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Relaxin Augments BMP‐2–Induced Osteoblast Differentiation and Bone Formation
ABSTRACT Relaxin (Rln), a polypeptide hormone of the insulin superfamily, is an ovarian peptide hormone that is involved in a diverse range of physiological and pathological reactions. In this study, we investigated the effect of Rln on bone morphogenetic protein 2 (BMP‐2)‐induced osteoblast differe...
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| Published in: | Journal of bone and mineral research 2014-07, Vol.29 (7), p.1586-1596 |
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| container_end_page | 1596 |
| container_issue | 7 |
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| container_title | Journal of bone and mineral research |
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| creator | Moon, Jung‐Sun Kim, Sun‐Hun Oh, Sin‐Hye Jeong, Yong‐Wook Kang, Jee‐Hae Park, Jong‐Chun Son, Hye‐Ju Bae, Suk Park, Byung‐Il Kim, Min‐Seok Koh, Jeong‐Tae Ko, Hyun‐Mi |
| description | ABSTRACT
Relaxin (Rln), a polypeptide hormone of the insulin superfamily, is an ovarian peptide hormone that is involved in a diverse range of physiological and pathological reactions. In this study, we investigated the effect of Rln on bone morphogenetic protein 2 (BMP‐2)‐induced osteoblast differentiation and bone formation. Expression of Rln receptors was examined in the primary mouse bone marrow stem cells (BMSCs) and mouse embryonic fibroblast cell line C3H/10T1/2 cells by RT‐PCR and Western blot during BMP‐2–induced osteoblast differentiation. The effect of Rln on osteoblast differentiation and mineralization was evaluated by measuring the alkaline phosphatase activity, osteocalcin production, and Alizarin red S staining. For the in vivo evaluation, BMP‐2 and/or Rln were administered with type I collagen into the back of mice, and after 3 weeks, bone formation was analyzed by micro–computed tomography (µCT). Western blot was performed to determine the effect of Rln on osteoblast differentiation‐related signaling pathway. Expression of Rxfp 1 in BMSCs and C3H/10T1/2 cells was significantly increased by BMP‐2. In vitro, Rln augmented BMP‐2–induced alkaline phosphatase expression, osteocalcin production, and matrix mineralization in BMSCs and C3H/10T1/2 cells. In addition, in vivo administration of Rln enhanced BMP‐2–induced bone formation in a dose‐dependent manner. Interestingly, Rln synergistically increased and sustained BMP‐2–induced Smad, p38, and transforming growth factor‐β activated kinase (TAK) 1 phosphorylation. BMP‐2–induced Runx 2 expression and activity were also significantly augmented by Rln. These results show that Rln enhanced synergistically BMP‐2–induced osteoblast differentiation and bone formation through its receptor, Rxfp 1, by augmenting and sustaining BMP‐2–induced Smad and p38 phosphorylation, which upregulate Runx 2 expression and activity. These results suggest that Rln might be useful for therapeutic application in destructive bone diseases. © 2014 American Society for Bone and Mineral Research. |
| doi_str_mv | 10.1002/jbmr.2197 |
