalmopathy: correlation with clinical features. Thyroid, 16: 967-974, 2006.
    • (2006) Thyroid , vol.16 , pp. 967-974
    • Gopinath, B.1    Musselman, R.2    Adams, C.L.3    Tani, J.4    Beard, N.5    Wall, J.R.6
  • 171
    • 0028169652 scopus 로고
    • Menier's disease: Role of antibodies against basementmembrane antigens
    • B. Fattori, P. L. Ghilardi, A. Casani, P. Miglirini, and L. Riente, Menier's disease: role of antibodies against basementmembrane antigens. Laryngoscope, 104: 1290-1294, 1994.
    • (1994) Laryngoscope , vol.104 , pp. 1290-1294
    • Fattori, B.1    Ghilardi, P.L.2    Casani, A.3    Miglirini, P.4    Riente, L.5
  • 172
    • 0027460466 scopus 로고
    • Antibodies to collagen in patients with idiopathic pulmonary fibrosis
    • G. Nakos, A. Adams, and N. Andriopoulos, Antibodies to collagen in patients with idiopathic pulmonary fibrosis. Chest, 103: 1051-1058, 1993.
    • (1993) Chest , vol.103 , pp. 1051-1058
    • Nakos, G.1    Adams, A.2    Andriopoulos, N.3
  • 173
    • 0035146630 scopus 로고    scopus 로고
    • Correlation between the immune responses to collagens type I, III, IV and V and Klebsiella pneumoniae in patients with Crohn's disease and ankylosing spondylitis
    • H. Tiwana, R. S. Natt, R. Benitez-Brito, S. Shah, C. Wilson, S. Bridger, M. Harbord, M. Sarner, and A. Ebringer, Correlation between the immune responses to collagens type I, III, IV and V and Klebsiella pneumoniae in patients with Crohn's disease and ankylosing spondylitis. Rheumatology (Oxford), 40: 15-23, 2001.
    • (2001) Rheumatology (Oxford) , vol.40 , pp. 15-23
    • Tiwana, H.1    Natt, R.S.2    Benitez-Brito, R.3    Shah, S.4    Wilson, C.5    Bridger, S.6    Harbord, M.7    Sarner, M.8    Ebringer, A.9
  • 174
    • 0036280843 scopus 로고    scopus 로고
    • The epidermolysis bullosa acquisita antigen (type VII collagen) is present in human colon and patients with crohn's disease have autoantibodies to type VII collagen
    • M. Chen, E. A. O'Toole, J. Sanghavi, N. Mahmud, D. Kelleher, D. Weir, J. A. Fairley, and D. T. Woodley, The epidermolysis bullosa acquisita antigen (type VII collagen) is present in human colon and patients with crohn's disease have autoantibodies to type VII collagen. J. Invest. Dermatol., 118: 1059-1064, 2002.
    • (2002) J. Invest. Dermatol , vol.118 , pp. 1059-1064
    • Chen, M.1    O'Toole, E.A.2    Sanghavi, J.3    Mahmud, N.4    Kelleher, D.5    Weir, D.6    Fairley, J.A.7    Woodley, D.T.8
  • 175
    • 14744287818 scopus 로고    scopus 로고
    • Subclass distribution of type VII collagen-specific autoantibodies in patients with inflammatory bowel disease
    • G. J. Oostingh, C. Sitaru, D. Zillikens, A. Kromminga, and H. Luhrs, Subclass distribution of type VII collagen-specific autoantibodies in patients with inflammatory bowel disease. J. Dermatol. Sci., 37: 182-184, 2005.
    • (2005) J. Dermatol. Sci , vol.37 , pp. 182-184
    • Oostingh, G.J.1    Sitaru, C.2    Zillikens, D.3    Kromminga, A.4    Luhrs, H.5
  • 176
    • 1542284204 scopus 로고    scopus 로고
    • Circulating basement membrane zone antibodies are found in lichen sclerosus of the vulva
    • A. Howard, D. Dean, S. Cooper, G. Kirtshig, and F. Wojnarowska, Circulating basement membrane zone antibodies are found in lichen sclerosus of the vulva. Australas. J. Dermatol., 45:12-15, 2004.
