메뉴 건너뛰기




Volumn 97, Issue 7, 1996, Pages 1589-1596

Dog mastocytoma cells secrete a 92-kD gelatinase activated extracellularly by mast cell chymase

Author keywords

degranulation; enzyme activation; mast cell; matrix metalloproteinase; serine protease

Indexed keywords

CHYMASE; GELATINASE;

EID: 0029995317     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI118583     Document Type: Article
Times cited : (117)

References (39)
  • 1
    • 0025096722 scopus 로고
    • Multiple modes of activation of latent fibroblast collagcnase: Evidence for the role of a Cys 73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation
    • Springman, E.B., E.L Angelton, H. Birkedal-Hansen, and H.E. Van Wart. 1990 Multiple modes of activation of latent fibroblast collagcnase: evidence for the role of a Cys 73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation. Proc. Natl. Acad. Sci. USA 87:364-368
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 364-368
    • Springman, E.B.1    Angelton, E.L.2    Birkedal-Hansen, H.3    Van Wart, H.E.4
  • 2
    • 0020494591 scopus 로고
    • Detergent-activation of latent collagenase and resolution of its component molecules
    • Birkedal-Hansen, H., and R.E. Taylor. 1982. Detergent-activation of latent collagenase and resolution of its component molecules. Biochem. Biophys. Res Commun. 107:1173-1178.
    • (1982) Biochem. Biophys. Res Commun. , vol.107 , pp. 1173-1178
    • Birkedal-Hansen, H.1    Taylor, R.E.2
  • 3
    • 0004553618 scopus 로고
    • Tissue cooperation in a proteolytic cascade activating human interstitial collagenase
    • He, C., S.M Wilhelm, and A.P. Pentland. 1989. Tissue cooperation in a proteolytic cascade activating human interstitial collagenase. Proc. Natl. Acad. Sci. USA. 66:2632-2636.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.66 , pp. 2632-2636
    • He, C.1    Wilhelm, S.M.2    Pentland, A.P.3
  • 4
    • 0026660964 scopus 로고
    • Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9
    • Ogata, Y., J.J Enghild, and H Nagase. 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
  • 5
    • 0025026410 scopus 로고
    • Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromeiysin)
    • Suzuki, K., J.J Enghild, T. Morodomi, G Salvesen, and H. Nagase. 1990. Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromeiysin). Biochemistry. 29:10261-10270.
    • (1990) Biochemistry , vol.29 , pp. 10261-10270
    • Suzuki, K.1    Enghild, J.J.2    Morodomi, T.3    Salvesen, G.4    Nagase, H.5
  • 7
    • 0024429920 scopus 로고
    • Synovial procollagenase activation by human mast cell tryptase dependence upon matrix metalloproteinase 3 activation
    • Gruber, B.L , M.J. Marchese, K. Suzuki, L.B. Schwartz, Y. Okada, H. Nagase, and N.S. Ramamurthy. 1989. Synovial procollagenase activation by human mast cell tryptase dependence upon matrix metalloproteinase 3 activation. J. Clin. Invest. 84:1657-1662.
    • (1989) J. Clin. Invest. , vol.84 , pp. 1657-1662
    • Gruber, B.L.1    Marchese, M.J.2    Suzuki, K.3    Schwartz, L.B.4    Okada, Y.5    Nagase, H.6    Ramamurthy, N.S.7
  • 8
    • 0028302145 scopus 로고
    • Mast cell proteinases activate precursor forms of collagenase and stromelysin, but not of gelatinases A and B
    • Lees, M , D.J. Taylor, and D.E. Woolley. 1994. Mast cell proteinases activate precursor forms of collagenase and stromelysin, but not of gelatinases A and B. Eur. J. Biochem. 223:171-177.
    • (1994) Eur. J. Biochem. , vol.223 , pp. 171-177
    • Lees, M.1    Taylor, D.J.2    Woolley, D.E.3
  • 9
    • 0028363122 scopus 로고
    • Human mast cell tryptase activates single-chain urinary-type plasminogen activator (pro urokinase)
