Cartilage aggrecan undergoes significant compositional and structural alterations during laryngeal cancer
Aggrecan is a key component of cartilage and is responsible for the integrity and function of the tissue. In this study, the content of aggrecan and its structural modifications in adjacent to cancer apparently normal cartilages (AANCs) from various stages of laryngeal squamous cell carcinoma (LSCC)...
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Veröffentlicht in: | Biochimica et biophysica acta 2006-07, Vol.1760 (7), p.1046-1053 |
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creator | Skandalis, Spyros S. Theocharis, Achilleas D. Vynios, Demitrios H. Papageorgakopoulou, Nickoletta Hjerpe, Anders Karamanos, Nikos K. Theocharis, Dimitrios A. |
description | Aggrecan is a key component of cartilage and is responsible for the integrity and function of the tissue. In this study, the content of aggrecan and its structural modifications in adjacent to cancer apparently normal cartilages (AANCs) from various stages of laryngeal squamous cell carcinoma (LSCC) were investigated. Our data demonstrated a stage-related loss of aggregable aggrecan in AANCs, compared to the healthy laryngeal cartilage (HLC), which was excessive in advanced stages of disease. On aggregable aggrecan level, AANCs were characterized by significant compositional and structural modifications, the extent of which was closely related with the stage of LSCC. Four concrete subpopulations of aggregable molecules with particular physicochemical characteristics were identified with a strong tendency to prevail subpopulations of molecules of lower hydrodynamic sizes with increasing LSCC stage. These findings demonstrated that the cleavage of aggregable aggrecan occurred in concrete peptide bonds within the CS-1 and CS-2 attachment domains. These significant alterations were closely associated with the process of cartilage destruction, indicating the crucial role of aggrecan during LSCC. |
doi_str_mv | 10.1016/j.bbagen.2006.02.007 |
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In this study, the content of aggrecan and its structural modifications in adjacent to cancer apparently normal cartilages (AANCs) from various stages of laryngeal squamous cell carcinoma (LSCC) were investigated. Our data demonstrated a stage-related loss of aggregable aggrecan in AANCs, compared to the healthy laryngeal cartilage (HLC), which was excessive in advanced stages of disease. On aggregable aggrecan level, AANCs were characterized by significant compositional and structural modifications, the extent of which was closely related with the stage of LSCC. Four concrete subpopulations of aggregable molecules with particular physicochemical characteristics were identified with a strong tendency to prevail subpopulations of molecules of lower hydrodynamic sizes with increasing LSCC stage. These findings demonstrated that the cleavage of aggregable aggrecan occurred in concrete peptide bonds within the CS-1 and CS-2 attachment domains. These significant alterations were closely associated with the process of cartilage destruction, indicating the crucial role of aggrecan during LSCC.</description><identifier>ISSN: 0304-4165</identifier><identifier>ISSN: 0006-3002</identifier><identifier>EISSN: 1872-8006</identifier><identifier>DOI: 10.1016/j.bbagen.2006.02.007</identifier><identifier>PMID: 16574327</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Adult ; Aggrecan degradation ; Aggrecans ; Aggregable aggrecan ; Carcinoma, Squamous Cell - metabolism ; Cartilage ; Cartilage - metabolism ; Cartilage - pathology ; Chondroitin Sulfate Proteoglycans - biosynthesis ; Chondroitin Sulfate Proteoglycans - chemistry ; Extracellular Matrix Proteins - biosynthesis ; Extracellular Matrix Proteins - chemistry ; Gene Expression Regulation, Neoplastic ; Glycosaminoglycans - chemistry ; Humans ; Immunohistochemistry ; Laryngeal cancer ; Laryngeal Neoplasms - metabolism ; Lectins, C-Type - biosynthesis ; Lectins, C-Type - chemistry ; Male ; Middle Aged ; Peptides - chemistry ; Protein Binding ; Protein Structure, Tertiary ; Proteoglycans</subject><ispartof>Biochimica et biophysica acta, 2006-07, Vol.1760 (7), p.1046-1053</ispartof><rights>2006 Elsevier B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c398t-b302cda37050c090870924f761cdf9e4544a4e1dd8cbacd931a3005f4975a44b3</citedby><cites>FETCH-LOGICAL-c398t-b302cda37050c090870924f761cdf9e4544a4e1dd8cbacd931a3005f4975a44b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0304416506000389$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16574327$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:1947022$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Skandalis, Spyros S.