    • (2004) Australas. J. Dermatol , vol.45 , pp. 12-15
    • Howard, A.1    Dean, D.2    Cooper, S.3    Kirtshig, G.4    Wojnarowska, F.5
  • 177
    • 23044496329 scopus 로고    scopus 로고
    • Erosive lichen planus of the vulva: Weak circulating basement membrane zone antibodies are present
    • S. M. Cooper, D. Dean, J. Allen, G. Kirtschig, and F. Wojnarowska, Erosive lichen planus of the vulva: weak circulating basement membrane zone antibodies are present. Clin. Exp. Dermatol., 30: 551-556, 2005.
    • (2005) Clin. Exp. Dermatol , vol.30 , pp. 551-556
    • Cooper, S.M.1    Dean, D.2    Allen, J.3    Kirtschig, G.4    Wojnarowska, F.5
  • 178
    • 0026232462 scopus 로고
    • Immunoglobulin isotype distribution of locally produced autoantibodies to collagen type I in adult periodontitis. Relationship to periodontal treatment
    • R. Jonsson, A. Pitts, C. Lue, S. Gay, and J. Mestecky, Immunoglobulin isotype distribution of locally produced autoantibodies to collagen type I in adult periodontitis. Relationship to periodontal treatment. J. Clin. Periodontol., 18: 703-707, 1991.
    • (1991) J. Clin. Periodontol , vol.18 , pp. 703-707
    • Jonsson, R.1    Pitts, A.2    Lue, C.3    Gay, S.4    Mestecky, J.5
  • 179
    • 33845777625 scopus 로고    scopus 로고
    • Autoantibodies directed to extracellular matrix components in patients with different clinical forms of periodontitis
    • L. A. De-Gennaro, J. D. Lopes, and M. Mariano, Autoantibodies directed to extracellular matrix components in patients with different clinical forms of periodontitis. J. Periodontol., 77: 2025-2030, 2006.
    • (2006) J. Periodontol , vol.77 , pp. 2025-2030
    • De-Gennaro, L.A.1    Lopes, J.D.2    Mariano, M.3
  • 181
    • 0030883484 scopus 로고    scopus 로고
    • T cell responses to human type II collagen in patients with rheumatoid arthritis and healthy controls
    • N. Snowden, I. Reynolds, K. Morgan, and L. Holt, T cell responses to human type II collagen in patients with rheumatoid arthritis and healthy controls. Arthritis Rheum., 40: 1210-1218, 1997.
    • (1997) Arthritis Rheum , vol.40 , pp. 1210-1218
    • Snowden, N.1    Reynolds, I.2    Morgan, K.3    Holt, L.4
  • 182
    • 13444263297 scopus 로고    scopus 로고
    • T cell proliferative response to type II collagen in the inflammatory process and joint damage in patients with rheumatoid arthritis
    • W. U. Kim and K. J. Kim, T cell proliferative response to type II collagen in the inflammatory process and joint damage in patients with rheumatoid arthritis. J. Rheumatol., 32: 225-230, 2005.
    • (2005) J. Rheumatol , vol.32 , pp. 225-230
    • Kim, W.U.1    Kim, K.J.2
  • 183
    • 0035085562 scopus 로고    scopus 로고
    • Shift toward T helper 1 cytokines by type II collagen-reactive T cells in patients with rheumatoid arthritis
    • S. H. Park, D. J. Min, M. L. Cho, W. U. Kim, J. Youn, W. Park, C. S. Cho, and H. Y. Kim, Shift toward T helper 1 cytokines by type II collagen-reactive T cells in patients with rheumatoid arthritis. Arthritis Rheum., 44: 561-569, 2001.
