The slow-binding inhibition of cathepsin K by its propeptide

Biochemical and Biophysical Research Communications

Volumn 276, Issue 3, 2000, Pages 924-929

  Billington, Caron J ^a   Mason, Patrizia ^a   Magny, Marie Claude ^a   Mort, John S ^a  

^a SHRINERS HOSPITAL FOR CHILDREN   (Canada)

Author keywords

Cathepsin K; Propeptide; Slow binding inhibition

Indexed keywords

CATHEPSIN K; COMPLEMENTARY DNA; CYSTEINE PROTEINASE INHIBITOR;

ARTICLE; CIRCULAR DICHROISM; DISSOCIATION CONSTANT; ENZYME BINDING; ENZYME KINETICS; ESCHERICHIA COLI; GENE EXPRESSION; NONHUMAN; PH; PRIORITY JOURNAL;

EID: 0034610021     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2000.3553     Document Type: Article

References (28)

1. Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary. Molecular cloning, sequencing and tissue distribution
2. Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts
3. Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix
4. The collagenolytic activity of cathepsin K is unique among mammalian proteinases
5. Proteolysis of human bone collagen by cathepsin K: Characterization of the cleavage sites generating the cross-linked N-telopeptide neoepitope
6. Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency
7. Novel mutations of the cathepsin K gene in patients with pycnodysostosis and their characterization
8. Characterization of novel cathepsin K mutations in the pro and mature polypeptide regions causing pycnodysostosis
9. Cathepsin K knockout mice develop osteopetrosis due to a deficit in matrix degradation but not demineralization
10. Peptide aldehyde inhibitors of cathepsin K inhibit bone resorption both in vitro and in vivo
11. Design of potent and selective human cathepsin K inhibitors that span the active site
12. Cysteine proteinase cathepsin K mRNA is expressed in synovium of patients with rheumatoid arthritis and is detected at sites of synovial bone destruction
13. The proregion of cathepsin L is required for proper folding, stability, and ER exit
14. Potent slow-binding inhibition of cathepsin B by its propeptide
15. Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases
16. The inhibition of cathepsin S by its propeptide - Specificity and mechanism of action
17. Interdependency of sequence and positional specificities for cysteine proteases of the papain family
18. Major increase in endopeptidase activity of human cathepsin B upon removal of occluding loop contacts
19. Crystal structure of wild-type human procathepsin K
20. The crystal structure of human procathepsin K
21. Two distinct gene subfamilies within the family of cysteine protease genes
22. Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment
23. The prosequence of procaricain forms an α-helical domain that prevents access to the substrate-binding cleft
24. The alpha1/2 helical backbone of the prodomains defines the intrinsic inhibitory specificity in the cathepsin L-like cysteine protease subfamily
25. Inhibition of trypanosomal cysteine proteinases by their propeptides
26. pH-induced conformational transitions of the propeptide of human cathepsin L. A role for a molten globule state in zymogen activation
27. Proteolytic activity of human osteoclast cathepsin K. Expression, purification, activation, and substrate identification
28. Autocatalytic activation of human cathepsin K