메뉴 건너뛰기




Volumn 270, Issue 18, 2003, Pages 3739-3749

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

Author keywords

CXC chemokine; Feedback; Interleukin 8; Mass spectrometry; Neutrophil

Indexed keywords

EPITHELIAL DERIVED NEUTROPHIL ACTIVATING FACTOR 78; GELATINASE B; INTERLEUKIN 8; NEUTROPHIL COLLAGENASE; NITROGEN;

EID: 0141782259     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03760.x     Document Type: Article
Times cited : (254)

References (57)
  • 2
    • 0032194115 scopus 로고    scopus 로고
    • Generation of biologically active IL-1β by matrix metalloproteinases: A novel caspase-1-independent pathway of IL-1β processing
    • Schönbeck, U., Mach, F. & Libby, P. (1998) Generation of biologically active IL-1β by matrix metalloproteinases: a novel caspase-1-independent pathway of IL-1β processing. J. Immunol. 161, 3340-3346.
    • (1998) J. Immunol. , vol.161 , pp. 3340-3346
    • Schönbeck, U.1    Mach, F.2    Libby, P.3
  • 3
    • 0034667542 scopus 로고    scopus 로고
    • 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
    • Van den Steen, P.E., Proost, P., Wuyts, A., Van Damme, J. & Opdenakker, G. (2000) Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact. Blood 96, 2673-2681.
    • (2000) Blood , vol.96 , pp. 2673-2681
    • Van Den Steen, P.E.1    Proost, P.2    Wuyts, A.3    Van Damme, J.4    Opdenakker, G.5
  • 4
    • 0034682885 scopus 로고    scopus 로고
    • Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3
    • McQuibban, G.A., Gong, J.H., Tam, E.M., McCulloch, C.A., Clark-Lewis, I. & Overall, C.M. (2000) Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. Science 289, 1202-1206.
    • (2000) Science , vol.289 , pp. 1202-1206
    • McQuibban, G.A.1    Gong, J.H.2    Tam, E.M.3    McCulloch, C.A.4    Clark-Lewis, I.5    Overall, C.M.6
  • 5
    • 0030825407 scopus 로고    scopus 로고
    • Chemokines
    • Rollins, B.J. (1997) Chemokines. Blood 90, 909-928.
    • (1997) Blood , vol.90 , pp. 909-928
    • Rollins, B.J.1
  • 6
    • 0002821076 scopus 로고    scopus 로고
    • Interleukin-8 and other CXC chemokines
    • Thomson, A., ed. Academic Press, London
    • Wuyts, A., Proost, P. & Van Damme, J. (1998) Interleukin-8 and other CXC chemokines. In The Cytokine Handbook (Thomson, A., ed.), pp. 271-311. Academic Press, London.
    • (1998) The Cytokine Handbook , pp. 271-311
    • Wuyts, A.1    Proost, P.2    Van Damme, J.3
  • 8
    • 0032185642 scopus 로고    scopus 로고
    • Proliferative effects of CXC chemokines in rat hepatocytes in vitro and in vivo
    • Colletti, L.M., Green, M., Burdick, M.D., Kunkel, S.L. & Strieter, R.M. (1998) Proliferative effects of CXC chemokines in rat hepatocytes in vitro and in vivo. Shock 10, 248-257.
    • (1998) Shock , vol.10 , pp. 248-257
    • Colletti, L.M.1    Green, M.2    Burdick, M.D.3    Kunkel, S.L.4    Strieter, R.M.5
  • 10
    • 0023818527 scopus 로고
    • 2-terminal sequence-characterized human monokine possessing neutrophil chemotactic, skin-reactive, and granulocytosis-promoting activity
    • 2-terminal sequence-characterized human monokine possessing neutrophil chemotactic, skin-reactive, and granulocytosis-promoting activity. J. Exp. Med. 167, 1364-1376.
    • (1988) J. Exp. Med. , vol.167 , pp. 1364-1376
    • Van Damme, J.1    Van Beeumen, J.2    Opdenakker, G.3    Billiau, A.4
  • 11
    • 0027308750 scopus 로고
    • Identification of a novel granulocyte chemotactic protein (GCP-2) from human tumor cells. In vitro and in vivo comparison with natural forms of GRO, IP-10, and IL-8
    • Proost, P., De Wolf-Peeters, C., Conings, R., Opdenakker, G., Billiau, A. & Van Damme, J. (1993) Identification of a novel granulocyte chemotactic protein (GCP-2) from human tumor cells. In vitro and in vivo comparison with natural forms of GRO, IP-10, and IL-8. J. Immunol. 150, 1000-1010.
