Osteoinductive capacity and heat stability of recombinant human bone morphogenetic protein-2 produced by Escherichia coli and dimerized by biochemical processing
One problem associated with clinical application of CHO-derived recombinant human bone morphogenetic protein (C-BMP-2) is its high cost due to the need for use of high doses. To solve this problem, Escherichia coli-derived BMP-2 (E-BMP-2) has been examined using the technique of molecular unfolding...
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| Veröffentlicht in: | Journal of bone and mineral metabolism 2009, Vol.27 (3), p.355-363 |
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| creator | Yano, Koichi Hoshino, Masatoshi Ohta, Yoichi Manaka, Tomoya Naka, Yoshifumi Imai, Yuuki Sebald, Walter Takaoka, Kunio |
| description | One problem associated with clinical application of CHO-derived recombinant human bone morphogenetic protein (C-BMP-2) is its high cost due to the need for use of high doses. To solve this problem, Escherichia coli-derived BMP-2 (E-BMP-2) has been examined using the technique of molecular unfolding and refolding. However, it is unclear whether the characteristics of E-BMP-2 are appropriate for clinical application. In this study, we examined the biological activity of E-BMP-2 and its heat tolerance in in vitro and in vivo systems. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) confirmed the high purity of E-BMP-2. E-BMP-2-induced alkaline phosphatase expression in osteoprogenitor cells (C2C12, ST2, and primary murine calvarial osteoblast cells) was dose-dependent, and consistently elicited ectopic new ossicles of significant size in mice, also in dose-dependent fashion. In addition, E-BMP-2 induced phosphorylation of Smad1/5/8 and mRNA expression of osteoblastic differentiation markers to the same extent as C-BMP-2. On the other hand, when E-BMP-2 was exposed to increasing heat over time, its bone-inducing capacity was maintained until reaching 70°C for 2 h or 90°C for 15 min. Thus, E-BMP-2 will exhibit a decrease in activity with the sterilization procedures required prior to use in surgery. These findings indicate that the biological capacity and heat stability of E-BMP-2 are almost equivalent to those of currently available C-BMP-2, and suggest that E-BMP-2 might, thus, solve current problems of cost impeding routine clinical use of rhBMP-2. |
| doi_str_mv | 10.1007/s00774-009-0040-3 |
| format | Article |
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To solve this problem, Escherichia coli-derived BMP-2 (E-BMP-2) has been examined using the technique of molecular unfolding and refolding. However, it is unclear whether the characteristics of E-BMP-2 are appropriate for clinical application. In this study, we examined the biological activity of E-BMP-2 and its heat tolerance in in vitro and in vivo systems. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) confirmed the high purity of E-BMP-2. E-BMP-2-induced alkaline phosphatase expression in osteoprogenitor cells (C2C12, ST2, and primary murine calvarial osteoblast cells) was dose-dependent, and consistently elicited ectopic new ossicles of significant size in mice, also in dose-dependent fashion. In addition, E-BMP-2 induced phosphorylation of Smad1/5/8 and mRNA expression of osteoblastic differentiation markers to the same extent as C-BMP-2. On the other hand, when E-BMP-2 was exposed to increasing heat over time, its bone-inducing capacity was maintained until reaching 70°C for 2 h or 90°C for 15 min. Thus, E-BMP-2 will exhibit a decrease in activity with the sterilization procedures required prior to use in surgery. These findings indicate that the biological capacity and heat stability of E-BMP-2 are almost equivalent to those of currently available C-BMP-2, and suggest that E-BMP-2 might, thus, solve current problems of cost impeding routine clinical use of rhBMP-2.