Characterization of recombinant human cementum protein 1 ( hrCEMP1): Primary role in biomineralization
Cementum protein 1 (CEMP1) has been recently cloned, and in vitro experiments have shown functions as regulator of cementoblast behavior and inducer of differentiation of non-osteogenic cells toward a cementoblastic/osteoblastic phenotype. In this study, we have produced a full-length human recombin...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2009-06, Vol.384 (1), p.49-54 |
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| creator | Villarreal-Ramírez, Eduardo Moreno, Abel Mas-Oliva, Jaime Chávez-Pacheco, Juan Luis Narayanan, A. Sampath Gil-Chavarría, Ivet Zeichner-David, Margarita Arzate, Higinio |
| description | Cementum protein 1 (CEMP1) has been recently cloned, and
in vitro experiments have shown functions as regulator of cementoblast behavior and inducer of differentiation of non-osteogenic cells toward a cementoblastic/osteoblastic phenotype. In this study, we have produced a full-length human recombinant CEMP1 protein in a human gingival fibroblast cell line. The purified protein (
hrCEMP1) has a M
r 50,000. Characterization of
hrCEMP1 indicates that its secondary structure is mainly composed of β-sheet (55%), where random coil and alpha helix conformations correspond to 35% and 10%, respectively. It was found that
hrCEMP1 is
N-glycosylated, phosphorylated and possesses strong affinity for hydroxyapatite. Even more important, our results show that
hrCEMP1 plays a role during the biomineralization process by promoting octacalcium phosphate (OCP) crystal nucleation. These features make CEMP1 a very good candidate for biotechnological applications in order to achieve cementum and/or bone regeneration. |
| doi_str_mv | 10.1016/j.bbrc.2009.04.072 |
| format | Article |
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in vitro experiments have shown functions as regulator of cementoblast behavior and inducer of differentiation of non-osteogenic cells toward a cementoblastic/osteoblastic phenotype. In this study, we have produced a full-length human recombinant CEMP1 protein in a human gingival fibroblast cell line. The purified protein (
hrCEMP1) has a M
r 50,000. Characterization of
hrCEMP1 indicates that its secondary structure is mainly composed of β-sheet (55%), where random coil and alpha helix conformations correspond to 35% and 10%, respectively. It was found that
hrCEMP1 is
N-glycosylated, phosphorylated and possesses strong affinity for hydroxyapatite. Even more important, our results show that
hrCEMP1 plays a role during the biomineralization process by promoting octacalcium phosphate (OCP) crystal nucleation. These features make CEMP1 a very good candidate for biotechnological applications in order to achieve cementum and/or bone regeneration.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2009.04.072</identifier><identifier>PMID: 19393626</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Biomineralization ; Calcification, Physiologic ; Cementum ; Cementum protein 1 ; Durapatite - chemistry ; Fibroblasts - metabolism ; Gingiva - cytology ; Gingiva - metabolism ; Glycosylation ; Humans ; Hydroxyapatite ; Mineralized tissues ; Octacalcium phosphate ; Periodontal regeneration ; Phosphorylation ; Protein Structure, Secondary ; Proteins - chemistry ; Proteins - genetics ; Proteins - metabolism ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics</subject><ispartof>Biochemical and biophysical research communications, 2009-06, Vol.384 (1), p.49-54</ispartof><rights>2009 