Engineering N-terminal domain of tissue inhibitor of metalloproteinase (TIMP)-3 to be a better inhibitor against tumour necrosis factor-α-converting enzyme

Biochemical Journal

Volumn 364, Issue 1, 2002, Pages 227-234

  Lee, Meng Huee ^a   Verma, Vandana ^a   Maskos, Klaus ^a   Nath, Deepa ^a   Knäuper, Vera ^a   Dodds, Philippa ^a   Amour, Augustin ^a   Murphy, Gillian ^a  

^a UNIVERSITY OF EAST ANGLIA   (United Kingdom)

Author keywords

Binding affinity; Gelatinase A; N terminal domain of TIMP 3; TACE

Indexed keywords

ENZYMES; MUTAGENS; TISSUE;

CELLULAR INHIBITION;

BIOCHEMISTRY;

GUANIDINE; TISSUE INHIBITOR OF METALLOPROTEINASE 3; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING KINETICS; BINDING SITE; ENZYME INHIBITION; FLUOROMETRY; GENE MUTATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN PURIFICATION;

EID: 0037093362     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/bj3640227     Document Type: Article

References (33)

1. Matrix metalloproteinases and processing of pro-TNF-α
2. Regulation of tumour necrosis factor-α processing by a metalloproteinase inhibitor
3. Relaxed specificity of matrix metalloproteinases (MMPs) and TIMP insensitivity of tumor necrosis factor-α (TNF-α) production suggest the major TNF-α converting enzyme is not an MMP
4. Tumor necrosis, cachexia, shock and inflammation: A common mediator
5. A metalloproteinase disintegrin that releases tumor-necrosis factor-α from cells
6. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α
7. Tissue inhibitor of metalloproteinases-3 inhibits shedding of L-selectin from leukocytes
8. Human myeloma cells shed the interleukin-6 receptor: Inhibition by tissue inhibitor of metalloproteinase-3 and hydroxamate-based metalloproteinase inhibitor
9. Tumour necrosis factor-α converting enzyme (ADAM-17) mediates cleavage and shedding of fractalkine (CX3CL1)
10. Differential shedding of transmembrane neuregulin isoforms by the tumor necrosis factor-α converting enzyme
11. Tumor necrosis factor-α converting enzyme is required for cleavage of erbB4/HER4
12. TNF-α converting enzyme (TACE) is inhibited by TIMP-3
13. Full-length and N-TIMP-3 display equal inhibitory activities towards TNF-α convertase
14. NMR structure of tissue inhibitor of metalloproteinases-1 implicates localized induced fit recognition of matrix metalloproteinases
15. Three-dimensional structure of human tissue inhibitor of metalloproteinases-2 at 2.1 Å resolution
16. High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3
17. The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity
18. Different domain interactions are involved in the binding of tissue inhibitors of metalloproteinases to stromelysin-1 and gelatinase A
19. The specificity of TIMP-2 for matrix metalloproteinases can be modified by single amino add mutations
20. TIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix
21. Inhibition of matrix metalloproteinases, therapeutic applications. Special issue
22. The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene family
23. The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases
24. Specific sequence elements are required for the expression of functional tumor necrosis factor α-converting enzyme (TACE)
25. TIMP-3 is a potent inhibitor of aggrecanase-1 (ADAM-TS4) and aggrecanase-2 (ADAM-TS5)
26. Crystal structure of the catalytic domain of human tumour necrosis factor-α-converting enzyme
27. Shedding of c-met is regulated by crosstalk between a G-protein coupled receptor and the EGF receptor and is mediated by a TIMP-3 sensitive metalloproteinase
28. The in vitro activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3
29. Shedding of syndecan-1 and -4 ectodomains is regulated by multiple signaling pathways and mediated by a TIMP-3 sensitive metalloproteinase
30. ADAM-12S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3
31. Expression and enzymatic activity of human disintegrin and metalloprteinase ADAM 19/meltrin-β
32. Methotrexate, a high affinity pseudosubstrate of dihydrofolate reductase
33. Localization of the functional domains of human tissue inhibitor of metalloproteinase-3 and the effects of a Sorby's fundus dystrophy mutation