Hyaluronan enhances cartilage repair through low grade tissue remodeling involving cytokines and matrix metalloproteinases
To determine whether the ability of high molecular weight hyaluronan (HA) to reverse cartilage damage caused by specific catabolic mediators of cartilage damage, fibronectin fragments (Fn-fs), occurs through a low grade of enhanced catabolic events such as enhanced matrix metalloproteinase (MMP) exp...
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| Veröffentlicht in: | Inflammation research 2004-10, Vol.53 (10), p.534-543 |
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| creator | Homandberg, G A Ummadi, V Kang, H |
| description | To determine whether the ability of high molecular weight hyaluronan (HA) to reverse cartilage damage caused by specific catabolic mediators of cartilage damage, fibronectin fragments (Fn-fs), occurs through a low grade of enhanced catabolic events such as enhanced matrix metalloproteinase (MMP) expression or cytokine activities.
HA from 6.8-kDa to 2 million daltons was studied.
The ability of HA to enhance matrix metalloproteinase-3 (MMP-3) epitopes and cartilage proteoglycan (PG) degradation neoepitopes was tested in bovine cartilage, as well as the ability of recombinant human interleukin-1 receptor antagonist protein (rhIRAP) to reverse PG depletion in cartilage first exposed to Fn-f.
All HA forms enhanced MMP-3 epitopes and PG degradation in normal undamaged cartilage and in the case of HA800, the degradation was not sufficient to decrease steady state levels of cartilage PG. When HA800 was added to Fn-f damaged cartilage, restoration of PG occurred, but this was blocked by rhIRAP.
These results collectively suggest that some of the repair activity of HA800 is through proteolytic activity which is not sufficient to decrease matrix PG content, but is nonetheless elevated above levels in cartilage not treated with HA800. |
| doi_str_mv | 10.1007/s00011-004-1292-y |
| format | Article |
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HA from 6.8-kDa to 2 million daltons was studied.
The ability of HA to enhance matrix metalloproteinase-3 (MMP-3) epitopes and cartilage proteoglycan (PG) degradation neoepitopes was tested in bovine cartilage, as well as the ability of recombinant human interleukin-1 receptor antagonist protein (rhIRAP) to reverse PG depletion in cartilage first exposed to Fn-f.
All HA forms enhanced MMP-3 epitopes and PG degradation in normal undamaged cartilage and in the case of HA800, the degradation was not sufficient to decrease steady state levels of cartilage PG. When HA800 was added to Fn-f damaged cartilage, restoration of PG occurred, but this was blocked by rhIRAP.
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HA from 6.8-kDa to 2 million daltons was studied.
The ability of HA to enhance matrix metalloproteinase-3 (MMP-3) epitopes and cartilage proteoglycan (PG) degradation neoepitopes was tested in bovine cartilage, as well as the ability of recombinant human interleukin-1 receptor antagonist protein (rhIRAP) to reverse PG depletion in cartilage first exposed to Fn-f.
All HA forms enhanced MMP-3 epitopes and PG degradation in normal undamaged cartilage and in the case of HA800, the degradation was not sufficient to decrease steady state levels of cartilage PG. When HA800 was added to Fn-f damaged cartilage, restoration of PG occurred, but this was blocked by rhIRAP.
These results collectively suggest that some of the repair activity of HA800 is through proteolytic activity which is not sufficient to decrease matrix PG content, but is nonetheless elevated above levels in cartilage not treated with HA800.</description><subject>Animals</subject><subject>Blotting, Western</subject><subject>Cartilage - drug effects</subject><subject>Cartilage - metabolism</subject><subject>Cattle</subject><subject>Culture Media, Conditioned - pharmacology</subject><subject>Culture Media, Serum-Free - metabolism</subject><subject>Cytokines - metabolism</subject><subject>Endopeptidases - chemistry</subject><subject>Epitopes - chemistry</subject><subject>Fibronectins - chemistry</subject><subject>Fibronectins - metabolism</subject><subject>Humans</subject><subject>Hyaluronic Acid - chemistry</subject><subject>Hyaluronic Acid - pharmacology</subject><subject>Immunohistochemistry</subject><subject>Insulin-Like Growth Factor I - metabolism</subject><subject>Interleukin 1 Receptor Antagonist Protein</subject><subject>Kinetics</subject><subject>Matrix Metalloproteinase 3 - chemistry</subject><subject>Matrix Metalloproteinases - metabolism</subject><subject>Oligopeptides - chemistry</subject><subject>Peptide Fragments - chemistry</subject><subject>Polymyxin B - chemistry</subject><subject>Prostaglandins - metabolism</subject><subject>Recombinant Proteins - chemistry</subject><subject>Sialoglycoproteins - chemistry</subject><subject>Time Factors</subject><issn>1023-3830</issn><issn>1420-908X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNpdkUFrFTEQx4MotlY_gBcJHrytzmSzb7NHKWoLhV4s9Bay2eS91GzyTLK166c3j_dA6GkG5jf_GfgR8h7hMwL0XzIAIDYAvEE2sGZ9Qc6RM2gGEPcvaw-sbVrRwhl5k_NDpQUT7DU5w64beuTinPy9WpVfUgwqUBN2KmiTqVapOK-2hiazVy7Rsktx2e6oj3_oNqnJ0OJyXg7zOU7Gu7ClLjxG_3jo9FriLxdqkAoTnVVJ7onOpijv4z7FYlxQ2eS35JVVPpt3p3pB7r5_-3l51dzc_ri-_HrT6JZtSiMGtAq0GLEXveZgRy6mgYmNtdhp3vGNwdYi9Gh5ZQAsV9oOCkeLmo-qvSCfjrn19u_F5CJnl7XxXgUTlyxrbtd1TFTw4zPwIS4p1N8kww1rGW9ZhfAI6RRzTsbKfXKzSqtEkAcr8mhFVivyYEWudefDKXgZZzP93zhpaP8BGR6LfQ</recordid><startdate>200410</startdate><enddate>200410</enddate><creator>Homandberg, G A</creator><creator>Ummadi, V</creator><creator>Kang, H</creator><general>Springer Nature 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>3V.