Proteoglycans and catabolic products of proteoglycans present in ligament
The aim of the present study was to characterize the proteoglycans and catabolic products of proteoglycans present in the tensile region of ligament and explant cultures of this tissue, and to compare these with those observed in the tensile region of tendon. Approx. 90% of the total proteoglycans i...
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Veröffentlicht in: | Biochemical journal 2005-01, Vol.385 (Pt 2), p.381-388 |
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creator | Ilic, Mirna Z Carter, Phillip Tyndall, Alicia Dudhia, Jayesh Handley, Christopher J |
description | The aim of the present study was to characterize the proteoglycans and catabolic products of proteoglycans present in the tensile region of ligament and explant cultures of this tissue, and to compare these with those observed in the tensile region of tendon. Approx. 90% of the total proteoglycans in fresh ligament was decorin, as estimated by N-terminal amino acid sequence analysis. Other species that were detected were biglycan and the large proteoglycans versican (splice variants V(0) and/or V1 and/or V2) and aggrecan. Approx. 23% of decorin detected in the matrix was degraded. Intact decorin and decorin fragments similar to those observed in the matrix that retained the N-terminus were also observed in the medium of ligament cultures. Intact biglycan core protein was detected in the matrix and medium of ligament cultures, and two fragments originating from the N-terminal region of biglycan were observed in the matrix of cultured ligament. Versican and versican fragments that retained the N-terminus of versican core protein were detected in fresh matrix and medium of tendon cultures. Approx. 42% of versican present in the fresh ligament was degraded. Aggrecan catabolites appearing in the culture medium were derived from aggrecanase cleavage of the core protein. An intact link protein and a degradation product from the N-terminal region of type XII collagen were also detected in the medium of the ligament explant. |
doi_str_mv | 10.1042/bj20040844 |
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Approx. 90% of the total proteoglycans in fresh ligament was decorin, as estimated by N-terminal amino acid sequence analysis. Other species that were detected were biglycan and the large proteoglycans versican (splice variants V(0) and/or V1 and/or V2) and aggrecan. Approx. 23% of decorin detected in the matrix was degraded. Intact decorin and decorin fragments similar to those observed in the matrix that retained the N-terminus were also observed in the medium of ligament cultures. Intact biglycan core protein was detected in the matrix and medium of ligament cultures, and two fragments originating from the N-terminal region of biglycan were observed in the matrix of cultured ligament. Versican and versican fragments that retained the N-terminus of versican core protein were detected in fresh matrix and medium of tendon cultures. Approx. 42% of versican present in the fresh ligament was degraded. Aggrecan catabolites appearing in the culture medium were derived from aggrecanase cleavage of the core protein. An intact link protein and a degradation product from the N-terminal region of type XII collagen were also detected in the medium of the ligament explant.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj20040844</identifier><identifier>PMID: 15329049</identifier><language>eng</language><publisher>England: Portland Press Ltd</publisher><subject>Aggrecans ; Animals ; Antibodies, Monoclonal - metabolism ; Biglycan ; Cattle ; Collateral Ligaments - chemistry ; Culture Media - chemistry ; Decorin ; Extracellular Matrix Proteins - chemistry ; Extracellular Matrix Proteins - immunology ; Extracellular Matrix Proteins - metabolism ; Lectins, C-Type ; Male ; Metacarpophalangeal Joint ; Molecular Weight ; Peptide Fragments - chemistry ; Peptide Fragments - immunology ; Peptide Fragments - metabolism ; Proteoglycans - chemistry ; Proteoglycans - immunology ; Proteoglycans - metabolism ; Sequence Analysis, Protein - methods ; Tissue Culture Techniques</subject><ispartof>Biochemical journal, 