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Relaxin (Rln), a polypeptide hormone of the insulin superfamily, is an ovarian peptide hormone that is involved in a diverse range of physiological and pathological reactions. In this study, we investigated the effect of Rln on bone morphogenetic protein 2 (BMP‐2)‐induced osteoblast differentiation and bone formation. Expression of Rln receptors was examined in the primary mouse bone marrow stem cells (BMSCs) and mouse embryonic fibroblast cell line C3H/10T1/2 cells by RT‐PCR and Western blot during BMP‐2–induced osteoblast differentiation. The effect of Rln on osteoblast differentiation and mineralization was evaluated by measuring the alkaline phosphatase activity, osteocalcin production, and Alizarin red S staining. For the in vivo evaluation, BMP‐2 and/or Rln were administered with type I collagen into the back of mice, and after 3 weeks, bone formation was analyzed by micro–computed tomography (µCT). Western blot was performed to determine the effect of Rln on osteoblast differentiation‐related signaling pathway. Expression of Rxfp 1 in BMSCs and C3H/10T1/2 cells was significantly increased by BMP‐2. In vitro, Rln augmented BMP‐2–induced alkaline phosphatase expression, osteocalcin production, and matrix mineralization in BMSCs and C3H/10T1/2 cells. In addition, in vivo administration of Rln enhanced BMP‐2–induced bone formation in a dose‐dependent manner. Interestingly, Rln synergistically increased and sustained BMP‐2–induced Smad, p38, and transforming growth factor‐β activated kinase (TAK) 1 phosphorylation. BMP‐2–induced Runx 2 expression and activity were also significantly augmented by Rln. These results show that Rln enhanced synergistically BMP‐2–induced osteoblast differentiation and bone formation through its receptor, Rxfp 1, by augmenting and sustaining BMP‐2–induced Smad and p38 phosphorylation, which upregulate Runx 2 expression and activity. These results suggest that Rln might be useful for therapeutic application in destructive bone diseases. © 2014 American Society for Bone and Mineral Research.</description><identifier>ISSN: 0884-0431</identifier><identifier>EISSN: 1523-4681</identifier><identifier>DOI: 10.1002/jbmr.2197</identifier><identifier>PMID: 24643989</identifier><identifier>CODEN: JBMREJ</identifier><language>eng</language><publisher>United States: Wiley Subscription Services, Inc</publisher><subject>Animals ; BMP ; BONE ; Bone Morphogenetic Protein 2 - pharmacology ; Calcification, Physiologic - drug effects ; Cell Differentiation - drug effects ; Cell Line ; Core Binding Factor Alpha 1 Subunit - metabolism ; Humans ; MAP Kinase Kinase Kinases - metabolism ; Mice, Inbred C57BL ; Osteoblasts - cytology ; Osteoblasts - drug effects ; Osteoblasts - enzymology ; Osteogenesis - drug effects ; p38 Mitogen-Activated Protein Kinases - metabolism ; Phosphorylation - drug effects ; Protein Binding - drug effects ; Receptors, G-Protein-Coupled - metabolism ; RELAXIN ; Relaxin - pharmacology ; RXFP ; Smad Proteins - metabolism</subject><ispartof>Journal of bone and mineral research, 2014-07, Vol.29 (7), p.1586-1596</ispartof><rights>2014 American Society for Bone and Mineral Research</rights><rights>2014 American Society for Bone and Mineral Research.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3537-ecf7a52a7f20797faf59d0bc8fd8ea8da73347d1cb4905c9f8e104ea4c303a0e0</citedby><cites>FETCH-LOGICAL-c3537-ecf7a52a7f20797faf59d0bc8fd8ea8da73347d1cb4905c9f8e104ea4c303a0e0</cites></display><links><openurl>$$Topenurl_article</openurl><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>783</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24643989$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Moon, Jung‐Sun</creatorcontrib><creatorcontrib>Kim, Sun‐Hun</creatorcontrib><creatorcontrib>Oh, Sin‐Hye</creatorcontrib><creatorcontrib>Jeong, Yong‐Wook</creatorcontrib><creatorcontrib>Kang, Jee‐Hae</creatorcontrib><creatorcontrib>Park, Jong‐Chun</creatorcontrib><creatorcontrib>Son, Hye‐Ju</creatorcontrib><creatorcontrib>Bae, Suk</creatorcontrib><creatorcontrib>Park, Byung‐Il</creatorcontrib><creatorcontrib>Kim, Min‐Seok</creatorcontrib><creatorcontrib>Koh, Jeong‐Tae</creatorcontrib><creatorcontrib>Ko, Hyun‐Mi</creatorcontrib><title>Relaxin Augments BMP‐2–Induced Osteoblast Differentiation and Bone Formation</title><title>Journal of bone and mineral research</title><addtitle>J Bone Miner Res</addtitle><description>ABSTRACT