</creatorcontrib><creatorcontrib>Theocharis, Achilleas D.</creatorcontrib><creatorcontrib>Vynios, Demitrios H.</creatorcontrib><creatorcontrib>Papageorgakopoulou, Nickoletta</creatorcontrib><creatorcontrib>Hjerpe, Anders</creatorcontrib><creatorcontrib>Karamanos, Nikos K.</creatorcontrib><creatorcontrib>Theocharis, Dimitrios A.</creatorcontrib><title>Cartilage aggrecan undergoes significant compositional and structural alterations during laryngeal cancer</title><title>Biochimica et biophysica acta</title><addtitle>Biochim Biophys Acta</addtitle><description>Aggrecan is a key component of cartilage and is responsible for the integrity and function of the tissue. In this study, the content of aggrecan and its structural modifications in adjacent to cancer apparently normal cartilages (AANCs) from various stages of laryngeal squamous cell carcinoma (LSCC) were investigated. Our data demonstrated a stage-related loss of aggregable aggrecan in AANCs, compared to the healthy laryngeal cartilage (HLC), which was excessive in advanced stages of disease. On aggregable aggrecan level, AANCs were characterized by significant compositional and structural modifications, the extent of which was closely related with the stage of LSCC. Four concrete subpopulations of aggregable molecules with particular physicochemical characteristics were identified with a strong tendency to prevail subpopulations of molecules of lower hydrodynamic sizes with increasing LSCC stage. These findings demonstrated that the cleavage of aggregable aggrecan occurred in concrete peptide bonds within the CS-1 and CS-2 attachment domains. These significant alterations were closely associated with the process of cartilage destruction, indicating the crucial role of aggrecan during LSCC.</description><subject>Adult</subject><subject>Aggrecan degradation</subject><subject>Aggrecans</subject><subject>Aggregable aggrecan</subject><subject>Carcinoma, Squamous Cell - metabolism</subject><subject>Cartilage</subject><subject>Cartilage - metabolism</subject><subject>Cartilage - pathology</subject><subject>Chondroitin Sulfate Proteoglycans - biosynthesis</subject><subject>Chondroitin Sulfate Proteoglycans - chemistry</subject><subject>Extracellular Matrix Proteins - biosynthesis</subject><subject>Extracellular Matrix Proteins - chemistry</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>Glycosaminoglycans - chemistry</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Laryngeal cancer</subject><subject>Laryngeal Neoplasms - metabolism</subject><subject>Lectins, C-Type - biosynthesis</subject><subject>Lectins, C-Type - chemistry</subject><subject>Male</subject><subject>Middle Aged</subject><subject>Peptides - chemistry</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Proteoglycans</subject><issn>0304-4165</issn><issn>0006-3002</issn><issn>1872-8006</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9UU2v1CAUJUbjG5_-A2O6ctd6KbS0GxMz8St5iRtdEwq3DWMHRqAa_7130onuZAOce87hcg9jLzk0HHj_5tRMk1kwNC1A30DbAKhH7MAH1dYDQY_ZAQTIWvK-u2PPcj4BrW7snrI7gpQUrTowfzSp-JWMKrMsCa0J1RYcpiVirrJfgp89gaWy8XyJ2Rcfg1krE1yVS9ps2dL1uhZM5lrLlduSD0u1mvQ7LEhFkltMz9mT2awZX9z2e_btw_uvx0_1w5ePn4_vHmorxqHUk4DWOiMUdGBhhEHB2MpZ9dy6eUTZSWkkcucGOxnrRsGNoG_NclSdkXIS96zeffMvvGyTviR_plZ0NF7foO90Qt2pvhUD8V_v_EuKPzbMRZ99triuJmDcsu4H6kLKkYhyJ9oUc044_7XmoK-R6JPeI9HXSDS0miIh2aub_zad0f0T3TIgwtudgDSVnx6TztYjjcx5yqNoF_3_X_gDcW2hmQ</recordid><startdate>20060701</startdate><enddate>20060701</enddate><creator>Skandalis, Spyros S.</creator><creator>Theocharis, Achilleas D.</creator><creator>Vynios, Demitrios H.</creator><creator>Papageorgakopoulou, Nickoletta</creator><creator>Hjerpe, Anders</creator><creator>Karamanos, Nikos K.</creator><creator>Theocharis, Dimitrios A.