</scope><scope>7QL</scope><scope>7T5</scope><scope>7T7</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>BENPR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>H94</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope></search><sort><creationdate>200410</creationdate><title>Hyaluronan enhances cartilage repair through low grade tissue remodeling involving cytokines and matrix metalloproteinases</title><author>Homandberg, G A ; Ummadi, V ; Kang, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c326t-891fa0c8b1787c40fb48d9286ff15c4546e13f1071f4b1700f4acf9a1bf1c4ba3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animals</topic><topic>Blotting, Western</topic><topic>Cartilage - drug effects</topic><topic>Cartilage - metabolism</topic><topic>Cattle</topic><topic>Culture Media, Conditioned - pharmacology</topic><topic>Culture Media, Serum-Free - metabolism</topic><topic>Cytokines - metabolism</topic><topic>Endopeptidases - chemistry</topic><topic>Epitopes - chemistry</topic><topic>Fibronectins - chemistry</topic><topic>Fibronectins - metabolism</topic><topic>Humans</topic><topic>Hyaluronic Acid - chemistry</topic><topic>Hyaluronic Acid - pharmacology</topic><topic>Immunohistochemistry</topic><topic>Insulin-Like Growth Factor I - metabolism</topic><topic>Interleukin 1 Receptor Antagonist Protein</topic><topic>Kinetics</topic><topic>Matrix Metalloproteinase 3 - chemistry</topic><topic>Matrix Metalloproteinases - metabolism</topic><topic>Oligopeptides - chemistry</topic><topic>Peptide Fragments - chemistry</topic><topic>Polymyxin B - chemistry</topic><topic>Prostaglandins - metabolism</topic><topic>Recombinant Proteins - chemistry</topic><topic>Sialoglycoproteins - chemistry</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Homandberg, G A</creatorcontrib><creatorcontrib>Ummadi, V</creatorcontrib><creatorcontrib>Kang, H</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><jtitle>Inflammation research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Homandberg, G A</au><au>Ummadi, V</au><au>Kang, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hyaluronan enhances cartilage repair through low grade tissue remodeling involving cytokines and matrix metalloproteinases</atitle><jtitle>Inflammation research</jtitle><addtitle>Inflamm Res</addtitle><date>2004-10</date><risdate>2004</risdate><volume>53</volume><issue>10</issue><spage>534</spage><epage>543</epage><pages>534-543</pages><issn>1023-3830</issn><eissn>1420-908X</eissn><abstract>To determine whether the ability of high molecular weight hyaluronan (HA) to reverse cartilage damage caused by specific catabolic mediators of cartilage damage, fibronectin fragments (Fn-fs), occurs through a low grade of enhanced catabolic events such as enhanced matrix metalloproteinase (MMP) expression or cytokine activities.
HA from 6.8-kDa to 2 million daltons was studied.
The ability of HA to enhance matrix metalloproteinase-3 (MMP-3) epitopes and cartilage proteoglycan (PG) degradation neoepitopes was tested in bovine cartilage, as well as the ability of recombinant human interleukin-1 receptor antagonist protein (rhIRAP) to reverse PG depletion in cartilage first exposed to Fn-f.
All HA forms enhanced MMP-3 epitopes and PG degradation in normal undamaged cartilage and in the case of HA800, the degradation was not sufficient to decrease steady state levels of cartilage PG. When HA800 was added to Fn-f damaged cartilage, restoration of PG occurred, but this was blocked by rhIRAP.
These results collectively suggest that some of the repair activity of HA800 is through proteolytic activity which is not sufficient to decrease matrix PG content, but is nonetheless elevated above levels in cartilage not treated with HA800.</abstract><cop>Switzerland</cop><pub>Springer Nature B.V</pub><pmid>15597148</pmid><doi>10.1007/s00011-004-1292-y</doi><tpages>10</tpages></addata></record> |
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| subjects | Animals Blotting, Western Cartilage - drug effects Cartilage - metabolism Cattle Culture Media, Conditioned - pharmacology Culture Media, Serum-Free - metabolism Cytokines - metabolism Endopeptidases - chemistry Epitopes - chemistry Fibronectins - chemistry Fibronectins - metabolism Humans Hyaluronic Acid - chemistry Hyaluronic Acid - pharmacology Immunohistochemistry Insulin-Like Growth Factor I - metabolism Interleukin 1 Receptor Antagonist Protein Kinetics Matrix Metalloproteinase 3 - chemistry Matrix Metalloproteinases - metabolism Oligopeptides - chemistry Peptide Fragments - chemistry Polymyxin B - chemistry Prostaglandins - metabolism Recombinant Proteins - chemistry Sialoglycoproteins - chemistry Time Factors |
| title | Hyaluronan enhances cartilage repair through low grade tissue remodeling involving cytokines and matrix metalloproteinases |
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