Neoepitopes reveal the features of type II collagen cleavage and the identity of a collagenase involved in the transformation of the epiphyses anlagen in development
In long bone development, the evolution of the cartilaginous anlagen into a secondary ossification center is initiated by the formation of canals. The excavation to create the canals is achieved through lysis of the two major cartilage components, aggrecan, and the type II collagen (COL2) fibril. Th...
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| Veröffentlicht in: | Developmental dynamics 2009-06, Vol.238 (6), p.1547-1563 |
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| creator | Lee, Eunice R. Lamplugh, Lisa Kluczyk, Beata Leblond, Charles P. Mort, John S. |
| description | In long bone development, the evolution of the cartilaginous anlagen into a secondary ossification center is initiated by the formation of canals. The excavation to create the canals is achieved through lysis of the two major cartilage components, aggrecan, and the type II collagen (COL2) fibril. The present study examines the lysis of the fibril. Because it is known that matrix metalloproteinases (MMPs) cleave COL2 in vitro at the Gly775‐Leu776 bond, it has been reasoned that, if such cleavage is detected in relation to the canals, it can be concluded that a collagenase is involved. Furthermore, because MMPs undergo change in domain structure with activation resulting in propeptide domain loss then, if such a loss is revealed in relation to the cleavage of COL2, this MMP is likely involved. The collective findings reveal that COL2 is attacked at the afore‐described susceptible peptide bond at the surface of cartilage canals and, that MMP‐13 cleaves it. Developmental Dynamics 238:1547–1563, 2009. © 2009 Wiley‐Liss, Inc. |
| doi_str_mv | 10.1002/dvdy.21960 |
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The excavation to create the canals is achieved through lysis of the two major cartilage components, aggrecan, and the type II collagen (COL2) fibril. The present study examines the lysis of the fibril. Because it is known that matrix metalloproteinases (MMPs) cleave COL2 in vitro at the Gly775‐Leu776 bond, it has been reasoned that, if such cleavage is detected in relation to the canals, it can be concluded that a collagenase is involved. Furthermore, because MMPs undergo change in domain structure with activation resulting in propeptide domain loss then, if such a loss is revealed in relation to the cleavage of COL2, this MMP is likely involved. The collective findings reveal that COL2 is attacked at the afore‐described susceptible peptide bond at the surface of cartilage canals and, that MMP‐13 cleaves it. Developmental Dynamics 238:1547–1563, 2009. © 2009 Wiley‐Liss, Inc.</description><identifier>ISSN: 1058-8388</identifier><identifier>EISSN: 1097-0177</identifier><identifier>DOI: 10.1002/dvdy.21960</identifier><identifier>PMID: 19441084</identifier><language>eng</language><publisher>New York: Wiley‐Liss, Inc</publisher><subject>Aggrecans - metabolism ; angiogenesis and endothelium ; Animals ; Antibodies - metabolism ; anti‐neoepitope antibodies ; COL2 ; collagen biomarkers ; collagen fragments ; Collagen Type II - genetics ; Collagen Type II - metabolism ; Collagenases - metabolism ; CTX‐II ; Enzyme Activation ; Epiphyses - anatomy & histology ; Epiphyses - embryology ; Epitopes ; Isoenzymes - genetics ; Isoenzymes - metabolism ; Matrix Metalloproteinase 13 - genetics ; Matrix Metalloproteinase 13 - metabolism ; Matrix Metalloproteinase 14 - metabolism ; Mice ; Mice, Inbred C57BL ; MMP activation ; MMPs ; MMP‐13 ; Protein Precursors - metabolism ; Rats ; Rats, Sprague-Dawley ; skeletal development ; type II collagen</subject><ispartof>Developmental dynamics, 2009-06, Vol.238 (6), p.1547-1563</ispartof><rights>Copyright © 2009 Wiley‐Liss, Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3940-d9d68b58905214a771416c8d99f79696bd29b7bc660afa8b666d67c17949e4e03</citedby><cites>FETCH-LOGICAL-c3940-d9d68b58905214a771416c8d99f79696bd29b7bc660afa8b666d67c17949e4e03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fdvdy.21960$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fdvdy.21960$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19441084$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, Eunice R.</creatorcontrib><creatorcontrib>Lamplugh, Lisa</creatorcontrib><creatorcontrib>Kluczyk, Beata</creatorcontrib><creatorcontrib>Leblond, Charles P.</creatorcontrib><creatorcontrib>Mort, John S.