    • (2001) Arthritis Rheum , vol.44 , pp. 561-569
    • Park, S.H.1    Min, D.J.2    Cho, M.L.3    Kim, W.U.4    Youn, J.5    Park, W.6    Cho, C.S.7    Kim, H.Y.8
  • 184
    • 12444341312 scopus 로고    scopus 로고
    • T cell epitopes of type II collagen in HLA-DRB1*0101 or DRB1*0405-positive Japanese patients with rheumatoid arthritis
    • Y. Ohnishi, A. Tsutsumi, T. Sakamaki, and T. Sumida, T cell epitopes of type II collagen in HLA-DRB1*0101 or DRB1*0405-positive Japanese patients with rheumatoid arthritis. Int. J. Mol. Med., 11: 331-335, 2003.
    • (2003) Int. J. Mol. Med , vol.11 , pp. 331-335
    • Ohnishi, Y.1    Tsutsumi, A.2    Sakamaki, T.3    Sumida, T.4
  • 186
    • 0038657723 scopus 로고    scopus 로고
    • Identification of self-epitopes recognized by T cells in rheumatoid arthritis demonstrates matrix metalloproteinases as a novel T cell target
    • J. ter Steege, M. Vianen, J. van Bilsen, J. Bijlsma, F. Lafeber, and M. Wauben, Identification of self-epitopes recognized by T cells in rheumatoid arthritis demonstrates matrix metalloproteinases as a novel T cell target. J. Rheumatol., 30: 1147-1156, 2003.
    • (2003) J. Rheumatol , vol.30 , pp. 1147-1156
    • ter Steege, J.1    Vianen, M.2    van Bilsen, J.3    Bijlsma, J.4    Lafeber, F.5    Wauben, M.6
  • 187
    • 17644422829 scopus 로고    scopus 로고
    • Analysis of the CD8+ T cell response to the G1 domain of aggrecan in ankylosing spondylitis
    • J. Zou, H. Appel, M. Rudwaleit, A. Thiel, and J. Sieper, Analysis of the CD8+ T cell response to the G1 domain of aggrecan in ankylosing spondylitis. Ann. Rheum. Dis., 64: 722-729. 2005.
    • (2005) Ann. Rheum. Dis , vol.64 , pp. 722-729
    • Zou, J.1    Appel, H.2    Rudwaleit, M.3    Thiel, A.4    Sieper, J.5
  • 188
    • 0041411251 scopus 로고    scopus 로고
    • Predominant cellular immune response to the cartilage autoantigenic G1 aggrecan in ankylosing spondylitis and rheumatoid arthritis
    • J. Zou, Y. Zhang, A. Thiel, M. Rudwaleit, S. L. Shi, A. Radbruch, R. Poole, J. Braun, and J. Sieper, Predominant cellular immune response to the cartilage autoantigenic G1 aggrecan in ankylosing spondylitis and rheumatoid arthritis. Rheumatology (Oxford), 42: 846-855, 2003.
    • (2003) Rheumatology (Oxford) , vol.42 , pp. 846-855
    • Zou, J.1    Zhang, Y.2    Thiel, A.3    Rudwaleit, M.4    Shi, S.L.5    Radbruch, A.6    Poole, R.7    Braun, J.8    Sieper, J.9
  • 189
  • 190
    • 0032936560 scopus 로고    scopus 로고
    • its role in acquired and inherited disorders or the dermal-epidermal junction
    • BP180/type XVII collagen
    • D. Zillikens and G. J. Giudice, BP180/type XVII collagen: its role in acquired and inherited disorders or the dermal-epidermal junction. Arch. Dermatol. Res., 291: 187-194, 1999.
    • (1999) Arch. Dermatol. Res , vol.291 , pp. 187-194
    • Zillikens, D.1    Giudice, G.J.2
  • 191
    • 0018830639 scopus 로고
    • Immunisation against heterologous type II collagen induces arthritis in mice
    • J. S. Courtenay, M. J. Dallman, A. D. Dayan, A. Martin, and B. Mosedale, Immunisation against heterologous type II collagen induces arthritis in mice. Nature, 283: 666-668, 1980.
