Conformational studies on the specific cleavage site of type I collagen (alpha-1) fragment (157-192) by cathepsins K and L by proton NMR spectroscopy

Citation
Ay. Nosaka et al., Conformational studies on the specific cleavage site of type I collagen (alpha-1) fragment (157-192) by cathepsins K and L by proton NMR spectroscopy, BIO MED CH, 7(2), 1999, pp. 375-379
Citations number
37
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Chemistry & Analysis
Journal title
BIOORGANIC & MEDICINAL CHEMISTRY
ISSN journal
0968-0896 → ACNP
Volume
7
Issue
2
Year of publication
1999
Pages
375 - 379
Database
ISI
SICI code
0968-0896(199902)7:2<375:CSOTSC>2.0.ZU;2-T
Abstract
Cathepsins K and L are cysteine proteinases which are considered to play an important role in bone resorption. Type I collagen is the most abundant co mponent of the extracellular matrix of bone and regarded as an endogenous s ubstrate for the cysteine proteinases in osteoclastic bone resorption. We h ave synthesized a fragment of Type I collagen (alpha-1) (157-192) as a subs trate for the cathepsins and found that cathepsins K and L cleave the fragm ent at different specific sites. The major cleavage sites for cathepsin K w ere Met159-Gly160, Ser162-Gly163 and Arg165-Gly166, while those for catheps in L were Gly166-Leu167 and Gln180-Gly181. The structure of the fragment wa s analyzed in aqueous solution by circular dichroism and proton NMR spectro scopy and the difference in the molecular recognition of collagen by cathep sins K and L was discussed from the structural aspect. (C) 1999 Elsevier Sc ience Ltd. All rights reserved.