Biophysical Characterization of the C-propeptide Trimer from Human Procollagen III Reveals a Tri-lobed Structure
Procollagen C-propeptide domains direct chain association during intracellular assembly of procollagen molecules. In addition, they control collagen solubility during extracellular proteolytic processing and fibril formation and interact with cell surface receptors and extracellular matrix component...
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| Veröffentlicht in: | The Journal of biological chemistry 2001-12, Vol.276 (52), p.48930-48936 |
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| container_end_page | 48936 |
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| container_issue | 52 |
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| container_title | The Journal of biological chemistry |
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| creator | Bernocco, Simonetta Finet, Stéphanie Ebel, Christine Eichenberger, Denise Mazzorana, Marlène Farjanel, Jean Hulmes, David J.S. |
| description | Procollagen C-propeptide domains direct chain association during intracellular assembly of procollagen molecules. In addition, they control collagen solubility during extracellular proteolytic processing and fibril formation and interact with cell surface receptors and extracellular matrix components involved in feedback inhibition, mineralization, cell growth arrest, and chemotaxis. At present, three-dimensional structural information for the C-propeptides, which would help to understand the underlying molecular mechanisms, is lacking. Here we have carried out a biophysical study of the recombinant C-propeptide trimer from human procollagen III using laser light scattering, analytical ultracentrifugation, and small angle x-ray scattering. The results show that the trimer is an elongated molecule, which by modeling of the x-ray scattering data appears to be cruciform in shape with three large lobes and one minor lobe. We speculate that each of the major lobes corresponds to one of the three component polypeptide chains, which come together in a junction region to connect to the rest of the procollagen molecule. |
| doi_str_mv | 10.1074/jbc.M108611200 |
| format | Article |
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In addition, they control collagen solubility during extracellular proteolytic processing and fibril formation and interact with cell surface receptors and extracellular matrix components involved in feedback inhibition, mineralization, cell growth arrest, and chemotaxis. At present, three-dimensional structural information for the C-propeptides, which would help to understand the underlying molecular mechanisms, is lacking. Here we have carried out a biophysical study of the recombinant C-propeptide trimer from human procollagen III using laser light scattering, analytical ultracentrifugation, and small angle x-ray scattering. The results show that the trimer is an elongated molecule, which by modeling of the x-ray scattering data appears to be cruciform in shape with three large lobes and one minor lobe. We speculate that each of the major lobes corresponds to one of the three component polypeptide chains, which come together in a junction region to connect to the rest of the procollagen molecule.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M108611200</identifier><identifier>PMID: 11684689</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Biochemistry, Molecular Biology ; Cell Line ; Collagen Type III - chemistry ; Collagen Type III - metabolism ; Culture Media, Serum-Free ; Humans ; Life Sciences ; Models, Molecular ; Procollagen - chemistry ; Procollagen - isolation & purification ; Procollagen - metabolism ; Protein Structure, Quaternary ; Recombinant Proteins - chemistry ; Recombinant Proteins - isolation & purification ; Scattering, Radiation ; Solutions ; Ultracentrifugation</subject><ispartof>The Journal of biological chemistry, 2001-12, Vol.276 (52), p.48930-48936</ispartof><rights>2001 © 2001 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c443t-53108b77c9691a55288d711d78a4df3836815daeb195116ebd334a425518709a3</citedby><cites>FETCH-LOGICAL-c443t-53108b77c9691a55288d711d78a4df3836815daeb195116ebd334a425518709a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,777,781,882,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11684689$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00313825$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Bernocco, Simonetta</creatorcontrib><creatorcontrib>Finet, Stéphanie</creatorcontrib><creatorcontrib>Ebel, Christine</creatorcontrib><creatorcontrib>Eichenberger, Denise</creatorcontrib><creatorcontrib>Mazzorana, Marlène</creatorcontrib><creatorcontrib>Farjanel, Jean</creatorcontrib><creatorcontrib>Hulmes, David J.S.</creatorcontrib><title>Biophysical Characterization of the C-propeptide Trimer from Human Procollagen III Reveals a Tri-lobed Structure</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Procollagen C-propeptide domains direct chain association during intracellular assembly of procollagen molecules. In addition, they control collagen solubility during extracellular proteolytic processing and fibril formation and interact with cell surface receptors and extracellular matrix components involved in feedback inhibition, mineralization, cell growth arrest, and chemotaxis. At present, three-dimensional structural information for the C-propeptides, which would help to understand the underlying molecular mechanisms, is lacking. Here we have carried out a biophysical study of the recombinant C-propeptide trimer from human procollagen III using laser light scattering, analytical ultracentrifugation, and small angle x-ray scattering. The results show that the trimer is an elongated molecule, which by modeling of the x-ray scattering data appears to be cruciform in shape with three large lobes and one minor lobe. We speculate that each of the major lobes corresponds to one of the three component polypeptide chains, which come together in a junction region to connect to the rest of the procollagen molecule.