Literature DB >> 1646720

The complex between a tissue inhibitor of metalloproteinases (TIMP-2) and 72-kDa progelatinase is a metalloproteinase inhibitor.

H Kolkenbrock1, D Orgel, A Hecker-Kia, W Noack, N Ulbrich.   

Abstract

Human rheumatoid synovial cells in culture secrete both 72-kDa progelatinase and a complex consisting of 72-kDa progelatinase and a 24-kDa inhibitor of metalloproteinases, TIMP-2. In addition, the culture medium contains TIMP-1, the classical inhibitor of metalloproteinases, with a molecular mass of 30 kDa. TIMP-1 does not form a complex with free 72-kDa progelatinase. Free progelatinase and progelatinase complexed with TIMP-2 can be activated with the organomercury compound p-aminophenylmercury acetate. The activated complex shows less than 10% the enzyme activity of activated free gelatinase. The progelatinase-TIMP-2 complex could be shown to be an inhibitor for other metalloproteinases, such as gelatinase and collagenase secreted by human rheumatoid synovia fibroblasts, as well as for the corresponding enzymes from human neutrophils.

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Year:  1991        PMID： 1646720     DOI： 10.1111/j.1432-1033.1991.tb16080.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN： 0014-2956


  18 in total

1.  Tissue inhibitor of metalloproteinase-1 and -2 RNA expression in rat and human liver fibrosis.

Authors:  H Herbst; T Wege; S Milani; G Pellegrini; H D Orzechowski; W O Bechstein; P Neuhaus; A M Gressner; D Schuppan
Journal:  Am J Pathol       Date:  1997-05       Impact factor: 4.307

Review 2.  Matrix Metalloproteinases, Vascular Remodeling, and Vascular Disease.

Authors:  Xi Wang; Raouf A Khalil
Journal:  Adv Pharmacol       Date:  2017-09-19

3.  Augmentation by eosinophils of gelatinase activity in the airway mucosa: comparative effects as a putative mediator of epithelial injury.

Authors:  C A Herbert; M J Arthur; C Robinson
Journal:  Br J Pharmacol       Date:  1996-02       Impact factor: 8.739

4.  Decreased homodimerization and increased TIMP-1 complexation of uteroplacental and uterine arterial matrix metalloproteinase-9 during hypertension-in-pregnancy.

Authors:  Juanjuan Chen; Zongli Ren; Minglin Zhu; Raouf A Khalil
Journal:  Biochem Pharmacol       Date:  2017-05-12       Impact factor: 5.858

5.  Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2.

Authors:  Ekaterina Morgunova; Ari Tuuttila; Ulrich Bergmann; Karl Tryggvason
Journal:  Proc Natl Acad Sci U S A       Date:  2002-05-28       Impact factor: 11.205

6.  Large inhibitor of metalloproteinases (LIMP) contains tissue inhibitor of metalloproteinases (TIMP)-2 bound to 72,000-M(r) progelatinase.

Authors:  V A Curry; I M Clark; H Bigg; T E Cawston
Journal:  Biochem J       Date:  1992-07-01       Impact factor: 3.857

7.  Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor.

Authors:  C Fernandez-Catalan; W Bode; R Huber; D Turk; J J Calvete; A Lichte; H Tschesche; K Maskos
Journal:  EMBO J       Date:  1998-09-01       Impact factor: 11.598

8.  Identification of tissue inhibitor of metalloproteinase-2 (TIMP-2)-progelatinase complex as the third metalloproteinase inhibitor peak in rheumatoid synovial fluid.

Authors:  T E Cawston; H F Bigg; I M Clark; B L Hazleman
Journal:  Ann Rheum Dis       Date:  1993-03       Impact factor: 19.103

9.  Identification, purification and partial characterization of tissue inhibitor of matrix metalloproteinase-2 in bovine pulmonary artery smooth muscle.

Authors:  Malay Mandal; Amritlal Mandal; Sudip Das; Tapati Chakraborti; Sajal Chakraborti
Journal:  Mol Cell Biochem       Date:  2003-12       Impact factor: 3.396

Review 10.  Role of matrix metalloproteinases in invasion and metastasis: biology, diagnosis and inhibitors.

Authors:  S McDonnell; B Fingleton
Journal:  Cytotechnology       Date:  1993       Impact factor: 2.058
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