Variability of BMP-2 content in DBM products derived from different long bone
Demineralized bone matrix (DBM) has been regarded as an ideal bone substitute as a native carrier of bone morphogenetic proteins (BMPs) and other growth factors. However, the osteoinductive properties diverse in different DBM products. We speculate that the harvest origin further contributing to var...
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| Veröffentlicht in: | Cell and tissue banking 2024-06, Vol.25 (2), p.697-703 |
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| creator | Zhao, Yong-jie Yin, Gang Liu, Bin Deng, Xiao-qiang Cao, Hai-yan Liu, Ying |
| description | Demineralized bone matrix (DBM) has been regarded as an ideal bone substitute as a native carrier of bone morphogenetic proteins (BMPs) and other growth factors. However, the osteoinductive properties diverse in different DBM products. We speculate that the harvest origin further contributing to variability of BMPs contents in DBM products besides the process technology. In the study, the cortical bone of femur, tibia, humerus, and ulna from a signal donor were prepared and followed demineralizd into DBM products. Proteins in bone martix were extracted using guanidine-HCl and collagenase, respectively, and BMP-2 content was detected by sandwich enzyme-linked immunosorbent assay (ELISA). Variability of BMP-2 content was found in 4 different DBM products. By guanidine-HCl extraction, the average concentration in DBMs harvested from ulna, humerus, tibia, and femur were 0.613 ± 0.053, 0.848 ± 0.051, 3.293 ± 0.268, and 21.763 ± 0.344, respectively (
p
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| doi_str_mv | 10.1007/s10561-024-10132-5 |
| format | Article |
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p
< 0.05), while using collagenase, the levels were 0.089 ± 0.004, 0.097 ± 0.004, 0.330 ± 0.012, and 1.562 ± 0.008, respectively (
p
< 0.05). In general, the content of BMP-2 in long bones of Lower limb was higher than that in long bones of upper limb, and GuHCl had remarkably superior extracted efficiency for BMP-2 compared to collagenase. The results suggest that the origin of cortical bones harvested to fabricate DBM products contribute to the variability of native BMP-2 content, while the protein extracted method only changes the measured values of BMP-2.</description><identifier>ISSN: 1389-9333</identifier><identifier>ISSN: 1573-6814</identifier><identifier>EISSN: 1573-6814</identifier><identifier>DOI: 10.1007/s10561-024-10132-5</identifier><identifier>PMID: 38489016</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Biomedical and Life Sciences ; Biomedicine ; Bone and Bones - chemistry ; Bone biomaterials ; Bone Demineralization Technique ; Bone matrix ; Bone Matrix - chemistry ; Bone morphogenetic protein 2 ; Bone Morphogenetic Protein 2 - analysis ; Bone Morphogenetic Protein 2 - metabolism ; Bone morphogenetic proteins ; Bones ; Cell Biology ; Collagen ; Collagenase ; Cortical bone ; Enzyme-linked immunosorbent assay ; Femur ; Full Length Paper ; Growth factors ; Guanidine ; Humans ; Humerus ; Life Sciences ; Long bone ; Osteogenesis ; Tibia ; Transplant Surgery ; Ulna</subject><ispartof>Cell and tissue banking, 2024-06, Vol.25 (2), p.697-703</ispartof><rights>The Author(s), under exclusive licence to Springer Nature B.V. 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2024. The Author(s), under exclusive licence to Springer Nature B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c326t-2c5f838017e32271b7ac9417ec70290c3c83062a4f7f2f049d6496724ffdeb7c3</cites><orcidid>0000-0002-7164-9515 ; 0000-0002-0280-3662 ; 0000-0002-8319-5776</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10561-024-10132-5$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10561-024-10132-5$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38489016$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhao, Yong-jie</creatorcontrib><creatorcontrib>Yin, Gang</creatorcontrib><creatorcontrib>Liu, Bin</creatorcontrib><creatorcontrib>Deng, Xiao-qiang</creatorcontrib><creatorcontrib>Cao, Hai-yan</creatorcontrib><creatorcontrib>Liu, Ying</creatorcontrib><title>Variability of BMP-2 content in DBM products derived from different long bone</title><title>Cell and tissue banking</title><addtitle>Cell Tissue