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c451t-5e7c5e196d4ec68dd54cf12252f45371342844a5973092b82c681333a07889c3</citedby><cites>FETCH-LOGICAL-c451t-5e7c5e196d4ec68dd54cf12252f45371342844a5973092b82c681333a07889c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2009.04.072$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19393626$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Villarreal-Ramírez, Eduardo</creatorcontrib><creatorcontrib>Moreno, Abel</creatorcontrib><creatorcontrib>Mas-Oliva, Jaime</creatorcontrib><creatorcontrib>Chávez-Pacheco, Juan Luis</creatorcontrib><creatorcontrib>Narayanan, A. Sampath</creatorcontrib><creatorcontrib>Gil-Chavarría, Ivet</creatorcontrib><creatorcontrib>Zeichner-David, Margarita</creatorcontrib><creatorcontrib>Arzate, Higinio</creatorcontrib><title>Characterization of recombinant human cementum protein 1 ( hrCEMP1): Primary role in biomineralization</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Cementum protein 1 (CEMP1) has been recently cloned, and
in vitro experiments have shown functions as regulator of cementoblast behavior and inducer of differentiation of non-osteogenic cells toward a cementoblastic/osteoblastic phenotype. In this study, we have produced a full-length human recombinant CEMP1 protein in a human gingival fibroblast cell line. The purified protein (
hrCEMP1) has a M
r 50,000. Characterization of
hrCEMP1 indicates that its secondary structure is mainly composed of β-sheet (55%), where random coil and alpha helix conformations correspond to 35% and 10%, respectively. It was found that
hrCEMP1 is
N-glycosylated, phosphorylated and possesses strong affinity for hydroxyapatite. Even more important, our results show that
hrCEMP1 plays a role during the biomineralization process by promoting octacalcium phosphate (OCP) crystal nucleation. These features make CEMP1 a very good candidate for biotechnological applications in order to achieve cementum and/or bone regeneration.</description><subject>Biomineralization</subject><subject>Calcification, Physiologic</subject><subject>Cementum</subject><subject>Cementum protein 1</subject><subject>Durapatite - chemistry</subject><subject>Fibroblasts - metabolism</subject><subject>Gingiva - cytology</subject><subject>Gingiva - metabolism</subject><subject>Glycosylation</subject><subject>Humans</subject><subject>Hydroxyapatite</subject><subject>Mineralized tissues</subject><subject>Octacalcium phosphate</subject><subject>Periodontal regeneration</subject><subject>Phosphorylation</subject><subject>Protein Structure, Secondary</subject><subject>Proteins - chemistry</subject><subject>Proteins - genetics</subject><subject>Proteins - metabolism</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9r3DAQxUVpSLbbfIEeik4lPdgZ_bFslVzCkjaFhOSQQ29ClsesFltKJTuQfvp62YXemtMc5vceM-8R8olByYCpy13ZtsmVHECXIEuo-TuyYqCh4Azke7ICAFVwzX6dkQ857wAYk0qfkjOmhRaKqxXpN1ubrJsw-T928jHQ2NOELo6tDzZMdDuPNlCHI4ZpHulzihP6QBm9oNu0ubl_ZF-_0cfkR5teaYoD0mXb-jj6gMkOR9eP5KS3Q8bz41yTp-83T5vb4u7hx8_N9V3hZMWmosLaVci06iQ61XRdJV3POK94LytRMyF5I6WtdC1A87bhC8SEEBbqptFOrMmXg-1y5u8Z82RGnx0Ogw0Y52xUzaVUSr8Jcqi02oe0JvwAuhRzTtib58OvhoHZt2B2Zt-C2bdgQJqlhUX0-eg-tyN2_yTH2Bfg6gDgksWLx2Sy8xgcdn7JfjJd9P_z_wtNGZd2</recordid><startdate>20090619</startdate><enddate>20090619</enddate><creator>Villarreal-Ramírez, Eduardo</creator><creator>Moreno, Abel</creator><creator>Mas-Oliva, Jaime</creator><creator>Chávez-Pacheco, Juan Luis</creator><creator>Narayanan, A. Sampath</creator><creator>Gil-Chavarría, Ivet</creator><creator>Zeichner-David, Margarita</creator><creator>Arzate, Higinio</creator><general>Elsevier 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>20090619</creationdate><title>Characterization of recombinant human cementum protein 1 ( hrCEMP1): Primary role in biomineralization</title><author>Villarreal-Ramírez, Eduardo ; Moreno, Abel ; Mas-Oliva, Jaime ; Chávez-Pacheco, Juan Luis ; Narayanan, A. Sampath ; Gil-Chavarría, Ivet ; Zeichner-David, Margarita ; Arzate, Higinio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c451t-5e7c5e196d4ec68dd54cf12252f45371342844a5973092b82c681333a07889c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Biomineralization</topic><topic>Calcification, Physiologic</topic><topic>Cementum</topic><topic>Cementum protein 1</topic><topic>Durapatite - chemistry</topic><topic>Fibroblasts - metabolism</topic><topic>Gingiva - cytology</topic><topic>Gingiva - metabolism</topic><topic>Glycosylation</topic><topic>Humans</topic><topic>Hydroxyapatite</topic><topic>Mineralized tissues</topic><topic>Octacalcium phosphate</topic><topic>Periodontal regeneration</topic><topic>Phosphorylation</topic><topic>Protein Structure, Secondary</topic><topic>Proteins - chemistry</topic><topic>Proteins - genetics</topic><topic>Proteins - metabolism</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Villarreal-Ramírez, Eduardo</creatorcontrib><creatorcontrib>Moreno, Abel</creatorcontrib><creatorcontrib>Mas-Oliva, Jaime</creatorcontrib><creatorcontrib>Chávez-Pacheco, Juan Luis</creatorcontrib><creatorcontrib>Narayanan, A. Sampath</creatorcontrib><creatorcontrib>Gil-Chavarría, Ivet</creatorcontrib><creatorcontrib>Zeichner-David, Margarita</creatorcontrib><creatorcontrib>Arzate, Higinio</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Villarreal-Ramírez, Eduardo</au><au>Moreno, Abel</au><au>Mas-Oliva, Jaime</au><au>Chávez-Pacheco, Juan Luis</au><au>Narayanan, A. Sampath</au><au>Gil-Chavarría, Ivet</au><au>Zeichner-David, Margarita</au><au>Arzate, Higinio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of recombinant human cementum protein 1 ( hrCEMP1): Primary role in biomineralization</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2009-06-19</date><risdate>2009</risdate><volume>384</volume><issue>1</issue><spage>49</spage><epage>54</epage><pages>49-54</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Cementum protein 1 (CEMP1) has been recently cloned, and
in vitro experiments have shown functions as regulator of cementoblast behavior and inducer of differentiation of non-osteogenic cells toward a cementoblastic/osteoblastic phenotype. In this study, we have produced a full-length human recombinant CEMP1 protein in a human gingival fibroblast cell line. The purified protein (
hrCEMP1) has a M
r 50,000. Characterization of
hrCEMP1 indicates that its secondary structure is mainly composed of β-sheet (55%), where random coil and alpha helix conformations correspond to 35% and 10%, respectively. It was found that
hrCEMP1 is
N-glycosylated, phosphorylated and possesses strong affinity for hydroxyapatite. Even more important, our results show that
hrCEMP1 plays a role during the biomineralization process by promoting octacalcium phosphate (OCP) crystal nucleation. These features make CEMP1 a very good candidate for biotechnological applications in order to achieve cementum and/or bone regeneration.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>19393626</pmid><doi>10.1016/j.bbrc.2009.04.072</doi><tpages>6</tpages></addata></record> |
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| subjects | Biomineralization Calcification, Physiologic Cementum Cementum protein 1 Durapatite - chemistry Fibroblasts - metabolism Gingiva - cytology Gingiva - metabolism Glycosylation Humans Hydroxyapatite Mineralized tissues Octacalcium phosphate Periodontal regeneration Phosphorylation Protein Structure, Secondary Proteins - chemistry Proteins - genetics Proteins - metabolism Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - genetics |
| title | Characterization of recombinant human cementum protein 1 ( hrCEMP1): Primary role in biomineralization |
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