Relaxin (Rln), a polypeptide hormone of the insulin superfamily, is an ovarian peptide hormone that is involved in a diverse range of physiological and pathological reactions. In this study, we investigated the effect of Rln on bone morphogenetic protein 2 (BMP‐2)‐induced osteoblast differentiation and bone formation. Expression of Rln receptors was examined in the primary mouse bone marrow stem cells (BMSCs) and mouse embryonic fibroblast cell line C3H/10T1/2 cells by RT‐PCR and Western blot during BMP‐2–induced osteoblast differentiation. The effect of Rln on osteoblast differentiation and mineralization was evaluated by measuring the alkaline phosphatase activity, osteocalcin production, and Alizarin red S staining. For the in vivo evaluation, BMP‐2 and/or Rln were administered with type I collagen into the back of mice, and after 3 weeks, bone formation was analyzed by micro–computed tomography (µCT). Western blot was performed to determine the effect of Rln on osteoblast differentiation‐related signaling pathway. Expression of Rxfp 1 in BMSCs and C3H/10T1/2 cells was significantly increased by BMP‐2. In vitro, Rln augmented BMP‐2–induced alkaline phosphatase expression, osteocalcin production, and matrix mineralization in BMSCs and C3H/10T1/2 cells. In addition, in vivo administration of Rln enhanced BMP‐2–induced bone formation in a dose‐dependent manner. Interestingly, Rln synergistically increased and sustained BMP‐2–induced Smad, p38, and transforming growth factor‐β activated kinase (TAK) 1 phosphorylation. BMP‐2–induced Runx 2 expression and activity were also significantly augmented by Rln. These results show that Rln enhanced synergistically BMP‐2–induced osteoblast differentiation and bone formation through its receptor, Rxfp 1, by augmenting and sustaining BMP‐2–induced Smad and p38 phosphorylation, which upregulate Runx 2 expression and activity. These results suggest that Rln might be useful for therapeutic application in destructive bone diseases. © 2014 American Society for Bone and Mineral Research.</description><subject>Animals</subject><subject>BMP</subject><subject>BONE</subject><subject>Bone Morphogenetic Protein 2 - pharmacology</subject><subject>Calcification, Physiologic - drug effects</subject><subject>Cell Differentiation - drug effects</subject><subject>Cell Line</subject><subject>Core Binding Factor Alpha 1 Subunit - metabolism</subject><subject>Humans</subject><subject>MAP Kinase Kinase Kinases - metabolism</subject><subject>Mice, Inbred C57BL</subject><subject>Osteoblasts - cytology</subject><subject>Osteoblasts - drug effects</subject><subject>Osteoblasts - enzymology</subject><subject>Osteogenesis - drug effects</subject><subject>p38 Mitogen-Activated Protein Kinases - metabolism</subject><subject>Phosphorylation - drug effects</subject><subject>Protein Binding - drug effects</subject><subject>Receptors, G-Protein-Coupled - metabolism</subject><subject>RELAXIN</subject><subject>Relaxin - pharmacology</subject><subject>RXFP</subject><subject>Smad Proteins - metabolism</subject><issn>0884-0431</issn><issn>1523-4681</issn><fulltext>false</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><recordid>eNp10E9LwzAYx_Egis4_B9-AFLzooduTJm3S4zadThRF9FzS9Il09I8mLbrbXoLgO9wrsXPqQfAUCB--PPwIOaTQpwDBYJaWth_QWGyQHg0D5vNI0k3SAym5D5zRHbLr3AwAojCKtslOwCPOYhn3yN09Fuotr7xh-1Ri1ThvdHO3XLwHy8XHtMpajZl36xqs00K5xjvLjUHbuVw1eV15qsq8UV2hN6lt-fW1T7aMKhwefL975HFy_jC-9K9vL6bj4bWvWciEj9oIFQZKmABELIwyYZxBqqXJJCqZKcEYFxnVKY8h1LGRSIGj4poBU4CwR07W3Wdbv7TomqTMncaiUBXWrUtoyCkTIKOgo8d_6KxubdVd16mQUd4Z0anTtdK2ds6iSZ5tXio7Tygkq5mT1czJaubOHn0X27TE7Ff-7NqBwRq85gXO_y8lV6Ob-6_kJ9QbiJc</recordid><startdate>201407</startdate><enddate>201407</enddate><creator>Moon, Jung‐Sun</creator><creator>Kim, Sun‐Hun</creator><creator>Oh, Sin‐Hye</creator><creator>Jeong, Yong‐Wook</creator><creator>Kang, Jee‐Hae</creator><creator>Park, Jong‐Chun</creator><creator>Son, Hye‐Ju</creator><creator>Bae, Suk</creator><creator>Park, Byung‐Il</creator><creator>Kim, Min‐Seok</creator><creator>Koh, Jeong‐Tae</creator><creator>Ko, Hyun‐Mi</creator><general>Wiley Subscription Services, 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>7TS</scope><scope>K9.</scope><scope>7X8</scope></search><sort><creationdate>201407</creationdate><title>Relaxin Augments BMP‐2–Induced Osteoblast Differentiation and Bone Formation</title><author>Moon, Jung‐Sun ; Kim, Sun‐Hun ; Oh, Sin‐Hye ; Jeong, Yong‐Wook ; Kang, Jee‐Hae ; Park, Jong‐Chun ; Son, Hye‐Ju ; Bae, Suk ; Park, Byung‐Il ; Kim, Min‐Seok ; Koh, Jeong‐Tae ; Ko, Hyun‐Mi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3537-ecf7a52a7f20797faf59d0bc8fd8ea8da73347d1cb4905c9f8e104ea4c303a0e0</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Animals</topic><topic>BMP</topic><topic>BONE</topic><topic>Bone Morphogenetic Protein 2 - pharmacology</topic><topic>Calcification, Physiologic - drug effects</topic><topic>Cell Differentiation - drug effects</topic><topic>Cell Line</topic><topic>Core Binding Factor Alpha 1 Subunit - metabolism</topic><topic>Humans</topic><topic>MAP Kinase Kinase Kinases - metabolism</topic><topic>Mice, Inbred C57BL</topic><topic>Osteoblasts - cytology</topic><topic>Osteoblasts - drug effects</topic><topic>Osteoblasts - enzymology</topic><topic>Osteogenesis - drug effects</topic><topic>p38 Mitogen-Activated Protein Kinases - metabolism</topic><topic>Phosphorylation - drug effects</topic><topic>Protein Binding - drug effects</topic><topic>Receptors, G-Protein-Coupled - metabolism</topic><topic>RELAXIN</topic><topic>Relaxin - pharmacology</topic><topic>RXFP</topic><topic>Smad Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><creatorcontrib>Moon, Jung‐Sun</creatorcontrib><creatorcontrib>Kim, Sun‐Hun</creatorcontrib><creatorcontrib>Oh, Sin‐Hye</creatorcontrib><creatorcontrib>Jeong, Yong‐Wook</creatorcontrib><creatorcontrib>Kang, Jee‐Hae</creatorcontrib><creatorcontrib>Park, Jong‐Chun</creatorcontrib><creatorcontrib>Son, Hye‐Ju</creatorcontrib><creatorcontrib>Bae, Suk</creatorcontrib><creatorcontrib>Park, Byung‐Il</creatorcontrib><creatorcontrib>Kim, Min‐Seok</creatorcontrib><creatorcontrib>Koh, Jeong‐Tae</creatorcontrib><creatorcontrib>Ko, Hyun‐Mi</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>Physical Education Index</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of bone and mineral research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>no_fulltext</fulltext></delivery><addata><au>Moon, Jung‐Sun</au><au>Kim, Sun‐Hun</au><au>Oh, Sin‐Hye</au><au>Jeong, Yong‐Wook</au><au>Kang, Jee‐Hae</au><au>Park, Jong‐Chun</au><au>Son, Hye‐Ju</au><au>Bae, Suk</au><au>Park, Byung‐Il</au><au>Kim, Min‐Seok</au><au>Koh, Jeong‐Tae</au><au>Ko, Hyun‐Mi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Relaxin Augments BMP‐2–Induced Osteoblast Differentiation and Bone Formation</atitle><jtitle>Journal of bone and mineral research</jtitle><addtitle>J Bone Miner Res</addtitle><date>2014-07</date><risdate>2014</risdate><volume>29</volume><issue>7</issue><spage>1586</spage><epage>1596</epage><pages>1586-1596</pages><issn>0884-0431</issn><eissn>1523-4681</eissn><coden>JBMREJ</coden><abstract>ABSTRACT