    • (1993) J. Immunol. , vol.150 , pp. 1000-1010
    • Proost, P.1    De Wolf-Peeters, C.2    Conings, R.3    Opdenakker, G.4    Billiau, A.5    Van Damme, J.6
  • 12
    • 0029014802 scopus 로고
    • Glucocorticoid-attenuated response genes encode intercellular mediators, including a new C-X-C chemokine
    • Smith, J.B. & Herschman, H.R. (1995) Glucocorticoid-attenuated response genes encode intercellular mediators, including a new C-X-C chemokine. J. Biol. Chem. 270, 16756-16765.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16756-16765
    • Smith, J.B.1    Herschman, H.R.2
  • 13
    • 0030586569 scopus 로고    scopus 로고
    • Identification of mouse granulocyte chemotactic protein-2 from fibroblasts and epithelial cells. Functional comparison with natural KC and macrophage inflammatory protein-2
    • Wuyts, A., Haelens, A., Proost, P., Lenaerts, J.-P., Conings, R., Opdenakker, G. & Van Damme, J. (1996) Identification of mouse granulocyte chemotactic protein-2 from fibroblasts and epithelial cells. Functional comparison with natural KC and macrophage inflammatory protein-2. J. Immunol. 157, 1736-1743.
    • (1996) J. Immunol. , vol.157 , pp. 1736-1743
    • Wuyts, A.1    Haelens, A.2    Proost, P.3    Lenaerts, J.-P.4    Conings, R.5    Opdenakker, G.6    Van Damme, J.7
  • 14
    • 0032509889 scopus 로고    scopus 로고
    • Chemokines: Chemotactic cytokines that mediate inflammation
    • Luster, A.D. (1998) Chemokines: chemotactic cytokines that mediate inflammation. N. Engl. J. Med. 338, 436-445.
    • (1998) N. Engl. J. Med. , vol.338 , pp. 436-445
    • Luster, A.D.1
  • 16
    • 0030887899 scopus 로고    scopus 로고
    • IL-8 and NAP-2 differ in their capacities to bind and chemoattract 293 cells transfected with either IL-8 receptor type A or type B
    • Ben-Baruch, A., Bengali, K., Tani, K., Xu, L., Oppenheim, J.J. & Wang, J.M. (1997) IL-8 and NAP-2 differ in their capacities to bind and chemoattract 293 cells transfected with either IL-8 receptor type A or type B. Cytokine 9, 37-45.
    • (1997) Cytokine , vol.9 , pp. 37-45
    • Ben-Baruch, A.1    Bengali, K.2    Tani, K.3    Xu, L.4    Oppenheim, J.J.5    Wang, J.M.6
  • 18
    • 0032127522 scopus 로고    scopus 로고
    • Differential usage of the CXC chemokine receptors 1 and 2 by interleukin-8, granulocyte chemotactic protein-2 and epithelial-cell-derived neutrophil attractant-78
    • Wuyts, A., Proost, P., Lenaerts, J.P., Ben-Baruch, A., Van Damme, J. & Wang, J.M. (1998) Differential usage of the CXC chemokine receptors 1 and 2 by interleukin-8, granulocyte chemotactic protein-2 and epithelial-cell-derived neutrophil attractant-78. Eur. J. Biochem. 255, 67-73.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 67-73
    • Wuyts, A.1    Proost, P.2    Lenaerts, J.P.3    Ben-Baruch, A.4    Van Damme, J.5    Wang, J.M.6
  • 19
    • 0025808816 scopus 로고
    • Purification and identification of 91-kDa neutrophil gelatinase. Release by the activating peptide interleukin-8
    • Masure, S., Proost, P., Van Damme, J. & Opdenakker, G. (1991) Purification and identification of 91-kDa neutrophil gelatinase. Release by the activating peptide interleukin-8. Eur. J. Biochem. 198, 391-398.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 391-398
    • Masure, S.1    Proost, P.2    Van Damme, J.3    Opdenakker, G.4
  • 20
    • 0023940237 scopus 로고
    • A novel neutrophil-activating factor produced by human mononuclear phagocytes
    • Peveri, P., Walz, A., Dewald, B. & Baggiolini, M. (1988) A novel neutrophil-activating factor produced by human mononuclear phagocytes. J. Exp. Med. 167, 1547-1559.