2005-01, Vol.385 (Pt 2), p.381-388</ispartof><rights>The Biochemical Society, London 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c442t-344ff19a95cc54dea7d4736f41e74ee43d7504522e1be1eb2186c3dbc8c3a8a03</citedby><cites>FETCH-LOGICAL-c442t-344ff19a95cc54dea7d4736f41e74ee43d7504522e1be1eb2186c3dbc8c3a8a03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1134708/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1134708/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15329049$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ilic, Mirna Z</creatorcontrib><creatorcontrib>Carter, Phillip</creatorcontrib><creatorcontrib>Tyndall, Alicia</creatorcontrib><creatorcontrib>Dudhia, Jayesh</creatorcontrib><creatorcontrib>Handley, Christopher J</creatorcontrib><title>Proteoglycans and catabolic products of proteoglycans present in ligament</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>The aim of the present study was to characterize the proteoglycans and catabolic products of proteoglycans present in the tensile region of ligament and explant cultures of this tissue, and to compare these with those observed in the tensile region of tendon. Approx. 90% of the total proteoglycans in fresh ligament was decorin, as estimated by N-terminal amino acid sequence analysis. Other species that were detected were biglycan and the large proteoglycans versican (splice variants V(0) and/or V1 and/or V2) and aggrecan. Approx. 23% of decorin detected in the matrix was degraded. Intact decorin and decorin fragments similar to those observed in the matrix that retained the N-terminus were also observed in the medium of ligament cultures. Intact biglycan core protein was detected in the matrix and medium of ligament cultures, and two fragments originating from the N-terminal region of biglycan were observed in the matrix of cultured ligament. Versican and versican fragments that retained the N-terminus of versican core protein were detected in fresh matrix and medium of tendon cultures. Approx. 42% of versican present in the fresh ligament was degraded. Aggrecan catabolites appearing in the culture medium were derived from aggrecanase cleavage of the core protein. An intact link protein and a degradation product from the N-terminal region of type XII collagen were also detected in the medium of the ligament explant.</description><subject>Aggrecans</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - metabolism</subject><subject>Biglycan</subject><subject>Cattle</subject><subject>Collateral Ligaments - chemistry</subject><subject>Culture Media - chemistry</subject><subject>Decorin</subject><subject>Extracellular Matrix Proteins - chemistry</subject><subject>Extracellular Matrix Proteins - immunology</subject><subject>Extracellular Matrix Proteins - metabolism</subject><subject>Lectins, C-Type</subject><subject>Male</subject><subject>Metacarpophalangeal Joint</subject><subject>Molecular Weight</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - immunology</subject><subject>Peptide Fragments - metabolism</subject><subject>Proteoglycans - chemistry</subject><subject>Proteoglycans - immunology</subject><subject>Proteoglycans - metabolism</subject><subject>Sequence Analysis, Protein - methods</subject><subject>Tissue Culture Techniques</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkE1Lw0AQhhdRbK1e_AGSkwchOrs7-boIWvyoFPSg52WzmdSUJFt3E6H_3pTWr9O8MA_vDA9jpxwuOaC4ypcCACFF3GNjjgmEaSLSfTYGEWMYg-AjduT9EoDjwB2yEY-kyACzMZu9ONuRXdRro1sf6LYIjO50buvKBCtni950PrDlJv_hVo48tV1QtUFdLXQz5GN2UOra08luTtjb_d3r9DGcPz_Mpjfz0CCKLpSIZckznUXGRFiQTgpMZFwipwSJUBZJBBgJQTwnTrngaWxkkZvUSJ1qkBN2ve1d9XlDhRlOO12rlasa7dbK6kr937TVu1rYT8W5HNykQ8H5rsDZj558p5rKG6pr3ZLtvYoTiQKieAAvtqBx1ntH5c8RDmpjXt0-fZsf4LO_b_2iO9XyC2AwgEI</recordid><startdate>20050115</startdate><enddate>20050115</enddate><creator>Ilic, Mirna Z</creator><creator>Carter, Phillip</creator><creator>Tyndall, Alicia</creator><creator>Dudhia, Jayesh</creator><creator>Handley, Christopher J</creator><general>Portland Press Ltd</general><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><scope>5PM</scope></search><sort><creationdate>20050115</creationdate><title>Proteoglycans and catabolic products of proteoglycans present in