Structural basis of collagen fiber degradation by cathepsin K

Proceedings of the National Academy of Sciences of the United States of America

Volumn 111, Issue 49, 2014, Pages 17474-17479

  Aguda, Adeleke H ^a,b   Panwar, Preety ^a,b   Du, Xin ^b   Nguyen, Nham T ^b   Brayer, Gary D ^b   Brömme, Dieter ^a,b  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

Cathepsin K; Collagen; Enzyme mechanism; Glycosaminoglycan

Indexed keywords

AMINO ACID; CATHEPSIN K; COLLAGEN; DIMER; FIBRILLAR COLLAGEN; GAG PROTEIN; GELATIN; GLYCOSAMINOGLYCAN; PROTEINASE; SYNTHETIC PEPTIDE; TROPOCOLLAGEN; PEPTIDE HYDROLASE;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; COLLAGEN DEGRADATION; COLLAGEN FIBER; HYDROLYSIS; MOLECULAR MODEL; MUTATION; PROTEIN BINDING; PROTEIN CLEAVAGE; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN UNFOLDING; SCANNING ELECTRON MICROSCOPY; BONE; BONE REMODELING; CHEMICAL STRUCTURE; CHEMISTRY; ELECTRON MICROSCOPY; ENZYME SPECIFICITY; HUMAN; METABOLISM; MUTAGENESIS; OSTEOPOROSIS; PICHIA; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

AMINO ACIDS; BINDING SITES; BONE AND BONES; BONE REMODELING; CATHEPSIN K; COLLAGEN; CRYSTALLOGRAPHY, X-RAY; GLYCOSAMINOGLYCANS; HUMANS; HYDROLYSIS; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; MUTAGENESIS; OSTEOPOROSIS; PEPTIDE HYDROLASES; PICHIA; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY;

EID: 84918557552     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1414126111     Document Type: Article

References (39)