    • (1980) Nature , vol.283 , pp. 666-668
    • Courtenay, J.S.1    Dallman, M.J.2    Dayan, A.D.3    Martin, A.4    Mosedale, B.5
  • 192
    • 0036177686 scopus 로고    scopus 로고
    • Extra-articular cartilage affected in collagen-induced, but not pristane-induced, arthritis models
    • A. S. Hansson, S. Lu, and R. Holmdahl, Extra-articular cartilage affected in collagen-induced, but not pristane-induced, arthritis models.Clin. Exp. Immunol., 127: 37-42, 2002.
    • (2002) Clin. Exp. Immunol , vol.127 , pp. 37-42
    • Hansson, A.S.1    Lu, S.2    Holmdahl, R.3
  • 193
    • 0025037855 scopus 로고
    • Arthritis in DBA/1 mice induced with passively transferred type II collagen immune serum. Immunohistopathology and serum levels of anti-type II collagen auto-antibodies
    • R. Holmdahl, L. Jansson, A. Larsson, and R. Jonsson, Arthritis in DBA/1 mice induced with passively transferred type II collagen immune serum. Immunohistopathology and serum levels of anti-type II collagen auto-antibodies. Scand. J. Immunol., 31: 147-157, 1990.
    • (1990) Scand. J. Immunol , vol.31 , pp. 147-157
    • Holmdahl, R.1    Jansson, L.2    Larsson, A.3    Jonsson, R.4
  • 194
    • 33645511657 scopus 로고    scopus 로고
    • Antibodies against citrullinated proteins enhance tissue injury in experimental autoimmune arthritis
    • K. A. Kuhn, L. Kulik, B. Tomooka, K. J. Braschler, W. P. Arend, W. H. Robinson, and V. M. Holers, Antibodies against citrullinated proteins enhance tissue injury in experimental autoimmune arthritis. J. Clin. Invest., 116: 961-973, 2006
    • (2006) J. Clin. Invest , vol.116 , pp. 961-973
    • Kuhn, K.A.1    Kulik, L.2    Tomooka, B.3    Braschler, K.J.4    Arend, W.P.5    Robinson, W.H.6    Holers, V.M.7
  • 195
    • 33750373414 scopus 로고    scopus 로고
    • Experimental spondyloarthropathies: Animal models of ankylosing spondylitis
    • V. A. Adarichev and T. T. Glant, Experimental spondyloarthropathies: animal models of ankylosing spondylitis. Curr. Rheumatol. Rep., 8: 267-274, 2006.
    • (2006) Curr. Rheumatol. Rep , vol.8 , pp. 267-274
    • Adarichev, V.A.1    Glant, T.T.2
  • 196
    • 27644508644 scopus 로고    scopus 로고
    • Molecular manipulation with the arthritogenic epitopes of the G1 domain of human cartilage proteoglycan aggrecan
    • Y. M Murad, Z. Szabó, K. Ludányi, and T. T. Glant, Molecular manipulation with the arthritogenic epitopes of the G1 domain of human cartilage proteoglycan aggrecan. Clin. Exp. Immunol., 142: 303-311, 2005.
    • (2005) Clin. Exp. Immunol , vol.142 , pp. 303-311
    • Murad, Y.M.1    Szabó, Z.2    Ludányi, K.3    Glant, T.T.4
  • 197
    • 16644373165 scopus 로고    scopus 로고
    • Proteoglycan aggrecan-induced arthritis: A murine autoimmune model of rheumatoid arthritis
    • T. T. Glant and K. Mikecz, Proteoglycan aggrecan-induced arthritis: a murine autoimmune model of rheumatoid arthritis. Methods Mol. Med., 102: 313-338, 2004.
