ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitorsq

Biochemical and Biophysical Research Communications

Volumn 293, Issue 1, 2002, Pages 501-508

  Carlos Rodríguez Manzaneque, Juan ^a   Westling, Jennifer ^b   Thai, Shelley N M ^a   Luque, Alfonso ^a   Knauper, Vera ^c   Murphy, Gillian ^c   Sandy, John D ^b,d   Iruela Arispe, M Luisa ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b SHRINERS HOSPITALS FOR CHILDREN   (United States)

^c UNIVERSITY OF EAST ANGLIA   (United Kingdom)

^d UNIVERSITY OF SOUTH FLORIDA   (United States)

Author keywords

ADAMTS; Aggrecan; Extracellular matrix; Metalloproteinase; Proteoglycan

Indexed keywords

AGGRECAN; AGGRECANASE; GLOBULAR PROTEIN; METALLOPROTEINASE INHIBITOR; MONOCLONAL ANTIBODY; MUTANT PROTEIN; PROTEIN; PROTEIN ADAMTS1; PROTEINASE; PROTEOGLYCAN; SCLEROPROTEIN; TISSUE INHIBITOR OF METALLOPROTEINASE 2; TISSUE INHIBITOR OF METALLOPROTEINASE 3; UNCLASSIFIED DRUG; ZINC;

ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SPECIFICITY; HUMAN; HUMAN CELL; MOUSE; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FAMILY;

AGGRECANS; AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; CARTILAGE; CHONDROSARCOMA; DNA PRIMERS; ENZYME INHIBITORS; EXTRACELLULAR MATRIX PROTEINS; HUMANS; LECTINS, C-TYPE; METALLOENDOPEPTIDASES; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; POLYMERASE CHAIN REACTION; PROTEOCHONDROITIN SULFATES; PROTEOGLYCANS; RATS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

EID: 0036295493     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)00254-1     Document Type: Article

References (38)

1. ECM and cell surface proteolysis: Regulating cellular ecology
2. cDNA cloning and expression of bovine procollagen I N-proteinase: A new member of the superfamily of zinc-metalloproreinases with binding sites for cells and other matrix components
3. Purification and cloning of aggrecanase-1: A member of the ADAMTS family of proteins
4. Cloning and characterization of AD-AMTS11, and aggrecanase from the ADAMTS family
5. 373 bond of the interglobular domain
6. ADAMTS-1 cleaves a cartilage proteoglycan aggrecan
7. 442 bond, a site which is cleaved by recombinant ADAMTS-1 and ADAMTS-4
8. Brain-enriched hyaluronan binding (BEHAB)/brevican cleavage in a glioma cell line is mediated by a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) family member
9. ADAMTS-1: A metalloproteinase-disintegrin essential for normal growth fertility and organ morphology and function
10. Transgenic mice with inactive alleles for procollagen N-proteinase (ADAMTS-2) develop fragile skin and male sterility
11. METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity
12. Analysis of the catabolism of aggrecan in cartilage explants by quantitation of peptides from the three globular domains
13. A simplified procedure for measuring amino-procollagen peptidase type I
14. Procollagen type III N-terminal endopeptidase in fibroblast culture
15. Inhibition of angiogenesis by thrombospondin-1 is mediated by 2 independent regions within the type 1 repeats
16. The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene family
17. Chemically and conformationally authentic active domain of human tissue inhibitor of metalloproteinases-2 refolded from bacterial inclusion bodies
18. Characterization of METH-1/ ADAMTS1 processing reveals two distinct active forms
19. Activated conformations of very late activation integrins detected by a group of antibodies (HUTS) specific for a novel regulatory region (355-425) of the common B1 chain
20. Chondrocyte-mediated catabolism of aggrecan: Aggrecanase-dependent cleavage induced by interleukin-1 or retinoic acid can be inhibited by glucosamine
21. The intermediates of aggrecanase-dependent cleavage of aggrecan in rat chondrosarcoma cells treated with interleukin-1
22. Metalloprotease-disintegrin MDC9: Intracellular maturation and catalytic activity
23. An anticatalytic monoclonal antibody to avian plasminogen activator: Its effect on behavior of RSV-transformed chick fibroblast
24. Generation and characterization of aggrecanase. A soluble cartilage-derived aggrecan-degrading activity
25. TIMP-3 is a potent inhibitor of aggrecanase 1 (ADAM-TS4) and aggrecanase 2(ADAM-TS5)
26. Inhibition of ADAMTS4 (aggrecanase-1) by tissue inhibitors of metalloproteinases (TIMP-1, 2, 3, and 4)
27. On the size of the active site in proteases. I. Papain
28. Sites of aggrecan cleavage by recombinant human aggrecanase-1 (ADAMTS-4)
29. Aggrecanase. A target for the design of inhibitors of cartilage degradation
30. Intact aggrecan and fragments generated by both aggrecanase and metalloproteinase-like activities are present in the developing and adult rat spinal cord and their relative abundance is altered by injury
31. Expression of ADAMTS homologues in articular cartilage
32. A disintegrin and metalloprotease with thrombospondin type 1 motifs (ADAMTS-1) and IL-1 receptor type 1 mRNAs are simultaneously induced in nerve injured motor neurons
33. 342) in the aggrecan interglobular domain
34. Glycation induced crosslinking of link proteins in vivo and in vitro
35. Analysis of aggrecan in human knee cartilage and synovial fluid indicates that aggrecanase (ADAMTS) activity is responsible for the catabolic turnover and loss of whole aggrecan whereas MMP-like activity is required primarily for C-terminal processing of the molecule
36. Identification of a stromelysin cleavage site within the interglobular domain of human aggrecan. Evidence for proteolysis at this site in vivo in human articular cartilage
37. Cathepsin B: An alternative protease for the generation of an aggrecan metalloproteinase cleavage neoepitope
38. Matrix proteoglycans: From molecular design to cellular function