Bank</addtitle><addtitle>Cell Tissue Bank</addtitle><description>Demineralized bone matrix (DBM) has been regarded as an ideal bone substitute as a native carrier of bone morphogenetic proteins (BMPs) and other growth factors. However, the osteoinductive properties diverse in different DBM products. We speculate that the harvest origin further contributing to variability of BMPs contents in DBM products besides the process technology. In the study, the cortical bone of femur, tibia, humerus, and ulna from a signal donor were prepared and followed demineralizd into DBM products. Proteins in bone martix were extracted using guanidine-HCl and collagenase, respectively, and BMP-2 content was detected by sandwich enzyme-linked immunosorbent assay (ELISA). Variability of BMP-2 content was found in 4 different DBM products. By guanidine-HCl extraction, the average concentration in DBMs harvested from ulna, humerus, tibia, and femur were 0.613 ± 0.053, 0.848 ± 0.051, 3.293 ± 0.268, and 21.763 ± 0.344, respectively (
p
< 0.05), while using collagenase, the levels were 0.089 ± 0.004, 0.097 ± 0.004, 0.330 ± 0.012, and 1.562 ± 0.008, respectively (
p
< 0.05). In general, the content of BMP-2 in long bones of Lower limb was higher than that in long bones of upper limb, and GuHCl had remarkably superior extracted efficiency for BMP-2 compared to collagenase. The results suggest that the origin of cortical bones harvested to fabricate DBM products contribute to the variability of native BMP-2 content, while the protein extracted method only changes the measured values of BMP-2.</description><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bone and Bones - chemistry</subject><subject>Bone biomaterials</subject><subject>Bone Demineralization Technique</subject><subject>Bone matrix</subject><subject>Bone Matrix - chemistry</subject><subject>Bone morphogenetic protein 2</subject><subject>Bone Morphogenetic Protein 2 - analysis</subject><subject>Bone Morphogenetic Protein 2 - metabolism</subject><subject>Bone morphogenetic proteins</subject><subject>Bones</subject><subject>Cell Biology</subject><subject>Collagen</subject><subject>Collagenase</subject><subject>Cortical bone</subject><subject>Enzyme-linked immunosorbent assay</subject><subject>Femur</subject><subject>Full Length Paper</subject><subject>Growth factors</subject><subject>Guanidine</subject><subject>Humans</subject><subject>Humerus</subject><subject>Life Sciences</subject><subject>Long bone</subject><subject>Osteogenesis</subject><subject>Tibia</subject><subject>Transplant Surgery</subject><subject>Ulna</subject><issn>1389-9333</issn><issn>1573-6814</issn><issn>1573-6814</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kD1PwzAQhi0E4qPwBxiQJRYWw9lOYnuk5VNqBQOwWoljV0FpDHaC1H-PSwtIDEw-65577_QgdEzhnAKIi0ghLygBlhEKlDOSb6F9mgtOCkmz7VRzqYjinO-hgxhfARgIxnfRHpeZVECLfTR7KUNTVk3b9EvsHR7PHgnDxne97XrcdPhqPMNvwdeD6SOubWg-bI1d8AtcN87ZsMJa381x5Tt7iHZc2UZ7tHlH6Pnm-mlyR6YPt_eTyykxnBU9YSZ3kkugwnLGBK1EaVSWfkYAU2C4kRwKVmZOOOYgU3WRqUKwzLnaVsLwETpb56bL3gcbe71oorFtW3bWD1EzlUumZCHzhJ7-QV_9ELp0nV7tEBJyBYlia8oEH2OwTr-FZlGGpaagV7L1WrZOsvWXbL2KPtlED9XC1j8j33YTwNdATK1ubsPv7n9iPwG33IdL</recordid><startdate>20240601</startdate><enddate>20240601</enddate><creator>Zhao, Yong-jie</creator><creator>Yin, Gang</creator><creator>Liu, Bin</creator><creator>Deng, Xiao-qiang</creator><creator>Cao, Hai-yan</creator><creator>Liu, Ying</creator><general>Springer Netherlands</general><general>Springer Nature B.V</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>7U9</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>NAPCQ</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-7164-9515</orcidid><orcidid>https://orcid.org/0000-0002-0280-3662</orcidid><orcidid>https://orcid.org/0000-0002-8319-5776</orcidid></search><sort><creationdate>20240601</creationdate><title>Variability of BMP-2 content in DBM products derived from different long bone</title><author>Zhao, Yong-jie ; Yin, Gang ; Liu, Bin ; Deng, Xiao-qiang ; Cao, Hai-yan ; Liu, Ying</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c326t-2c5f838017e32271b7ac9417ec70290c3c83062a4f7f2f049d6496724ffdeb7c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Bone and Bones - chemistry</topic><topic>Bone biomaterials</topic><topic>Bone Demineralization Technique</topic><topic>Bone matrix</topic><topic>Bone