    • (1988) J. Exp. Med. , vol.167 , pp. 1547-1559
    • Peveri, P.1    Walz, A.2    Dewald, B.3    Baggiolini, M.4
  • 21
    • 0024359599 scopus 로고
    • Neutrophil activating factor (NAF) induces polymorphonuclear leukocyte adherence to endothelial cells and to subendothelial matrix proteins
    • Carveth, H.J., Bohnsack, J.F., McIntyre, T.M., Baggiolini, M., Prescott, S.M. & Zimmerman, G.A. (1989) Neutrophil activating factor (NAF) induces polymorphonuclear leukocyte adherence to endothelial cells and to subendothelial matrix proteins. Biochem. Biophys. Res. Commun. 162, 387-393.
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 387-393
    • Carveth, H.J.1    Bohnsack, J.F.2    McIntyre, T.M.3    Baggiolini, M.4    Prescott, S.M.5    Zimmerman, G.A.6
  • 22
    • 0025303942 scopus 로고
    • Neutrophil-activating protein 1/interleukin 8 stimulates the binding activity of the leukocyte adhesion receptor CD11b/CD18 on human neutrophils
    • Detmers, P.A., Lo, S.K., Olsen-Egbert, E., Walz, A., Baggiolini, M. & Cohn, Z.A. (1990) Neutrophil-activating protein 1/interleukin 8 stimulates the binding activity of the leukocyte adhesion receptor CD11b/CD18 on human neutrophils. J. Exp. Med. 171, 1155-1162.
    • (1990) J. Exp. Med. , vol.171 , pp. 1155-1162
    • Detmers, P.A.1    Lo, S.K.2    Olsen-Egbert, E.3    Walz, A.4    Baggiolini, M.5    Cohn, Z.A.6
  • 23
    • 0011489860 scopus 로고
    • Activation of the endogenous metalloproteinase, gelatinase, by triggered human neutrophils
    • Peppin, G.J. & Weiss, S.J. (1986) Activation of the endogenous metalloproteinase, gelatinase, by triggered human neutrophils. Proc. Natl. Acad. Sci. USA 83, 4322-4326.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4322-4326
    • Peppin, G.J.1    Weiss, S.J.2
  • 24
    • 0026660964 scopus 로고
    • Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9
    • Ogata, Y., Enghild, J.J. & Nagase, H. (1992) Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9. J. Biol. Chem. 267, 3581-3584.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3581-3584
    • Ogata, Y.1    Enghild, J.J.2    Nagase, H.3
  • 26
    • 0029824947 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinase 9 expression by a ribozyme blocks metastasis in a rat sarcoma model system
    • Hua, J. & Muschel, R.J. (1996) Inhibition of matrix metalloproteinase 9 expression by a ribozyme blocks metastasis in a rat sarcoma model system. Cancer Res. 56, 5279-5284.
    • (1996) Cancer Res. , vol.56 , pp. 5279-5284
    • Hua, J.1    Muschel, R.J.2
  • 27
    • 0033485667 scopus 로고    scopus 로고
    • Possible involvement of matrix metalloproteinase-9 in Langerhans cell migration and maturation
    • Kobayashi, Y., Matsumoto, M., Kotani, M. & Makino, T. (1999) Possible involvement of matrix metalloproteinase-9 in Langerhans cell migration and maturation. J. Immunol. 163, 5989-5993.
    • (1999) J. Immunol. , vol.163 , pp. 5989-5993
    • Kobayashi, Y.1    Matsumoto, M.2    Kotani, M.3    Makino, T.4
  • 28
    • 0034672426 scopus 로고    scopus 로고
    • Stromal-derived factor 1-induced megakaryocyte migration and plalelet production is dependent on matrix metalloproteinases
    • Lane, W.J., Dias, S., Hattori, K., Heissig, B., Choy, M., Rabbany, S.Y., Wood, J., Moore, M.A. & Rafii, S. (2000) Stromal-derived factor 1-induced megakaryocyte migration and plalelet production is dependent on matrix metalloproteinases. Blood 96, 4152-4159.