1. Brömme D, Okamoto K (1995) Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution. Biol Chem Hoppe Seyler 376(6):379-384
2. Drake FH, et al. (1996) Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts. J Biol Chem 271(21):12511-12516
3. Bromme D (2011) Cystein cathepsins and the skeleton. Clin Rev Bone Miner Metab 9(2):83-93
4. Panwar P, et al. (2013) Effects of cysteine proteases on the structural and mechanical properties of collagen fibers. J Biol Chem 288(8):5940-5950
5. Yasuda Y, Kaleta J, Brömme D (2005) The role of cathepsins in osteoporosis and arthritis: Rationale for the design of new therapeutics. Adv Drug Deliv Rev 57(7): 973-993
6. Podgorski I (2009) Future of anticathepsin K drugs: Dual therapy for skeletal disease and atherosclerosis? Future Med Chem 1(1):21-34
7. Brömme D, Lecaille F (2009) Cathepsin K inhibitors for osteoporosis and potential offtarget effects. Expert Opin Investig Drugs 18(5):585-600
8. Saftig P, et al. (1998) Impaired osteoclastic bone resorption leads to osteopetrosis in cathepsin-K-deficient mice. Proc Natl Acad Sci USA 95(23):13453-13458
9. Gelb BD, Shi GP, Chapman HA, Desnick RJ (1996) Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency. Science 273(5279):1236-1238
10. Everts V, et al. (2003) Cathepsin K deficiency in pycnodysostosis results in accumulation of non-digested phagocytosed collagen in fibroblasts. Calcif Tissue Int 73(4):380-386
11. Costa AG, Cusano NE, Silva BC, Cremers S, Bilezikian JP (2011) Cathepsin K: Its skeletal actions and role as a therapeutic target in osteoporosis. Nat Rev Rheumatol 7(8): 447-456
12. Chapurlat RD (2014) Treatment of postmenopausal osteoporosis with odanacatib. Expert Opin Pharmacother 15(4):559-564
13. Bertini I, et al. (2012) Structural basis for matrix metalloproteinase 1-catalyzed collagenolysis. J Am Chem Soc 134(4):2100-2110
14. Manka SW, et al. (2012) Structural insights into triple-helical collagen cleavage by matrix metalloproteinase 1. Proc Natl Acad Sci USA 109(31):12461-12466
15. McGrath ME, Klaus JL, Barnes MG, Brömme D (1997) Crystal structure of human cathepsin K complexed with a potent inhibitor. Nat Struct Biol 4(2):105-109
16. McGrath ME (1999) The lysosomal cysteine proteases. Annu Rev Biophys Biomol Struct 28:181-204
17. Li Z, Hou WS, Escalante-Torres CR, Gelb BD, Bromme D (2002) Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate. J Biol Chem 277(32):28669-28676
18. Li Z, Kienetz M, Cherney MM, James MN, Brömme D (2008) The crystal and molecular structures of a cathepsin K:chondroitin sulfate complex. J Mol Biol 383(1):78-91
19. Waddington RJ, Roberts HC, Sugars RV, Schönherr E (2003) Differential roles for small leucine-rich proteoglycans in bone formation. Eur Cell Mater 6:12-21, discussion 21
20. Cherney MM, et al. (2011) Structure-activity analysis of cathepsin K/chondroitin 4-sulfate interactions. J Biol Chem 286(11):8988-8998
21. Nallaseth FS, Lecaille F, Li Z, Brömme D (2013) The role of basic amino acid surface clusters on the collagenase activity of cathepsin K. Biochemistry 52(44):7742-7752
22. Raman R, Sasisekharan V, Sasisekharan R (2005) Structural insights into biological roles of protein-glycosaminoglycan interactions. Chem Biol 12(3):267-277
23. Obrink B (1973) A study of the interactions between monomeric tropocollagen and glycosaminoglycans. Eur J Biochem 33(2):387-400
24. Raspanti M, et al. (2008) Glycosaminoglycans show a specific periodic interaction with type I collagen fibrils. J Struct Biol 164(1):134-139
25. Stamov DR, Müller A, Wegrowski Y, Brezillon S, Franz CM (2013) Quantitative analysis of type I collagen fibril regulation by lumican and decorin using AFM. J Struct Biol 183(3):394-403
26. Garnero P, et al. (1998) The collagenolytic activity of cathepsin K is unique among mammalian proteinases. J Biol Chem 273(48):32347-32352
27. Li Z, Hou WS, Brömme D (2000) Collagenolytic activity of cathepsin K is specifically modulated by cartilage-resident chondroitin sulfates. Biochemistry 39(3):529-536
28. Li Z, et al. (2004) Regulation of collagenase activities of human cathepsins by glycosaminoglycans. J Biol Chem 279(7):5470-5479
29. Novinec M, Kovacic L, Lenarcic B, Baici A (2010) Conformational flexibility and allosteric regulation of cathepsin K. Biochem J 429(2):379-389
30. Perumal S, Antipova O, Orgel JP (2008) Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysis. Proc Natl Acad Sci USA 105(8):2824-2829
31. KafienahW, Brömme D, Buttle DJ, Croucher LJ, Hollander AP (1998) Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix. Biochem J 331(Pt 3):727-732
32. Chung L, et al. (2004) Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis. EMBO J 23(15):3020-3030
33. Fields GB (2013) Interstitial collagen catabolism. J Biol Chem 288(13):8785-8793
34. Eckhard U, Schönauer E, Nüss D, Brandstetter H (2011) Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis. Nat Struct Mol Biol 18(10):1109-1114
35. Sharma V, et al. (2014) Structural requirements for the collagenase and elastase activity of cathepsin K and its selective inhibition by an exosite inhibitor. Biochem J, in press. 36.
36. Yamashita DS, Dodds RA (2000) Cathepsin K and the design of inhibitors of cathepsin K. Curr Pharm Des 6(1):1-24
37. Dauth S, et al. (2011) Cathepsin K deficiency in mice induces structural and metabolic changes in the central nervous system that are associated with learning and memory deficits. BMC Neurosci 12:74
38. Linnevers CJ, et al. (1997) Expression of human cathepsin K in Pichia pastoris and preliminary crystallographic studies of an inhibitor complex. Protein Sci 6(4):919-921
39. Selent J, Kaleta J, Li Z, Lalmanach G, Brömme D (2007) Selective inhibition of the collagenase activity of cathepsin K. J Biol Chem 282(22):16492-16501.