</description><subject>Biochemistry, Molecular Biology</subject><subject>Cell Line</subject><subject>Collagen Type III - chemistry</subject><subject>Collagen Type III - metabolism</subject><subject>Culture Media, Serum-Free</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Models, Molecular</subject><subject>Procollagen - chemistry</subject><subject>Procollagen - isolation & purification</subject><subject>Procollagen - metabolism</subject><subject>Protein Structure, Quaternary</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Scattering, Radiation</subject><subject>Solutions</subject><subject>Ultracentrifugation</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kcGP1CAYxYnRuLOrV4-GgzHZQ0coUOhxnagzyRiNrok3QuHrlk1bKrRj1r9eJjNxT3KBwO97eY-H0CtK1pRI_u6-sevPlKiK0pKQJ2iVz6xggv58ilaElLSoS6Eu0GVK9yQvXtPn6ILSSvFK1Ss0vfdh6h6St6bHm85EY2eI_o-ZfRhxaPHcAd4UUwwTTLN3gG-jHyDiNoYBb5fBjPhrDDb0vbmDEe92O_wNDmD6hM2RLfrQgMPf57jYeYnwAj1r8yO8PO9X6MfHD7ebbbH_8mm3udkXlnM2F4LlII2Utq5qaoQolXKSUieV4a5lilWKCmegobXIaaBxjHHDSyGokqQ27Apdn3Q70-spezbxQQfj9fZmr493hDDKVCkONLNvT2yO-WuBNOvBJws50ghhSVqWTFJOZAbXJ9DGkFKE9p8yJfrYh8596Mc-8sDrs_LSDOAe8XMBGXhztunvut8-gm58sB0MupSVFqXmGTrqqBMG-csOHqJO1sNoweURO2sX_P8s_AUQOqM1</recordid><startdate>20011228</startdate><enddate>20011228</enddate><creator>Bernocco, Simonetta</creator><creator>Finet, Stéphanie</creator><creator>Ebel, Christine</creator><creator>Eichenberger, Denise</creator><creator>Mazzorana, Marlène</creator><creator>Farjanel, Jean</creator><creator>Hulmes, David J.S.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>1XC</scope></search><sort><creationdate>20011228</creationdate><title>Biophysical Characterization of the C-propeptide Trimer from Human Procollagen III Reveals a Tri-lobed Structure</title><author>Bernocco, Simonetta ; Finet, Stéphanie ; Ebel, Christine ; Eichenberger, Denise ; Mazzorana, Marlène ; Farjanel, Jean ; Hulmes, David J.S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-53108b77c9691a55288d711d78a4df3836815daeb195116ebd334a425518709a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Biochemistry, Molecular Biology</topic><topic>Cell Line</topic><topic>Collagen Type III - chemistry</topic><topic>Collagen Type III - metabolism</topic><topic>Culture Media, Serum-Free</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Models, Molecular</topic><topic>Procollagen - chemistry</topic><topic>Procollagen - isolation & purification</topic><topic>Procollagen - metabolism</topic><topic>Protein Structure, Quaternary</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Scattering, Radiation</topic><topic>Solutions</topic><topic>Ultracentrifugation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bernocco, Simonetta</creatorcontrib><creatorcontrib>Finet, Stéphanie</creatorcontrib><creatorcontrib>Ebel, Christine</creatorcontrib><creatorcontrib>Eichenberger, Denise</creatorcontrib><creatorcontrib>Mazzorana, Marlène</creatorcontrib><creatorcontrib>Farjanel, Jean</creatorcontrib><creatorcontrib>Hulmes, David J.S.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Hyper Article en Ligne (HAL)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bernocco, Simonetta</au><au>Finet, Stéphanie</au><au>Ebel, Christine</au><au>Eichenberger, Denise</au><au>Mazzorana, Marlène</au><au>Farjanel, Jean</au><au>Hulmes, David J.S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biophysical Characterization of the C-propeptide Trimer from Human Procollagen III Reveals a Tri-lobed Structure</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2001-12-28</date><risdate>2001</risdate><volume>276</volume><issue>52</issue><spage>48930</spage><epage>48936</epage><pages>48930-48936</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Procollagen C-propeptide domains direct chain association during intracellular assembly of procollagen molecules. In addition, they control collagen solubility during extracellular proteolytic processing and fibril formation and interact with cell surface receptors and extracellular matrix components involved in feedback inhibition, mineralization, cell growth arrest, and chemotaxis. At present, three-dimensional structural information for the C-propeptides, which would help to understand the underlying molecular mechanisms, is lacking. Here we have carried out a biophysical study of the recombinant C-propeptide trimer from human procollagen III using laser light scattering, analytical ultracentrifugation, and small angle x-ray scattering. The results show that the trimer is an elongated molecule, which by modeling of the x-ray scattering data appears to be cruciform in shape with three large lobes and one minor lobe. 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| subjects | Biochemistry, Molecular Biology Cell Line Collagen Type III - chemistry Collagen Type III - metabolism Culture Media, Serum-Free Humans Life Sciences Models, Molecular Procollagen - chemistry Procollagen - isolation & purification Procollagen - metabolism Protein Structure, Quaternary Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Scattering, Radiation Solutions Ultracentrifugation |
| title | Biophysical Characterization of the C-propeptide Trimer from Human Procollagen III Reveals a Tri-lobed Structure |
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