    • Stack, M., and D. Johnson. 1994. Human mast cell tryptase activates single-chain urinary-type plasminogen activator (pro urokinase). J. Biol. Chem. 269:9416-9419.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9416-9419
    • Stack, M.1    Johnson, D.2
  • 11
    • 0018358936 scopus 로고
    • Ultrastructure of pulmonary mast cells in patients with fibrolic lung disorders
    • Kawanarai, O., V.J. Ferrans, J D. Fulmer. and R.G. Crystal. 1979. Ultrastructure of pulmonary mast cells in patients with fibrolic lung disorders Lab. Invest. 40:717-734.
    • (1979) Lab. Invest. , vol.40 , pp. 717-734
    • Kawanarai, O.1    Ferrans, V.J.2    Fulmer, J.D.3    Crystal, R.G.4
  • 14
  • 15
    • 0024299058 scopus 로고
    • Purification and characterization of dog mastocytoma chymase: Identification of an octapeptide conserved in chytnotryptic leukocyte proteinases
    • Caughey, G.H., N F. Viro, S.C. Lazarus, and J.A. Nadel. 1988. Purification and characterization of dog mastocytoma chymase: identification of an octapeptide conserved in chytnotryptic leukocyte proteinases. Biochim. Biophys. Acta. 952.142-149.
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 142-149
    • Caughey, G.H.1    Viro, N.F.2    Lazarus, S.C.3    Nadel, J.A.4
  • 17
    • 0029042981 scopus 로고
    • Purification and characterization of dog mast cell protease-3, an oligomeric relative of tryptases
    • Raymond, W., E. Tam, J. Blount, and G. Caughey. 1995. Purification and characterization of dog mast cell protease-3, an oligomeric relative of tryptases. J Biol. Chem. 270:13164-13170.
    • (1995) J Biol. Chem. , vol.270 , pp. 13164-13170
    • Raymond, W.1    Tam, E.2    Blount, J.3    Caughey, G.4
  • 18
    • 0021918104 scopus 로고
    • Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase
    • Hibbs, M.S., K.A. Hasty, J.S. Seyer, A.H. Kang, and C.L. Mainardi. 1985. Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase. J. Biol. Chem. 260:2493-2500.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2493-2500
    • Hibbs, M.S.1    Hasty, K.A.2    Seyer, J.S.3    Kang, A.H.4    Mainardi, C.L.5
  • 19
    • 0023022058 scopus 로고
    • Properties of radiolabeled type I, II, and III collagens related to their use as substrates in collagenase assays
    • Mookhtiar, K.A., S.K. Mallya, and H.E. Van Wart. 1986. Properties of radiolabeled type I, II, and III collagens related to their use as substrates in collagenase assays. Anal. Biochem 158:322-333.
    • (1986) Anal. Biochem , vol.158 , pp. 322-333
    • Mookhtiar, K.A.1    Mallya, S.K.2    Van Wart, H.E.3
  • 20
    • 0029146477 scopus 로고
    • Neutrophil elastase processing of gelatinase A is mediated by extracellular matrix
    • Rice, A., and M.J. Banda. 1995. Neutrophil elastase processing of gelatinase A is mediated by extracellular matrix. Biochemistry. 34:9249-9256.
    • (1995) Biochemistry. , vol.34 , pp. 9249-9256
    • Rice, A.1    Banda, M.J.2
  • 21
    • 0027759314 scopus 로고
    • Bis(5-amidino-2-benzimidazolyl)methane and related amidines are potent, reversible inhibitors of mast cell tryptases
    • Caughey, G.H., W.W. Raymond, E. Bacci, R.J. Lombardy, and R R. Tidwell. 1993. Bis(5-amidino-2-benzimidazolyl)methane and related amidines are potent, reversible inhibitors of mast cell tryptases. J. Pharmacol. Exp. Ther 264:676-682.
    • (1993) J. Pharmacol. Exp. Ther , vol.264 , pp. 676-682
    • Caughey, G.H.1    Raymond, W.W.2    Bacci, E.3    Lombardy, R.J.4    Tidwell, R.R.5
  • 22
    • 0006506596 scopus 로고
    • Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2
    • Goldberg, G.I., B.L. Marmer, G.A. Grant, A.Z. Eisen. S. Wilhelm, and C. He. 1989. Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2. Proc. Natl. Acad. Sci USA. 86:8207-8211.
    • (1989) Proc. Natl. Acad. Sci USA , vol.86 , pp. 8207-8211
    • Goldberg, G.I.1    Marmer, B.L.2    Grant, G.A.3    Eisen, A.Z.4    Wilhelm, S.5    He, C.6