</description><identifier>ISSN: 0914-8779</identifier><identifier>EISSN: 1435-5604</identifier><identifier>DOI: 10.1007/s00774-009-0040-3</identifier><identifier>PMID: 19229473</identifier><language>eng</language><publisher>Japan: Japan : Springer Japan</publisher><subject>Alkaline Phosphatase - biosynthesis ; Animals ; Biochemical Phenomena - drug effects ; Biological and medical sciences ; Bone and Bones - diagnostic imaging ; Bone and Bones - drug effects ; Bone Morphogenetic Protein 2 ; Bone Morphogenetic Proteins - biosynthesis ; Bone Morphogenetic Proteins - pharmacology ; Cell Differentiation - drug effects ; Cells, Cultured ; Diseases of the osteoarticular system ; E coli ; Electrophoresis, Polyacrylamide Gel ; Enzyme Induction - drug effects ; Escherichia coli - metabolism ; Hot Temperature ; Humans ; Medical research ; Medical sciences ; Medicine ; Medicine & Public Health ; Metabolic Diseases ; Mice ; Mice, Inbred ICR ; Original Article ; Orthopedics ; Osteoblasts - cytology ; Osteoblasts - drug effects ; Osteoblasts - enzymology ; Osteogenesis - drug effects ; Protein Multimerization - drug effects ; Protein Stability - drug effects ; Proteins ; Radiography ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - pharmacology ; Smad Proteins - metabolism ; Transforming Growth Factor beta - biosynthesis ; Transforming Growth Factor beta - pharmacology</subject><ispartof>Journal of bone and mineral metabolism, 2009, Vol.27 (3), p.355-363</ispartof><rights>The Japanese Society for Bone and Mineral Research and Springer 2009</rights><rights>2009 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c543t-d339e549d6ee2f56075ca25eaf5afaddf746af302ca56f3e2230e34a818ab5b13</citedby><cites>FETCH-LOGICAL-c543t-d339e549d6ee2f56075ca25eaf5afaddf746af302ca56f3e2230e34a818ab5b13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00774-009-0040-3$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00774-009-0040-3$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21359062$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19229473$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yano, Koichi</creatorcontrib><creatorcontrib>Hoshino, Masatoshi</creatorcontrib><creatorcontrib>Ohta, Yoichi</creatorcontrib><creatorcontrib>Manaka, Tomoya</creatorcontrib><creatorcontrib>Naka, Yoshifumi</creatorcontrib><creatorcontrib>Imai, Yuuki</creatorcontrib><creatorcontrib>Sebald, Walter</creatorcontrib><creatorcontrib>Takaoka, Kunio</creatorcontrib><title>Osteoinductive capacity and heat stability of recombinant human bone morphogenetic protein-2 produced by Escherichia coli and dimerized by biochemical processing</title><title>Journal of bone and mineral metabolism</title><addtitle>J Bone Miner Metab</addtitle><addtitle>J Bone Miner Metab</addtitle><description>One problem associated with clinical application of CHO-derived recombinant human bone morphogenetic protein (C-BMP-2) is its high cost due to the need for use of high doses. To solve this problem, Escherichia coli-derived BMP-2 (E-BMP-2) has been examined using the technique of molecular unfolding and refolding. However, it is unclear whether the characteristics of E-BMP-2 are appropriate for clinical application. In this study, we examined the biological activity of E-BMP-2 and its heat tolerance in in vitro and in vivo systems. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) confirmed the high purity of E-BMP-2. E-BMP-2-induced alkaline phosphatase expression in osteoprogenitor cells (C2C12, ST2, and primary murine calvarial osteoblast cells) was dose-dependent, and consistently elicited ectopic new ossicles of significant size in mice, also in dose-dependent fashion. In addition, E-BMP-2 induced phosphorylation of Smad1/5/8 and mRNA expression of osteoblastic differentiation markers to the same extent as C-BMP-2. On the other hand, when E-BMP-2 was exposed to increasing heat over time, its bone-inducing capacity was maintained until reaching 70°C for 2 h or 90°C for 15 min. Thus, E-BMP-2 will exhibit a decrease in activity with the sterilization procedures required prior to use in surgery. These findings indicate that the biological capacity and heat stability of E-BMP-2 are almost equivalent to those of currently available C-BMP-2, and suggest that E-BMP-2 might, thus, solve current problems of cost impeding routine clinical use of rhBMP-2.</description><subject>Alkaline Phosphatase - biosynthesis</subject><subject>Animals</subject><subject>Biochemical Phenomena - drug effects</subject><subject>Biological and medical sciences</subject><subject>Bone and Bones - diagnostic imaging</subject><subject>Bone and Bones - drug effects</subject><subject>Bone Morphogenetic Protein 2</subject><subject>Bone Morphogenetic Proteins - biosynthesis</subject><subject>Bone Morphogenetic Proteins - pharmacology</subject><subject>Cell Differentiation - drug effects</subject><subject>Cells, Cultured</subject><subject>Diseases of the osteoarticular system</subject><subject>E coli</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Induction - drug effects</subject><subject>Escherichia coli - metabolism</subject><subject>Hot Temperature</subject><subject>Humans</subject><subject>Medical