ligament</title><author>Ilic, Mirna Z ; Carter, Phillip ; Tyndall, Alicia ; Dudhia, Jayesh ; Handley, Christopher J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c442t-344ff19a95cc54dea7d4736f41e74ee43d7504522e1be1eb2186c3dbc8c3a8a03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Aggrecans</topic><topic>Animals</topic><topic>Antibodies, Monoclonal - metabolism</topic><topic>Biglycan</topic><topic>Cattle</topic><topic>Collateral Ligaments - chemistry</topic><topic>Culture Media - chemistry</topic><topic>Decorin</topic><topic>Extracellular Matrix Proteins - chemistry</topic><topic>Extracellular Matrix Proteins - immunology</topic><topic>Extracellular Matrix Proteins - metabolism</topic><topic>Lectins, C-Type</topic><topic>Male</topic><topic>Metacarpophalangeal Joint</topic><topic>Molecular Weight</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - immunology</topic><topic>Peptide Fragments - metabolism</topic><topic>Proteoglycans - chemistry</topic><topic>Proteoglycans - immunology</topic><topic>Proteoglycans - metabolism</topic><topic>Sequence Analysis, Protein - methods</topic><topic>Tissue Culture Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ilic, Mirna Z</creatorcontrib><creatorcontrib>Carter, Phillip</creatorcontrib><creatorcontrib>Tyndall, Alicia</creatorcontrib><creatorcontrib>Dudhia, Jayesh</creatorcontrib><creatorcontrib>Handley, Christopher J</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ilic, Mirna Z</au><au>Carter, Phillip</au><au>Tyndall, Alicia</au><au>Dudhia, Jayesh</au><au>Handley, Christopher J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteoglycans and catabolic products of proteoglycans present in ligament</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>2005-01-15</date><risdate>2005</risdate><volume>385</volume><issue>Pt 2</issue><spage>381</spage><epage>388</epage><pages>381-388</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>The aim of the present study was to characterize the proteoglycans and catabolic products of proteoglycans present in the tensile region of ligament and explant cultures of this tissue, and to compare these with those observed in the tensile region of tendon. Approx. 90% of the total proteoglycans in fresh ligament was decorin, as estimated by N-terminal amino acid sequence analysis. Other species that were detected were biglycan and the large proteoglycans versican (splice variants V(0) and/or V1 and/or V2) and aggrecan. Approx. 23% of decorin detected in the matrix was degraded. Intact decorin and decorin fragments similar to those observed in the matrix that retained the N-terminus were also observed in the medium of ligament cultures. Intact biglycan core protein was detected in the matrix and medium of ligament cultures, and two fragments originating from the N-terminal region of biglycan were observed in the matrix of cultured ligament. Versican and versican fragments that retained the N-terminus of versican core protein were detected in fresh matrix and medium of tendon cultures. Approx. 42% of versican present in the fresh ligament was degraded. Aggrecan catabolites appearing in the culture medium were derived from aggrecanase cleavage of the core protein. An intact link protein and a degradation product from the N-terminal region of type XII collagen were also detected in the medium of the ligament explant.</abstract><cop>England</cop><pub>Portland Press Ltd</pub><pmid>15329049</pmid><doi>10.1042/bj20040844</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Aggrecans Animals Antibodies, Monoclonal - metabolism Biglycan Cattle Collateral Ligaments - chemistry Culture Media - chemistry Decorin Extracellular Matrix Proteins - chemistry Extracellular Matrix Proteins - immunology Extracellular Matrix Proteins - metabolism Lectins, C-Type Male Metacarpophalangeal Joint Molecular Weight Peptide Fragments - chemistry Peptide Fragments - immunology Peptide Fragments - metabolism Proteoglycans - chemistry Proteoglycans - immunology Proteoglycans - metabolism Sequence Analysis, Protein - methods Tissue Culture Techniques |
title | Proteoglycans and catabolic products of proteoglycans present in ligament |
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