  • 23
    • 0024394212 scopus 로고
    • Tissue inhibitor of metalloproteinase (TIMP-2): A new member of the metalloproteinase inhibitor family
    • Stetler-Stevenson, W.G., H.C. Krutzsch, and L.A. Liotta. 1989. Tissue inhibitor of metalloproteinase (TIMP-2): a new member of the metalloproteinase inhibitor family. J. Biol. Chem. 264:17374-17378.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17374-17378
    • Stetler-Stevenson, W.G.1    Krutzsch, H.C.2    Liotta, L.A.3
  • 24
    • 0026465338 scopus 로고
    • Role of the 21-kDa protein TIMP-3 in oncogenic transformation of cultured chicken embryo fibroblasts
    • Yang, T.-T., and S.P. Hawkes. 1992. Role of the 21-kDa protein TIMP-3 in oncogenic transformation of cultured chicken embryo fibroblasts. Proc. Natl Acad Sci. USA. 89:10676-10680.
    • (1992) Proc. Natl Acad Sci. USA , vol.89 , pp. 10676-10680
    • Yang, T.-T.1    Hawkes, S.P.2
  • 25
    • 0027256664 scopus 로고
    • Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase
    • Kjeldsen, L., A.H. Johnsen, H. Sengelov, and N. Borregaard. 1993. Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase. J. Biol. Chem. 268:10425-10432.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10425-10432
    • Kjeldsen, L.1    Johnsen, A.H.2    Sengelov, H.3    Borregaard, N.4
  • 26
    • 0024330327 scopus 로고
    • SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages
    • Wilhelm, S.M., I.E. Collier, B.L. Marmer, A.Z. Eisen, G.A. Grant, and G.I. Goldberg. 1989. SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages. J. Biol. Chem. 264:17213-17221
    • (1989) J. Biol. Chem. , vol.264 , pp. 17213-17221
    • Wilhelm, S.M.1    Collier, I.E.2    Marmer, B.L.3    Eisen, A.Z.4    Grant, G.A.5    Goldberg, G.I.6
  • 29
    • 0025340185 scopus 로고
    • Structure of the human type IV collagenase gene
    • Huhtala, P., L. Chow, and K. Tryggvason. 1990. Structure of the human type IV collagenase gene. J. Biol Chem. 265:11077-11082.
    • (1990) J. Biol Chem. , vol.265 , pp. 11077-11082
    • Huhtala, P.1    Chow, L.2    Tryggvason, K.3
  • 30
    • 0025025442 scopus 로고
    • The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • Van Wart, H.E., and H. Birkedal-Hansen. 1990 The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl. Acad. Sci USA. 87.5578-5582.
    • (1990) Proc. Natl. Acad. Sci USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 32
    • 0025230509 scopus 로고
    • Metalloproteinases and their inhibitors in matrix remodeling
    • Matrisian, L.M. 1990. Metalloproteinases and their inhibitors in matrix remodeling. Trends Genet. 6:21-125.
    • (1990) Trends Genet. , vol.6 , pp. 21-125
    • Matrisian, L.M.1
  • 36
    • 0027420678 scopus 로고
    • Structural and functional heterogeneity among peroxidase-negative granules in human neutrophils: Identification of a distinct gelatinase-containing granule subset by combined immunocytochemistry and subcellular fractionation
    • Kjeldsen, L., D F. Bainton, H. Sengelov, and N. Borregaard. 1993. Structural and functional heterogeneity among peroxidase-negative granules in human neutrophils: identification of a distinct gelatinase-containing granule subset by combined immunocytochemistry and subcellular fractionation. Blood. 82:3183-3191.
    • (1993) Blood , vol.82 , pp. 3183-3191
    • Kjeldsen, L.1    Bainton, D.F.2    Sengelov, H.3    Borregaard, N.4
  • 37
    • 0029014101 scopus 로고
    • Furin-dependent intracellular activation of the human stromelysin-3 zymogen
    • Pei, D.. and S. Weiss. 1995. Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature (Loind ). 375 244-247.
    • (1995) Nature (Loind ) , vol.375 , pp. 244-247
    • Pei, D.1    Weiss, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.