</creatorcontrib><title>Neoepitopes reveal the features of type II collagen cleavage and the identity of a collagenase involved in the transformation of the epiphyses anlagen in development</title><title>Developmental dynamics</title><addtitle>Dev Dyn</addtitle><description>In long bone development, the evolution of the cartilaginous anlagen into a secondary ossification center is initiated by the formation of canals. The excavation to create the canals is achieved through lysis of the two major cartilage components, aggrecan, and the type II collagen (COL2) fibril. The present study examines the lysis of the fibril. Because it is known that matrix metalloproteinases (MMPs) cleave COL2 in vitro at the Gly775‐Leu776 bond, it has been reasoned that, if such cleavage is detected in relation to the canals, it can be concluded that a collagenase is involved. Furthermore, because MMPs undergo change in domain structure with activation resulting in propeptide domain loss then, if such a loss is revealed in relation to the cleavage of COL2, this MMP is likely involved. The collective findings reveal that COL2 is attacked at the afore‐described susceptible peptide bond at the surface of cartilage canals and, that MMP‐13 cleaves it. Developmental Dynamics 238:1547–1563, 2009. © 2009 Wiley‐Liss, Inc.</description><subject>Aggrecans - metabolism</subject><subject>angiogenesis and endothelium</subject><subject>Animals</subject><subject>Antibodies - metabolism</subject><subject>anti‐neoepitope antibodies</subject><subject>COL2</subject><subject>collagen biomarkers</subject><subject>collagen fragments</subject><subject>Collagen Type II - genetics</subject><subject>Collagen Type II - metabolism</subject><subject>Collagenases - metabolism</subject><subject>CTX‐II</subject><subject>Enzyme Activation</subject><subject>Epiphyses - anatomy & histology</subject><subject>Epiphyses - embryology</subject><subject>Epitopes</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - metabolism</subject><subject>Matrix Metalloproteinase 13 - genetics</subject><subject>Matrix Metalloproteinase 13 - metabolism</subject><subject>Matrix Metalloproteinase 14 - metabolism</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>MMP activation</subject><subject>MMPs</subject><subject>MMP‐13</subject><subject>Protein Precursors - metabolism</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>skeletal development</subject><subject>type II collagen</subject><issn>1058-8388</issn><issn>1097-0177</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctO3TAQhq2qqFzKpg9QZdUFUsCT-PiyrLgeCcEGKrGKnHhSUiVxavsE5YF4T5yTo7IrK4_Gn74Z-yfkG9BToDQ7M6OZTjNQnH4iB0CVSCkI8XmuVzKVuZT75ND7P5RSyRl8IfugGAMq2QF5vUOLQxPsgD5xOKJuk_CMSY06bFzs2ToJ04DJep1Utm31b-yTqkU9xirRvdnSjcE-NGGaaf2P0z7e9KNtRzSx2JLB6d7X1nU6NLbf2mM3bjA8Tz6O0_0yIuImbtPaoYvqr2Sv1q3H4915RB6vLh_Ob9Lb--v1-c_btMoVo6lRhstyJRVdZcC0EMCAV9IoVQvFFS9NpkpRVpxTXWtZcs4NFxUIxRQypPkR-bF4B2f_btCHomt8hfE5PdqNL7jIIf5c_iGYUaEUwGw8WcDKWe8d1sXgmk67qQBazOkVc3rFNr0If99ZN2WH5h3dxRUBWICXpsXpP6ri4tfF0yJ9A5Mzp-Q</recordid><startdate>200906</startdate><enddate>200906</enddate><creator>Lee, Eunice R.</creator><creator>Lamplugh, Lisa</creator><creator>Kluczyk, Beata</creator><creator>Leblond, Charles P.</creator><creator>Mort, John S.</creator><general>Wiley‐Liss, Inc</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>7QP</scope><scope>7X8</scope></search><sort><creationdate>200906</creationdate><title>Neoepitopes reveal the features of type II collagen cleavage and the identity of a collagenase involved in the transformation of the epiphyses anlagen in development</title><author>Lee, Eunice R. ; 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The excavation to create the canals is achieved through lysis of the two major cartilage components, aggrecan, and the type II collagen (COL2) fibril. The present study examines the lysis of the fibril. Because it is known that matrix metalloproteinases (MMPs) cleave COL2 in vitro at the Gly775‐Leu776 bond, it has been reasoned that, if such cleavage is detected in relation to the canals, it can be concluded that a collagenase is involved. Furthermore, because MMPs undergo change in domain structure with activation resulting in propeptide domain loss then, if such a loss is revealed in relation to the cleavage of COL2, this MMP is likely involved. The collective findings reveal that COL2 is attacked at the afore‐described susceptible peptide bond at the surface of cartilage canals and, that MMP‐13 cleaves it. 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| subjects | Aggrecans - metabolism angiogenesis and endothelium Animals Antibodies - metabolism anti‐neoepitope antibodies COL2 collagen biomarkers collagen fragments Collagen Type II - genetics Collagen Type II - metabolism Collagenases - metabolism CTX‐II Enzyme Activation Epiphyses - anatomy & histology Epiphyses - embryology Epitopes Isoenzymes - genetics Isoenzymes - metabolism Matrix Metalloproteinase 13 - genetics Matrix Metalloproteinase 13 - metabolism Matrix Metalloproteinase 14 - metabolism Mice Mice, Inbred C57BL MMP activation MMPs MMP‐13 Protein Precursors - metabolism Rats Rats, Sprague-Dawley skeletal development type II collagen |
| title | Neoepitopes reveal the features of type II collagen cleavage and the identity of a collagenase involved in the transformation of the epiphyses anlagen in development |
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