    • (2000) Blood , vol.96 , pp. 4152-4159
    • Lane, W.J.1    Dias, S.2    Hattori, K.3    Heissig, B.4    Choy, M.5    Rabbany, S.Y.6    Wood, J.7    Moore, M.A.8    Rafii, S.9
  • 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
    • Van den Steen, P.E., Proost, P., Grillet, B., Brand, D.D., Kang, A.H., Van Damme, J. & Opdenakker, G. (2002) 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) 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
    • 0034806212 scopus 로고    scopus 로고
    • Matrix metalloproteinases regulate neutrophil-endothelial cell adhesion through generation of endothelin-1[1-32]
    • Fernandez-Patron, C., Zouki, C., Whittal, R., Chan, J.S., Davidge, S.T. & Filep, J.G. (2001) Matrix metalloproteinases regulate neutrophil-endothelial cell adhesion through generation of endothelin-1[1-32]. FASEB J. 15, 2230-2240.
    • (2001) FASEB J. , vol.15 , pp. 2230-2240
    • Fernandez-Patron, C.1    Zouki, C.2    Whittal, R.3    Chan, J.S.4    Davidge, S.T.5    Filep, J.G.6
  • 32
    • 0032497366 scopus 로고    scopus 로고
    • Functional comparison of two human monocyte chemotactic protein-2 isoforms, role of the amino-terminal pyroglutamic acid and processing by CD26/dipeptidyl peptidase IV
    • Van Coillie, E., Proost, P., Van Aelst, I., Struyf, S., Polfliet, M., De Meester, I., Harvey, D.J., Van Damme, J. & Opdenakker, G. (1998) Functional comparison of two human monocyte chemotactic protein-2 isoforms, role of the amino-terminal pyroglutamic acid and processing by CD26/dipeptidyl peptidase IV. Biochemistry 37, 12672-12680.
    • (1998) Biochemistry , vol.37 , pp. 12672-12680
    • Van Coillie, E.1    Proost, P.2    Van Aelst, I.3    Struyf, S.4    Polfliet, M.5    De Meester, I.6    Harvey, D.J.7    Van Damme, J.8    Opdenakker, G.9
  • 36
    • 0030669839 scopus 로고    scopus 로고
    • Sequence similarities of a subgroup of CXC chemokines related to murine LIX: Implications for the interpretation of evolutionary relationships among chemokines
    • Smith, J.B., Rovai, L.E. & Herschman, H.R. (1997) Sequence similarities of a subgroup of CXC chemokines related to murine LIX: implications for the interpretation of evolutionary relationships among chemokines. J. Leukoc. Biol. 62, 598-603.
    • (1997) J. Leukoc. Biol. , vol.62 , pp. 598-603
    • Smith, J.B.1    Rovai, L.E.2    Herschman, H.R.3
  • 37
    • 0033547791 scopus 로고    scopus 로고
    • Amino-terminal processing of chemokine ENA-78 regulates biological activity
    • Nufer, O., Corbett, M. & Walz, A. (1999) Amino-terminal processing of chemokine ENA-78 regulates biological activity. Biochemistry 38, 636-442.
    • (1999) Biochemistry , vol.38 , pp. 636-442
    • Nufer, O.1    Corbett, M.2    Walz, A.3
  • 39
    • 0037103183 scopus 로고    scopus 로고
    • Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo
    • McQuibban, G.A., Gong, J.H., Wong, J.P., Wallace, J.L., Clark-Lewis, I. & Overall, C.M. (2002) Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo. Blood 100, 1160-1167.
    • (2002) Blood , vol.100 , pp. 1160-1167
    • McQuibban, G.A.1    Gong, J.H.2    Wong, J.P.3    Wallace, J.L.4    Clark-Lewis, I.5    Overall, C.M.6
  • 40
    • 0028136620 scopus 로고
    • Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3
    • Padrines, M., Wolf M., Walz, A. & Baggiolini, M. (1994) Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3. FEBS Lett. 352, 231-235.
    • (1994) FEBS Lett. , vol.352 , pp. 231-235
    • Padrines, M.1    Wolf, M.2    Walz, A.3    Baggiolini, M.4
  • 41
    • 0026717943 scopus 로고
    • Recombinant tumor necrosis factor-α potentiates neutrophil degranulation in response to host defense cytokines neutrophil-activating peptide 2 and IL-8 by modulating intracellular cyclic AMP levels
    • Brandt, E., Petersen, F. & Flad, H.D. (1992) Recombinant tumor necrosis factor-α potentiates neutrophil degranulation in response to host defense cytokines neutrophil-activating peptide 2 and IL-8 by modulating intracellular cyclic AMP levels. J. Immunol. 149, 1356-1364.
