PREFERENTIAL INACTIVATION OF TISSUE INHIBITOR OF METALLOPROTEINASES-1 THAT IS BOUND TO THE PRECURSOR OF MATRIX METALLOPROTEINASE-9 (PROGELATINASE-B) BY HUMAN NEUTROPHIL ELASTASE

被引:140
作者
ITOH, Y [1 ]
NAGASE, H [1 ]
机构
[1] UNIV KANSAS,MED CTR,DEPT BIOCHEM & MOLEC BIOL,KANSAS CITY,KS 66160
关键词
D O I
10.1074/jbc.270.28.16518
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The precursor of matrix metalloproteinase 9 (pro-MMP-9) forms a complex with the tissue inhibitor of metalloproteinases (TIMP)-1 through the C-terminal domain of each molecule, and the N-terminal domain of TIMP-1 in the complex interacts and inhibits active MMPs. We have reported that a catalytic amount of MMP-3 (stromelysin 1) activates pro-MMP-9 (Ogata, Y., Enghild, J. J., and Nagase, H. (1992) J. Biol. Chem. 267, 3581-3584). To activate pro-MMP-9 in the complex, however, an excess molar amount of MMP-3 is required to saturate the TIMP-1 in the complex. The aim of this study was to test the hypothesis that the requirement for excess MMP-3 can be circumvented by specific destruction of TIMP-1 by non-target proteinases. We have tested trypsin, plasmin, cathepsin G, neutrophil elastase, and chymotrypsin as possible inactivators of TIMP-1 and found that neutrophil elastase inactivates TIMP-1 in the complex without significant destruction of pro-MMP-9. Once TIMP-1 is inactivated, pro MMP-9 can be readily activated by a catalytic amount of MMP-3. These results suggest that neutrophil elastase may participate in connective tissue destruction at the inflammatory sites not only by its direct action on matrix macromolecules but also by rendering pro-MMP-9 in the pro-MMP-9 . TIMP-1 complex activable by MMP-3 as well as activating pro MMP-3.
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页码:16518 / 16521
页数:4
相关论文
共 39 条
  • [1] MATRIX METALLOPROTEINASES - A REVIEW
    BIRKEDALHANSEN, H
    MOORE, WGI
    BODDEN, MK
    WINDSOR, LJ
    BIRKEDALHANSEN, B
    DECARLO, A
    ENGLER, JA
    [J]. CRITICAL REVIEWS IN ORAL BIOLOGY & MEDICINE, 1993, 4 (02) : 197 - 250
  • [2] RAPID AND REPRODUCIBLE ASSAY FOR COLLAGENASE USING [ACETYLATED-1-C-14 COLLAGEN
    CAWSTON, TE
    BARRETT, AJ
    [J]. ANALYTICAL BIOCHEMISTRY, 1979, 99 (02) : 340 - 345
  • [3] FOSANG AJ, 1992, J BIOL CHEM, V267, P19470
  • [4] GOLDBERG GI, 1992, J BIOL CHEM, V267, P4583
  • [5] ENDOPEPTIDASE FROM RHEUMATOID SYNOVIAL TISSUE-CULTURE
    HARRIS, ED
    KRANE, SM
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1972, 258 (02) : 566 - +
  • [6] EXPRESSION OF A METALLOPROTEINASE THAT DEGRADES NATIVE TYPE-V COLLAGEN AND DENATURED COLLAGENS BY CULTURED HUMAN ALVEOLAR MACROPHAGES
    HIBBS, MS
    HOIDAL, JR
    KANG, AH
    [J]. JOURNAL OF CLINICAL INVESTIGATION, 1987, 80 (06) : 1644 - 1650
  • [7] EVIDENCE THAT HUMAN RHEUMATOID SYNOVIAL MATRIX METALLOPROTEINASE-3 IS AN ENDOGENOUS ACTIVATOR OF PROCOLLAGENASE
    ITO, A
    NAGASE, H
    [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1988, 267 (01) : 211 - 216
  • [8] JOHNSON DA, 1986, J BIOL CHEM, V261, P4748
  • [9] PRODUCTION OF GELATIN-DEGRADING MATRIX METALLOPROTEINASES (TYPE-IV COLLAGENASES) AND INHIBITORS BY ARTICULAR CHONDROCYTES DURING THEIR DEDIFFERENTIATION BY SERIAL SUBCULTURES AND UNDER STIMULATION BY INTERLEUKIN-1 AND TUMOR-NECROSIS-FACTOR-ALPHA
    LEFEBVRE, V
    PEETERSJORIS, C
    VAES, G
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1991, 1094 (01) : 8 - 18
  • [10] 92-KD TYPE-IV COLLAGENASE MEDIATES INVASION OF HUMAN CYTOTROPHOBLASTS
    LIBRACH, CL
    WERB, Z
    FITZGERALD, ML
    CHIU, K
    CORWIN, NM
    ESTEVES, RA
    GROBELNY, D
    GALARDY, R
    DAMSKY, CH
    FISHER, SJ
    [J]. JOURNAL OF CELL BIOLOGY, 1991, 113 (02) : 437 - 449