Relaxin (Rln), a polypeptide hormone of the insulin superfamily, is an ovarian peptide hormone that is involved in a diverse range of physiological and pathological reactions. In this study, we investigated the effect of Rln on bone morphogenetic protein 2 (BMP‐2)‐induced osteoblast differentiation and bone formation. Expression of Rln receptors was examined in the primary mouse bone marrow stem cells (BMSCs) and mouse embryonic fibroblast cell line C3H/10T1/2 cells by RT‐PCR and Western blot during BMP‐2–induced osteoblast differentiation. The effect of Rln on osteoblast differentiation and mineralization was evaluated by measuring the alkaline phosphatase activity, osteocalcin production, and Alizarin red S staining. For the in vivo evaluation, BMP‐2 and/or Rln were administered with type I collagen into the back of mice, and after 3 weeks, bone formation was analyzed by micro–computed tomography (µCT). Western blot was performed to determine the effect of Rln on osteoblast differentiation‐related signaling pathway. Expression of Rxfp 1 in BMSCs and C3H/10T1/2 cells was significantly increased by BMP‐2. In vitro, Rln augmented BMP‐2–induced alkaline phosphatase expression, osteocalcin production, and matrix mineralization in BMSCs and C3H/10T1/2 cells. In addition, in vivo administration of Rln enhanced BMP‐2–induced bone formation in a dose‐dependent manner. Interestingly, Rln synergistically increased and sustained BMP‐2–induced Smad, p38, and transforming growth factor‐β activated kinase (TAK) 1 phosphorylation. BMP‐2–induced Runx 2 expression and activity were also significantly augmented by Rln. These results show that Rln enhanced synergistically BMP‐2–induced osteoblast differentiation and bone formation through its receptor, Rxfp 1, by augmenting and sustaining BMP‐2–induced Smad and p38 phosphorylation, which upregulate Runx 2 expression and activity. These results suggest that Rln might be useful for therapeutic application in destructive bone diseases. © 2014 American Society for Bone and Mineral Research.</abstract><cop>United States</cop><pub>Wiley Subscription Services, Inc</pub><pmid>24643989</pmid><doi>10.1002/jbmr.2197</doi><tpages>11</tpages></addata></record> |
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| ispartof | Journal of bone and mineral research, 2014-07, Vol.29 (7), p.1586-1596 |
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| subjects | Animals BMP BONE Bone Morphogenetic Protein 2 - pharmacology Calcification, Physiologic - drug effects Cell Differentiation - drug effects Cell Line Core Binding Factor Alpha 1 Subunit - metabolism Humans MAP Kinase Kinase Kinases - metabolism Mice, Inbred C57BL Osteoblasts - cytology Osteoblasts - drug effects Osteoblasts - enzymology Osteogenesis - drug effects p38 Mitogen-Activated Protein Kinases - metabolism Phosphorylation - drug effects Protein Binding - drug effects Receptors, G-Protein-Coupled - metabolism RELAXIN Relaxin - pharmacology RXFP Smad Proteins - metabolism |
| title | Relaxin Augments BMP‐2–Induced Osteoblast Differentiation and Bone Formation |
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