research</subject><subject>Medical sciences</subject><subject>Medicine</subject><subject>Medicine & Public Health</subject><subject>Metabolic Diseases</subject><subject>Mice</subject><subject>Mice, Inbred ICR</subject><subject>Original Article</subject><subject>Orthopedics</subject><subject>Osteoblasts - cytology</subject><subject>Osteoblasts - drug effects</subject><subject>Osteoblasts - enzymology</subject><subject>Osteogenesis - drug effects</subject><subject>Protein Multimerization - drug effects</subject><subject>Protein Stability - drug effects</subject><subject>Proteins</subject><subject>Radiography</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Smad Proteins - metabolism</subject><subject>Transforming Growth Factor beta - biosynthesis</subject><subject>Transforming Growth Factor beta - pharmacology</subject><issn>0914-8779</issn><issn>1435-5604</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9kctu1DAUhi0EokPhAdiAJcQy4GsuS1SVi1SpC-jaOnGOJ64m9mAnlYa34U1xyAhYsfBFx9__H9s_IS85e8cZa97nMjWqYqwrQ7FKPiI7rqSudM3UY7JjHVdV2zTdBXmW8z1jvNENf0oueCdEpxq5Iz9v84zRh2Gxs39AauEI1s8nCmGgI8JM8wy9P6yl6GhCG6feBwgzHZcJAu1jQDrFdBzjHgPO3tJjijP6UIl1V4xxoP2JXmc7YvJ29EBtPPjfHQY_ldqPjeh9LMjkLRxWpcWcfdg_J08cHDK-OK-X5O7j9berz9XN7acvVx9uKquVnKtByg616oYaUbjyAY22IDSC0-BgGFyjanCSCQu6dhKFkAylgpa30Ouey0vyZvMtrb8vmGdzH5cUSkvDOZflt2QrC8U3yqaYc0JnjslPkE6GM7OGYrZQTAnFrKGYVfPq7Lz0Ew5_FecUCvD2DEAuj3cJgvX5Dye41B2rReHExuVyFPaY_rnif7q_3kQOooF9KsZ3XwXjkvGad13dyl85fbFh</recordid><startdate>2009</startdate><enddate>2009</enddate><creator>Yano, Koichi</creator><creator>Hoshino, Masatoshi</creator><creator>Ohta, Yoichi</creator><creator>Manaka, Tomoya</creator><creator>Naka, Yoshifumi</creator><creator>Imai, Yuuki</creator><creator>Sebald, Walter</creator><creator>Takaoka, Kunio</creator><general>Japan : Springer Japan</general><general>Springer Japan</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>IQODW</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>3V.</scope><scope>7QP</scope><scope>7RV</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>K9.</scope><scope>KB0</scope><scope>M0S</scope><scope>M1P</scope><scope>NAPCQ</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope></search><sort><creationdate>2009</creationdate><title>Osteoinductive capacity and heat stability of recombinant human bone morphogenetic protein-2 produced by Escherichia coli and dimerized by biochemical processing</title><author>Yano, Koichi ; Hoshino, Masatoshi ; Ohta, Yoichi ; Manaka, Tomoya ; Naka, Yoshifumi ; Imai, Yuuki ; Sebald, Walter ; Takaoka, Kunio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c543t-d339e549d6ee2f56075ca25eaf5afaddf746af302ca56f3e2230e34a818ab5b13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Alkaline Phosphatase - biosynthesis</topic><topic>Animals</topic><topic>Biochemical Phenomena - drug effects</topic><topic>Biological and medical sciences</topic><topic>Bone and Bones - diagnostic imaging</topic><topic>Bone and Bones - drug effects</topic><topic>Bone Morphogenetic Protein 2</topic><topic>Bone Morphogenetic Proteins - biosynthesis</topic><topic>Bone Morphogenetic Proteins - pharmacology</topic><topic>Cell Differentiation - drug effects</topic><topic>Cells, Cultured</topic><topic>Diseases of the osteoarticular system</topic><topic>E coli</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme Induction - drug effects</topic><topic>Escherichia coli - metabolism</topic><topic>Hot Temperature</topic><topic>Humans</topic><topic>Medical research</topic><topic>Medical sciences</topic><topic>Medicine</topic><topic>Medicine & Public Health</topic><topic>Metabolic Diseases</topic><topic>Mice</topic><topic>Mice, Inbred ICR</topic><topic>Original Article</topic><topic>Orthopedics</topic><topic>Osteoblasts - cytology</topic><topic>Osteoblasts - drug effects</topic><topic>Osteoblasts - enzymology</topic><topic>Osteogenesis - drug effects</topic><topic>Protein Multimerization - drug effects</topic><topic>Protein Stability - drug effects</topic><topic>Proteins</topic><topic>Radiography</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Smad Proteins - metabolism</topic><topic>Transforming Growth Factor beta - biosynthesis</topic><topic>Transforming Growth Factor beta - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yano, Koichi</creatorcontrib><creatorcontrib>Hoshino, Masatoshi</creatorcontrib><creatorcontrib>Ohta, Yoichi</creatorcontrib><creatorcontrib>Manaka, Tomoya</creatorcontrib><creatorcontrib>Naka, Yoshifumi</creatorcontrib><creatorcontrib>Imai, Yuuki</creatorcontrib><creatorcontrib>Sebald, Walter</creatorcontrib><creatorcontrib>Takaoka, Kunio</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><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>Calcium & Calcified Tissue Abstracts</collection><collection>Nursing & Allied Health Database</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>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>ProQuest One Community College</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Nursing & Allied Health Premium</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>Journal of bone and mineral metabolism</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yano, Koichi</au><au>Hoshino, Masatoshi</au><au>Ohta, Yoichi</au><au>Manaka, Tomoya</au><au>Naka, Yoshifumi</au><au>Imai, Yuuki</au><au>Sebald, Walter</au><au>Takaoka, Kunio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Osteoinductive capacity and heat stability of recombinant human bone morphogenetic protein-2 produced by Escherichia coli and dimerized by biochemical processing</atitle><jtitle>Journal of bone and mineral metabolism</jtitle><stitle>J Bone Miner Metab</stitle><addtitle>J Bone Miner Metab</addtitle><date>2009</date><risdate>2009</risdate><volume>27</volume><issue>3</issue><spage>355</spage><epage>363</epage><pages>355-363</pages><issn>0914-8779</issn><eissn>1435-5604</eissn><abstract>One problem associated with clinical application of CHO-derived recombinant human bone morphogenetic protein (C-BMP-2) is its high cost due to the need for use of high doses. To solve this problem, Escherichia coli-derived BMP-2 (E-BMP-2) has been examined using the technique of molecular unfolding and refolding. However, it is unclear whether the characteristics of E-BMP-2 are appropriate for clinical application. In this study, we examined the biological activity of E-BMP-2 and its heat tolerance in in vitro and in vivo systems. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) confirmed the high purity of E-BMP-2. E-BMP-2-induced alkaline phosphatase expression in osteoprogenitor cells (C2C12, ST2, and primary murine calvarial osteoblast cells) was dose-dependent, and consistently elicited ectopic new ossicles of significant size in mice, also in dose-dependent fashion. In addition, E-BMP-2 induced phosphorylation of Smad1/5/8 and mRNA expression of osteoblastic differentiation markers to the same extent as C-BMP-2. On the other hand, when E-BMP-2 was exposed to increasing heat over time, its bone-inducing capacity was maintained until reaching 70°C for 2 h or 90°C for 15 min. Thus, E-BMP-2 will exhibit a decrease in activity with the sterilization procedures required prior to use in surgery. These findings indicate that the biological capacity and heat stability of E-BMP-2 are almost equivalent to those of currently available C-BMP-2, and suggest that E-BMP-2 might, thus, solve current problems of cost impeding routine clinical use of rhBMP-2.</abstract><cop>Japan</cop><pub>Japan : Springer Japan</pub><pmid>19229473</pmid><doi>10.1007/s00774-009-0040-3</doi><tpages>9</tpages></addata></record> |
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| ispartof | Journal of bone and mineral metabolism, 2009, Vol.27 (3), p.355-363 |
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| subjects | Alkaline Phosphatase - biosynthesis Animals Biochemical Phenomena - drug effects Biological and medical sciences Bone and Bones - diagnostic imaging Bone and Bones - drug effects Bone Morphogenetic Protein 2 Bone Morphogenetic Proteins - biosynthesis Bone Morphogenetic Proteins - pharmacology Cell Differentiation - drug effects Cells, Cultured Diseases of the osteoarticular system E coli Electrophoresis, Polyacrylamide Gel Enzyme Induction - drug effects Escherichia coli - metabolism Hot Temperature Humans Medical research Medical sciences Medicine Medicine & Public Health Metabolic Diseases Mice Mice, Inbred ICR Original Article Orthopedics Osteoblasts - cytology Osteoblasts - drug effects Osteoblasts - enzymology Osteogenesis - drug effects Protein Multimerization - drug effects Protein Stability - drug effects Proteins Radiography Recombinant Proteins - biosynthesis Recombinant Proteins - pharmacology Smad Proteins - metabolism Transforming Growth Factor beta - biosynthesis Transforming Growth Factor beta - pharmacology |
| title | Osteoinductive capacity and heat stability of recombinant human bone morphogenetic protein-2 produced by Escherichia coli and dimerized by biochemical processing |
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