Structural biochemistry and activation of matrix metalloproteases

Current Opinion in Cell Biology

Volumn 5, Issue 5, 1993, Pages 891-897

  Kleiner Jr , David E ^a   Stetler Stevenson, William G ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN; METALLOPROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE;

AMINO ACID SEQUENCE; ANIMAL; BINDING SITE; ENZYMOLOGY; EXON; EXTRACELLULAR MATRIX; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; REVIEW;

AMINO ACID SEQUENCE; ANIMAL; BINDING SITES; EXONS; EXTRACELLULAR MATRIX; GLYCOPROTEINS; HUMAN; METALLOENDOPEPTIDASES; MOLECULAR SEQUENCE DATA; TISSUE INHIBITOR OF METALLOPROTEINASES;

EID: 0027683226     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/0955-0674(93)90040-W     Document Type: Article

References (45)

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3. Matrix Metalloproteinases and Their Inhibitors in Connective Tissue Remodeling
4. Matrix Metalloproteinases: A Review
5. Nomenclature and Glossary of the Matrix Metalloproteinases
6. A Novel Metalloproteinase Gene Specifically Expressed in Stromal Cells of Breast Carcinoma
7. Expression of the stromelysin-3 gene in fibroblastic cells of invasive carcinomas of the breast and other human tissues: a review
8. On the Structure and Chromosome Location of the 72- and 92-kDa Human Type IV Collagenase Genes
9. Complete Structure of the Human Gene for 92-kDa Type IV Collagenas. Divergent Regulation of Expression for the 92- and 72-kilodalton Enzymes Genes in HT-1080 Cells
10. The Matrix-Degrading Metalloproteinases
11. Stepwise Activation Mechanisms of the Precursor of Matrix Metalloproteinase 3 (Stromelysin) by Proteinases and (4-Aminophenyl) Mercuric Acetate
12. Multiple Modes of Activation of Latent Human Fibroblast Collagenase — Evidence for the Role of a Cys-73 Active-Site Zinc Complex in Latency and a Cysteine Switch Mechanism for Activation
13. Mutational Analysis of the Transin (Rat Stromelysin) Autoinhibitor Region Demonstrates a Role for Residues Surrounding the ‘Cysteine Switch’
14. Inhibition of Human Type IV Collagenase by a Highly Conserved Peptide Sequence Derived from Its Prosegment
15. Stereo-Specific Inhibition of Sea Urchin Envelysin (Hatching Enzyme) by a Synthetic Autoinhibitor Peptide with a Cysteine-Switch Consensus Sequence
16. Inhibition of Tumor Cell Invasion by a Highly Conserved Peptide Sequence from the Matrix Metalloproteinase Enzyme Prosegment
17. Characterization of Zinc-Binding Sites in Human Stromelysin-1 — Stoichiometry of the Catalytic Domain and Identification of a Cysteine Ligand in the Proenzyme
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19. The Role of the C-Terminal Domain in Collagenase and Stromelysin Specificity
20. Role of Zinc-Binding and Hemopexin Domain-Encoded Sequences in the Substrate Specificity of Collagenase and Stromelysin-2 as Revealed by Chimeric Proteins
21. The Recombinant Catalytic Domain of Human Neutrophil Collagenase Lacks Type I Collagen Substrate Specificity
22. Domain Structure of Human 72-kDa Gelatinase/Type IV Collagenase. Characterization of Proteolytic Activity and Identification of the Tissue Inhibitor of Metalloproteinase-2 (TIMP-2) Binding Regions
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. Sequence of Human Tissue Inhibitor of Metalloproteinases and Its Identity to Erythroid-Potentiating Activity
25. Purification and Characterization of Two Related but Distinct Metalloproteinase Inhibitors Secreted by Bovine Aortic Endothelial Cells
26. Tissue Inhibitor of Metalloproteinase (TIMP-2): A New Member of the Metalloproteinase Inhibitor Family
27. A New Inhibitor of Metalloproteinases from Chicken: ChIMP-3. A Third Member of the TIMP Family
28. Disulphide Bond Assignment in Human Tissue Inhibitor of Metalloproteinases (TIMP)
29. Human 72-Kilodalton Type IV Collagenase Forms a Complex with a Tissue Inhibitor of Metalloproteinases Designated TIMP-2
30. SV40-Transformed Human Lung Fibroblasts Secrete a 92-kDa Type IV Collagenase Which is Identical to That Secreted by Normal Human Macrophages
31. The N-Terminal Domain of Tissue Inhibitor of Metalloproteinases Retains Metalloproteinase Inhibitory Activity
32. Characterization of the Functional Domain of Tissue Inhibitor of Metalloproteinases-2 (TIMP-2)
33. Site-Directed Mutations That Alter the Inhibitory Activity of the Tissue Inhibitor of Metalloproteinases-1: Importance of the N-Terminal Region Between Cysteine 3 and Cysteine 13
34. The Activation of Human Type IV Collagenase Proenzyme. Sequence Identification of the Major Conversion Product Following Organomercurial Activation
35. Higher-Order Complex Formation Between the 72-Kilodalton Type IV Collagenase and Tissue Inhibitor of Metalloproteinases-2
36. Stability Analysis of Latent and Active 72-kDa Type IV Collagenase: The Role of Tissue Inhibitor of Metalloproteinases-2 (TIMP-2)
37. The Complex Between a Tissue Inhibitor of Metalloproteinases (TIMP-2) and 72-kDa Progelatinase is a Metalloproteinase Inhibitor
38. Large Inhibitor of Metalloproteinases (LIMP) Contains Tissue Inhibitor of Metalloproteinases (TIMP)-2 Bound to 72,000-M(r) Progelatinase
39. Interaction of 92-kDa Type IV Collagenase with the Tissue Inhibitor of Metalloproteinases Prevents Dimerization, Complex Formation with Interstitial Collagenase and Activation of the Proenzyme with Stromelysin
40. Secretion of Basement Membrane Collagen Degrading Enzyme and Plasminogen Activator by Transformed Cells — Role in Metastasis
41. Proteolytic Processing of the 72,000-Da Type IV Collagenase by Urokinase Plasminogen Activator
42. Independent Expression and Cellular Processing of Mr 72,000 Type IV Collagenase and Interstitial Collagenase in Human Tumorigenic Cell Lines
43. Cell-Mediated Degradation of Type IV Collagen and Gelatin Films is Dependent on the Activation of Matrix Metalloproteinases
44. Cellular Activation of the 72 kDa Type-IV Procollagenase/TIMP-2 Complex
45. Tumor Cell Surface-Associated Binding Site for the M(r) 72,000 Type IV Collagenase