    • (1992) J. Immunol. , vol.149 , pp. 1356-1364
    • Brandt, E.1    Petersen, F.2    Flad, H.D.3
  • 42
    • 0032571360 scopus 로고    scopus 로고
    • Amino-terminal truncation of chemokines by CD26/dipeptidyl-peptidase IV. Conversion of RANTES into a potent inhibitor of monocyte chemotaxis and HIV-1-infection
    • Proost, P., De Meester, I., Schols, D., Struyf, S., Lambeir, A.M., Wuyts, A., Opdenakker, G., De Clercq, E., Scharpé, S. & Van Damme, J. (1998) Amino-terminal truncation of chemokines by CD26/dipeptidyl-peptidase IV. Conversion of RANTES into a potent inhibitor of monocyte chemotaxis and HIV-1-infection. J. Biol. Chem. 273, 7222-7227.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7222-7227
    • Proost, P.1    De Meester, I.2    Schols, D.3    Struyf, S.4    Lambeir, A.M.5    Wuyts, A.6    Opdenakker, G.7    De Clercq, E.8    Scharpé, S.9    Van Damme, J.10
  • 43
    • 0030819309 scopus 로고    scopus 로고
    • Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation, normal T cell expressed and secreted) by dipeptidyl peptidase IV (CD26)-mediated cleavage
    • Oravecz, T., Pall, M., Roderiquez, G., Gorrell, M.D., Ditto, M., Nguyen, N.Y., Boykins, R., Unsworth, E. & Norcross, M.A. (1997) Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation, normal T cell expressed and secreted) by dipeptidyl peptidase IV (CD26)-mediated cleavage. J. Exp. Med. 186, 1865-1872.
    • (1997) J. Exp. Med. , vol.186 , pp. 1865-1872
    • Oravecz, T.1    Pall, M.2    Roderiquez, G.3    Gorrell, M.D.4    Ditto, M.5    Nguyen, N.Y.6    Boykins, R.7    Unsworth, E.8    Norcross, M.A.9
  • 45
    • 0034284379 scopus 로고    scopus 로고
    • Cleavage by CD26/dipeptidyl peptidase IV converts the chemokine LD78β into a most efficient monocyte attractant and CCR1 agonist
    • Proost, P., Menten, P., Struyf, S., Schutyser, E., De Meester, I. & Van Damme, J. (2000) Cleavage by CD26/dipeptidyl peptidase IV converts the chemokine LD78β into a most efficient monocyte attractant and CCR1 agonist. Blood 96, 1674-1680.
    • (2000) Blood , vol.96 , pp. 1674-1680
    • Proost, P.1    Menten, P.2    Struyf, S.3    Schutyser, E.4    De Meester, I.5    Van Damme, J.6
  • 47
    • 0029021473 scopus 로고
    • Monocyte chemotactic protein 1 is released during lethal and sublethal bacteremia in baboons
    • Jansen, P.M., Van Damme, J., Put, W., de Jong, I.W., Taylor, F.B.J. & Hack, C.E. (1995) Monocyte chemotactic protein 1 is released during lethal and sublethal bacteremia in baboons. J. Infect. Dis. 171, 1640-1642.
    • (1995) J. Infect. Dis. , vol.171 , pp. 1640-1642
    • Jansen, P.M.1    Van Damme, J.2    Put, W.3    De Jong, I.W.4    Taylor, F.B.J.5    Hack, C.E.6
  • 54
    • 0026890915 scopus 로고
    • Cytokines and proteases in invasive processes: Molecular similarities between inflammation and cancer
    • Opdenakker, G. & Van Damme, J. (1992) Cytokines and proteases in invasive processes: molecular similarities between inflammation and cancer. Cytokine. 4, 251-258.
    • (1992) Cytokine , vol.4 , pp. 251-258
    • Opdenakker, G.1    Van Damme, J.2
  • 55
    • 0034721666 scopus 로고    scopus 로고
    • MMP-9 supplied by bone marrow-derived cells contributes to skin carcinogenesis
    • Coussens, L.M., Tinkle, C.L., Hanahan, D. & Werb, Z. (2000) MMP-9 supplied by bone marrow-derived cells contributes to skin carcinogenesis. Cell 103, 481-490.
    • (2000) Cell , vol.103 , pp. 481-490
    • Coussens, L.M.1    Tinkle, C.L.2    Hanahan, D.3    Werb, Z.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.