    • (2004) Methods Mol. Med , vol.102 , pp. 313-338
    • Glant, T.T.1    Mikecz, K.2
  • 198
    • 10244278101 scopus 로고    scopus 로고
    • Architectural remodeling in lungs of rabbits induced by type V collagen immunization: A preliminary morphologic model to study diffuse connective tissue diseases
    • W. R. Teodoro, A. P. Velosa, S. S. Witzel, A. L. Garippo, C. Farhat, E. R. Parra, S. Sonohara, V. L. Capelozzi, and N. H. Yoshinari, Architectural remodeling in lungs of rabbits induced by type V collagen immunization: a preliminary morphologic model to study diffuse connective tissue diseases. Pathol. Res. Pract., 200: 681-691, 2004.
    • (2004) Pathol. Res. Pract , vol.200 , pp. 681-691
    • Teodoro, W.R.1    Velosa, A.P.2    Witzel, S.S.3    Garippo, A.L.4    Farhat, C.5    Parra, E.R.6    Sonohara, S.7    Capelozzi, V.L.8    Yoshinari, N.H.9
  • 199
    • 0021713694 scopus 로고
    • Detection of autoantibodies and glomerular injury in rabbits immunized with denatured human fibronectin monomer
    • J. E. Murphy-Ullrich, T. D. Oberley, and D.F Mosher, Detection of autoantibodies and glomerular injury in rabbits immunized with denatured human fibronectin monomer. Am. J. Pathol., 117: 1-11, 1984.
    • (1984) Am. J. Pathol , vol.117 , pp. 1-11
    • Murphy-Ullrich, J.E.1    Oberley, T.D.2    Mosher, D.F.3
  • 200
    • 0030035657 scopus 로고    scopus 로고
    • Significance of anti-nuclear and anti-extracellular matrix autoantibodies for albuminuria in murine lupus nephritis; a longitudinal study on plasma and glomerular eluates in MRL/l mice
    • M. C. van Bruggen, C. Kramers, M. N. Hylkema, R. J. Smeenk, and J. H. Berden, Significance of anti-nuclear and anti-extracellular matrix autoantibodies for albuminuria in murine lupus nephritis; a longitudinal study on plasma and glomerular eluates in MRL/l mice. Clin. Exp. Immunol., 105: 132-139, 1996.
    • (1996) Clin. Exp. Immunol , vol.105 , pp. 132-139
    • van Bruggen, M.C.1    Kramers, C.2    Hylkema, M.N.3    Smeenk, R.J.4    Berden, J.H.5
  • 201
    • 25444475774 scopus 로고    scopus 로고
    • scleroderma phenotype
    • Autoantibodies to fibrillin-1 activate normal human fibroblasts in culture through the TGF-beta pathway to recapitulate the
    • X. Zhou, F. K. Tan, D. M. Milewicz, X. Guo, C. A. Bona, and F. C. Arnett, Autoantibodies to fibrillin-1 activate normal human fibroblasts in culture through the TGF-beta pathway to recapitulate the "scleroderma phenotype." J. Immunol., 175: 4555-4560, 2005.
    • (2005) J. Immunol , vol.175 , pp. 4555-4560
    • Zhou, X.1    Tan, F.K.2    Milewicz, D.M.3    Guo, X.4    Bona, C.A.5    Arnett, F.C.6
  • 202
    • 0038284750 scopus 로고    scopus 로고
    • Autoimmune thyroid diseases: Etiology, pathogenesis, and dermatologic manifestations
    • J. Ai, J. M. Leonhardt, and W. R. Heymann, Autoimmune thyroid diseases: etiology, pathogenesis, and dermatologic manifestations. J. Am. Acad. Dermatol., 48: 641-659, 2003.
    • (2003) J. Am. Acad. Dermatol , vol.48 , pp. 641-659
    • Ai, J.1    Leonhardt, J.M.2    Heymann, W.R.3


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