Matrix - chemistry</topic><topic>Bone morphogenetic protein 2</topic><topic>Bone Morphogenetic Protein 2 - analysis</topic><topic>Bone Morphogenetic Protein 2 - metabolism</topic><topic>Bone morphogenetic proteins</topic><topic>Bones</topic><topic>Cell Biology</topic><topic>Collagen</topic><topic>Collagenase</topic><topic>Cortical bone</topic><topic>Enzyme-linked immunosorbent assay</topic><topic>Femur</topic><topic>Full Length Paper</topic><topic>Growth factors</topic><topic>Guanidine</topic><topic>Humans</topic><topic>Humerus</topic><topic>Life Sciences</topic><topic>Long bone</topic><topic>Osteogenesis</topic><topic>Tibia</topic><topic>Transplant Surgery</topic><topic>Ulna</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhao, Yong-jie</creatorcontrib><creatorcontrib>Yin, Gang</creatorcontrib><creatorcontrib>Liu, Bin</creatorcontrib><creatorcontrib>Deng, Xiao-qiang</creatorcontrib><creatorcontrib>Cao, Hai-yan</creatorcontrib><creatorcontrib>Liu, Ying</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Nursing & Allied Health Premium</collection><collection>MEDLINE - Academic</collection><jtitle>Cell and tissue banking</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhao, Yong-jie</au><au>Yin, Gang</au><au>Liu, Bin</au><au>Deng, Xiao-qiang</au><au>Cao, Hai-yan</au><au>Liu, Ying</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Variability of BMP-2 content in DBM products derived from different long bone</atitle><jtitle>Cell and tissue banking</jtitle><stitle>Cell Tissue Bank</stitle><addtitle>Cell Tissue Bank</addtitle><date>2024-06-01</date><risdate>2024</risdate><volume>25</volume><issue>2</issue><spage>697</spage><epage>703</epage><pages>697-703</pages><issn>1389-9333</issn><issn>1573-6814</issn><eissn>1573-6814</eissn><abstract>Demineralized bone matrix (DBM) has been regarded as an ideal bone substitute as a native carrier of bone morphogenetic proteins (BMPs) and other growth factors. However, the osteoinductive properties diverse in different DBM products. We speculate that the harvest origin further contributing to variability of BMPs contents in DBM products besides the process technology. In the study, the cortical bone of femur, tibia, humerus, and ulna from a signal donor were prepared and followed demineralizd into DBM products. Proteins in bone martix were extracted using guanidine-HCl and collagenase, respectively, and BMP-2 content was detected by sandwich enzyme-linked immunosorbent assay (ELISA). Variability of BMP-2 content was found in 4 different DBM products. By guanidine-HCl extraction, the average concentration in DBMs harvested from ulna, humerus, tibia, and femur were 0.613 ± 0.053, 0.848 ± 0.051, 3.293 ± 0.268, and 21.763 ± 0.344, respectively (
p
< 0.05), while using collagenase, the levels were 0.089 ± 0.004, 0.097 ± 0.004, 0.330 ± 0.012, and 1.562 ± 0.008, respectively (
p
< 0.05). In general, the content of BMP-2 in long bones of Lower limb was higher than that in long bones of upper limb, and GuHCl had remarkably superior extracted efficiency for BMP-2 compared to collagenase. The results suggest that the origin of cortical bones harvested to fabricate DBM products contribute to the variability of native BMP-2 content, while the protein extracted method only changes the measured values of BMP-2.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>38489016</pmid><doi>10.1007/s10561-024-10132-5</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0002-7164-9515</orcidid><orcidid>https://orcid.org/0000-0002-0280-3662</orcidid><orcidid>https://orcid.org/0000-0002-8319-5776</orcidid></addata></record> |
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| subjects | Biomedical and Life Sciences Biomedicine Bone and Bones - chemistry Bone biomaterials Bone Demineralization Technique Bone matrix Bone Matrix - chemistry Bone morphogenetic protein 2 Bone Morphogenetic Protein 2 - analysis Bone Morphogenetic Protein 2 - metabolism Bone morphogenetic proteins Bones Cell Biology Collagen Collagenase Cortical bone Enzyme-linked immunosorbent assay Femur Full Length Paper Growth factors Guanidine Humans Humerus Life Sciences Long bone Osteogenesis Tibia Transplant Surgery Ulna |
| title | Variability of BMP-2 content in DBM products derived from different long bone |
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