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
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 component of the extracellular matrix of bone and regarded as an endogenous substrate for the cysteine proteinases in osteoclastic bone resorption. We h...
Gespeichert in:
| Veröffentlicht in: | Bioorganic & medicinal chemistry 1999-02, Vol.7 (2), p.375-379 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 379 |
|---|---|
| container_issue | 2 |
| container_start_page | 375 |
| container_title | Bioorganic & medicinal chemistry |
| container_volume | 7 |
| creator | Nosaka, A Y Kanaori, K Teno, N Togame, H Inaoka, T Takai, M Kokubo, T |
| description | 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 component of the extracellular matrix of bone and regarded as an endogenous substrate for the cysteine proteinases in osteoclastic bone resorption. We have synthesized a fragment of Type I collagen (alpha-1) (157-192) as a substrate for the cathepsins and found that cathepsins K and L cleave the fragment at different specific sites. The major cleavage sites for cathepsin K were Met159-Gly160, Ser162-Gly163 and Arg165-Gly166, while those for cathepsin L were Gly166-Leu167 and Gln180-Gly181. The structure of the fragment was analyzed in aqueous solution by circular dichroism and proton NMR spectroscopy and the difference in the molecular recognition of collagen by cathepsins K and L was discussed from the structural aspect. |
| doi_str_mv | 10.1016/S0968-0896(98)00227-2 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_69717363</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>69717363</sourcerecordid><originalsourceid>FETCH-LOGICAL-c305t-3a5ed0056a344292ad38259dec890822ea83745de7f0641587c3d6200dd53c813</originalsourceid><addsrcrecordid>eNpNUctu2zAQ5CFF4ib5hBR7KuyDEj5EiTwWRpMGcROgTc4EQ65sFZKoinQBf0j-t3RsFD0tMDu7M7tDyBWj14yy6uYn1ZUqqNLVXKsFpZzXBT8hs3_wGfkY4y-aO6Vmp-SMUc6UEmxG3pZhaMLU29SGwXYQ09a3GCEMkDYIcUTXNq0D16H9Y9cZaRNCaOB5NyLcgwtdl-EB5rYbN7ZgC2gmu-5xSDBnsi6Y5gt43YGzed8Y2yHCA9jBw2qPjlNIWerx-493qTSF6MK4uyAfGttFvDzWc_Jy-_V5-a1YPd3dL7-sCieoTIWwEj2lsrKiLLnm1gvFpfbolKaKc7RK1KX0WDe0KplUtRO-4pR6L4VTTJyTz4e92cfvLcZk-jY6zCcNGLbRVLpmtahEJsoD0WWHccLGjFPb22lnGDX7DMx7Bmb_bKNz3WdgeJ77dBTYvvbo_5s6BCD-AnvBgvI</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>69717363</pqid></control><display><type>article</type><title>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</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Nosaka, A Y ; Kanaori, K ; Teno, N ; Togame, H ; Inaoka, T ; Takai, M ; Kokubo, T</creator><creatorcontrib>Nosaka, A Y ; Kanaori, K ; Teno, N ; Togame, H ; Inaoka, T ; Takai, M ; Kokubo, T</creatorcontrib><description>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 component of the extracellular matrix of bone and regarded as an endogenous substrate for the cysteine proteinases in osteoclastic bone resorption. We have synthesized a fragment of Type I collagen (alpha-1) (157-192) as a substrate for the cathepsins and found that cathepsins K and L cleave the fragment at different specific sites. The major cleavage sites for cathepsin K were Met159-Gly160, Ser162-Gly163 and Arg165-Gly166, while those for cathepsin L were Gly166-Leu167 and Gln180-Gly181. The structure of the fragment was analyzed in aqueous solution by circular dichroism and proton NMR spectroscopy and the difference in the molecular recognition of collagen by cathepsins K and L was discussed from the structural aspect.</description><identifier>ISSN: 0968-0896</identifier><identifier>DOI: 10.1016/S0968-0896(98)00227-2</identifier><identifier>PMID: 10218831</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Sequence ; Cathepsin K ; Cathepsin L ; Cathepsins - metabolism ; Chromatography, High Pressure Liquid ; Circular Dichroism ; Collagen - chemistry ; Cysteine Endopeptidases ; Endopeptidases ; Humans ; Kidney - metabolism ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Temperature</subject><ispartof>Bioorganic & medicinal chemistry, 1999-02, Vol.7 (2), p.375-379</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c305t-3a5ed0056a344292ad38259dec890822ea83745de7f0641587c3d6200dd53c813</citedby><cites>FETCH-LOGICAL-c305t-3a5ed0056a344292ad38259dec890822ea83745de7f0641587c3d6200dd53c813</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10218831$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nosaka, A Y</creatorcontrib><creatorcontrib>Kanaori, K</creatorcontrib><creatorcontrib>Teno, N</creatorcontrib><creatorcontrib>Togame, H</creatorcontrib><creatorcontrib>Inaoka, T</creatorcontrib><creatorcontrib>Takai, M</creatorcontrib><creatorcontrib>Kokubo, T</creatorcontrib><title>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</title><title>Bioorganic & medicinal chemistry</title><addtitle>Bioorg Med Chem</addtitle><description>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 component of the extracellular matrix of bone and regarded as an endogenous substrate for the cysteine proteinases in osteoclastic bone resorption. We have synthesized a fragment of Type I collagen (alpha-1) (157-192) as a substrate for the cathepsins and found that cathepsins K and L cleave the fragment at different specific sites. The major cleavage sites for cathepsin K were Met159-Gly160, Ser162-Gly163 and Arg165-Gly166, while those for cathepsin L were Gly166-Leu167 and Gln180-Gly181. The structure of the fragment was analyzed in aqueous solution by circular dichroism and proton NMR spectroscopy and the difference in the molecular recognition of collagen by cathepsins K and L was discussed from the structural aspect.