</creator><general>Elsevier B.V</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>ADTPV</scope><scope>AOWAS</scope></search><sort><creationdate>20060701</creationdate><title>Cartilage aggrecan undergoes significant compositional and structural alterations during laryngeal cancer</title><author>Skandalis, Spyros S. ; Theocharis, Achilleas D. ; Vynios, Demitrios H. ; Papageorgakopoulou, Nickoletta ; Hjerpe, Anders ; Karamanos, Nikos K. ; Theocharis, Dimitrios A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c398t-b302cda37050c090870924f761cdf9e4544a4e1dd8cbacd931a3005f4975a44b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Adult</topic><topic>Aggrecan degradation</topic><topic>Aggrecans</topic><topic>Aggregable aggrecan</topic><topic>Carcinoma, Squamous Cell - metabolism</topic><topic>Cartilage</topic><topic>Cartilage - metabolism</topic><topic>Cartilage - pathology</topic><topic>Chondroitin Sulfate Proteoglycans - biosynthesis</topic><topic>Chondroitin Sulfate Proteoglycans - chemistry</topic><topic>Extracellular Matrix Proteins - biosynthesis</topic><topic>Extracellular Matrix Proteins - chemistry</topic><topic>Gene Expression Regulation, Neoplastic</topic><topic>Glycosaminoglycans - chemistry</topic><topic>Humans</topic><topic>Immunohistochemistry</topic><topic>Laryngeal cancer</topic><topic>Laryngeal Neoplasms - metabolism</topic><topic>Lectins, C-Type - biosynthesis</topic><topic>Lectins, C-Type - chemistry</topic><topic>Male</topic><topic>Middle Aged</topic><topic>Peptides - chemistry</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Proteoglycans</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Skandalis, Spyros S.</creatorcontrib><creatorcontrib>Theocharis, Achilleas D.</creatorcontrib><creatorcontrib>Vynios, Demitrios H.</creatorcontrib><creatorcontrib>Papageorgakopoulou, Nickoletta</creatorcontrib><creatorcontrib>Hjerpe, Anders</creatorcontrib><creatorcontrib>Karamanos, Nikos K.</creatorcontrib><creatorcontrib>Theocharis, Dimitrios A.</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>SwePub</collection><collection>SwePub Articles</collection><jtitle>Biochimica et biophysica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Skandalis, Spyros S.</au><au>Theocharis, Achilleas D.</au><au>Vynios, Demitrios H.</au><au>Papageorgakopoulou, Nickoletta</au><au>Hjerpe, Anders</au><au>Karamanos, Nikos K.</au><au>Theocharis, Dimitrios A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cartilage aggrecan undergoes significant compositional and structural alterations during laryngeal cancer</atitle><jtitle>Biochimica et biophysica acta</jtitle><addtitle>Biochim Biophys Acta</addtitle><date>2006-07-01</date><risdate>2006</risdate><volume>1760</volume><issue>7</issue><spage>1046</spage><epage>1053</epage><pages>1046-1053</pages><issn>0304-4165</issn><issn>0006-3002</issn><eissn>1872-8006</eissn><abstract>Aggrecan is a key component of cartilage and is responsible for the integrity and function of the tissue. In this study, the content of aggrecan and its structural modifications in adjacent to cancer apparently normal cartilages (AANCs) from various stages of laryngeal squamous cell carcinoma (LSCC) were investigated. Our data demonstrated a stage-related loss of aggregable aggrecan in AANCs, compared to the healthy laryngeal cartilage (HLC), which was excessive in advanced stages of disease. On aggregable aggrecan level, AANCs were characterized by significant compositional and structural modifications, the extent of which was closely related with the stage of LSCC. Four concrete subpopulations of aggregable molecules with particular physicochemical characteristics were identified with a strong tendency to prevail subpopulations of molecules of lower hydrodynamic sizes with increasing LSCC stage. These findings demonstrated that the cleavage of aggregable aggrecan occurred in concrete peptide bonds within the CS-1 and CS-2 attachment domains. These significant alterations were closely associated with the process of cartilage destruction, indicating the crucial role of aggrecan during LSCC.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>16574327</pmid><doi>10.1016/j.bbagen.2006.02.007</doi><tpages>8</tpages></addata></record> |
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subjects | Adult Aggrecan degradation Aggrecans Aggregable aggrecan Carcinoma, Squamous Cell - metabolism Cartilage Cartilage - metabolism Cartilage - pathology Chondroitin Sulfate Proteoglycans - biosynthesis Chondroitin Sulfate Proteoglycans - chemistry Extracellular Matrix Proteins - biosynthesis Extracellular Matrix Proteins - chemistry Gene Expression Regulation, Neoplastic Glycosaminoglycans - chemistry Humans Immunohistochemistry Laryngeal cancer Laryngeal Neoplasms - metabolism Lectins, C-Type - biosynthesis Lectins, C-Type - chemistry Male Middle Aged Peptides - chemistry Protein Binding Protein Structure, Tertiary Proteoglycans |
title | Cartilage aggrecan undergoes significant compositional and structural alterations during laryngeal cancer |
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