</description><subject>Amino Acid Sequence</subject><subject>Cathepsin K</subject><subject>Cathepsin L</subject><subject>Cathepsins - metabolism</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Circular Dichroism</subject><subject>Collagen - chemistry</subject><subject>Cysteine Endopeptidases</subject><subject>Endopeptidases</subject><subject>Humans</subject><subject>Kidney - metabolism</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Molecular Sequence Data</subject><subject>Temperature</subject><issn>0968-0896</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNUctu2zAQ5CFF4ib5hBR7KuyDEj5EiTwWRpMGcROgTc4EQ65sFZKoinQBf0j-t3RsFD0tMDu7M7tDyBWj14yy6uYn1ZUqqNLVXKsFpZzXBT8hs3_wGfkY4y-aO6Vmp-SMUc6UEmxG3pZhaMLU29SGwXYQ09a3GCEMkDYIcUTXNq0D16H9Y9cZaRNCaOB5NyLcgwtdl-EB5rYbN7ZgC2gmu-5xSDBnsi6Y5gt43YGzed8Y2yHCA9jBw2qPjlNIWerx-493qTSF6MK4uyAfGttFvDzWc_Jy-_V5-a1YPd3dL7-sCieoTIWwEj2lsrKiLLnm1gvFpfbolKaKc7RK1KX0WDe0KplUtRO-4pR6L4VTTJyTz4e92cfvLcZk-jY6zCcNGLbRVLpmtahEJsoD0WWHccLGjFPb22lnGDX7DMx7Bmb_bKNz3WdgeJ77dBTYvvbo_5s6BCD-AnvBgvI</recordid><startdate>199902</startdate><enddate>199902</enddate><creator>Nosaka, A Y</creator><creator>Kanaori, K</creator><creator>Teno, N</creator><creator>Togame, H</creator><creator>Inaoka, T</creator><creator>Takai, M</creator><creator>Kokubo, T</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>199902</creationdate><title>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</title><author>Nosaka, A Y ; Kanaori, K ; Teno, N ; Togame, H ; Inaoka, T ; Takai, M ; Kokubo, T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c305t-3a5ed0056a344292ad38259dec890822ea83745de7f0641587c3d6200dd53c813</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Sequence</topic><topic>Cathepsin K</topic><topic>Cathepsin L</topic><topic>Cathepsins - metabolism</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Circular Dichroism</topic><topic>Collagen - chemistry</topic><topic>Cysteine Endopeptidases</topic><topic>Endopeptidases</topic><topic>Humans</topic><topic>Kidney - metabolism</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Molecular Sequence Data</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nosaka, A Y</creatorcontrib><creatorcontrib>Kanaori, K</creatorcontrib><creatorcontrib>Teno, N</creatorcontrib><creatorcontrib>Togame, H</creatorcontrib><creatorcontrib>Inaoka, T</creatorcontrib><creatorcontrib>Takai, M</creatorcontrib><creatorcontrib>Kokubo, T</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Bioorganic & medicinal chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nosaka, A Y</au><au>Kanaori, K</au><au>Teno, N</au><au>Togame, H</au><au>Inaoka, T</au><au>Takai, M</au><au>Kokubo, T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>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</atitle><jtitle>Bioorganic & medicinal chemistry</jtitle><addtitle>Bioorg Med Chem</addtitle><date>1999-02</date><risdate>1999</risdate><volume>7</volume><issue>2</issue><spage>375</spage><epage>379</epage><pages>375-379</pages><issn>0968-0896</issn><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 component of the extracellular matrix of bone and regarded as an endogenous substrate for the cysteine proteinases in osteoclastic bone resorption. We have synthesized a fragment of Type I collagen (alpha-1) (157-192) as a substrate for the cathepsins and found that cathepsins K and L cleave the fragment at different specific sites. The major cleavage sites for cathepsin K were Met159-Gly160, Ser162-Gly163 and Arg165-Gly166, while those for cathepsin L were Gly166-Leu167 and Gln180-Gly181. The structure of the fragment was analyzed in aqueous solution by circular dichroism and proton NMR spectroscopy and the difference in the molecular recognition of collagen by cathepsins K and L was discussed from the structural aspect.</abstract><cop>England</cop><pmid>10218831</pmid><doi>10.1016/S0968-0896(98)00227-2</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0968-0896 |
| ispartof | Bioorganic & medicinal chemistry, 1999-02, Vol.7 (2), p.375-379 |
| issn | 0968-0896 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_69717363 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amino Acid Sequence Cathepsin K Cathepsin L Cathepsins - metabolism Chromatography, High Pressure Liquid Circular Dichroism Collagen - chemistry Cysteine Endopeptidases Endopeptidases Humans Kidney - metabolism Magnetic Resonance Spectroscopy Molecular Sequence Data Temperature |
| title | 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 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T10%3A11%3A02IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Conformational%20studies%20on%20the%20specific%20cleavage%20site%20of%20Type%20I%20collagen%20(alpha-1)%20fragment%20(157-192)%20by%20cathepsins%20K%20and%20L%20by%20proton%20NMR%20spectroscopy&rft.jtitle=Bioorganic%20&%20medicinal%20chemistry&rft.au=Nosaka,%20A%20Y&rft.date=1999-02&rft.volume=7&rft.issue=2&rft.spage=375&rft.epage=379&rft.pages=375-379&rft.issn=0968-0896&rft_id=info:doi/10.1016/S0968-0896(98)00227-2&rft_dat=%3Cproquest_cross%3E69717363%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=69717363&rft_id=info:pmid/10218831&rfr_iscdi=true |