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{{Infobox_gene}}
{{PBB_Controls
'''Bone morphogenetic protein 2''' or '''BMP-2''' belongs to the [[Transforming growth factor beta superfamily|TGF-β superfamily]] of [[protein]]s.<ref name="pmid2376592">{{cite journal | vauthors = Sampath TK, Coughlin JE, Whetstone RM, Banach D, Corbett C, Ridge RJ, Ozkaynak E, Oppermann H, Rueger DC | title = Bovine osteogenic protein is composed of dimers of OP-1 and BMP-2A, two members of the transforming growth factor-beta superfamily | journal = J. Biol. Chem. | volume = 265 | issue = 22 | pages = 13198–205  | date = August 1990 | pmid = 2376592 | doi =  | url = http://www.jbc.org/cgi/content/abstract/265/22/13198 }}</ref>
| update_page = yes
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| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = BMP2.png
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 3bmp.
| Name = Bone morphogenetic protein 2
| HGNCid = 1069
| Symbol = BMP2
| AltSymbols =; BMP2A
| OMIM = 112261
| ECnumber = 
| Homologene = 926
| MGIid = 88177
| GeneAtlas_image1 = PBB_GE_BMP2_205289_at_tn.png
| GeneAtlas_image2 = PBB_GE_BMP2_205290_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0001649 |text = osteoblast differentiation}} {{GNF_GO|id=GO:0001658 |text = ureteric bud branching}} {{GNF_GO|id=GO:0001837 |text = epithelial to mesenchymal transition}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0009790 |text = embryonic development}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0030282 |text = bone mineralization}} {{GNF_GO|id=GO:0030509 |text = BMP signaling pathway}} {{GNF_GO|id=GO:0035051 |text = cardiac cell differentiation}} {{GNF_GO|id=GO:0040007 |text = growth}} {{GNF_GO|id=GO:0042475 |text = odontogenesis (sensu Vertebrata)}} {{GNF_GO|id=GO:0045165 |text = cell fate commitment}} {{GNF_GO|id=GO:0045449 |text = regulation of transcription}} {{GNF_GO|id=GO:0045669 |text = positive regulation of osteoblast differentiation}} {{GNF_GO|id=GO:0045778 |text = positive regulation of ossification}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}} {{GNF_GO|id=GO:0048711 |text = positive regulation of astrocyte differentiation}} {{GNF_GO|id=GO:0051216 |text = cartilage development}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 650
    | Hs_Ensembl = ENSG00000125845
    | Hs_RefseqProtein = NP_001191
    | Hs_RefseqmRNA = NM_001200
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 20
    | Hs_GenLoc_start = 6696311
    | Hs_GenLoc_end = 6708927
    | Hs_Uniprot = P12643
    | Mm_EntrezGene = 12156
    | Mm_Ensembl = ENSMUSG00000027358
    | Mm_RefseqmRNA = NM_007553
    | Mm_RefseqProtein = NP_031579
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 133244640
    | Mm_GenLoc_end = 133254326
    | Mm_Uniprot = Q3V1I4
  }}
}}
__NOTOC__
{{SI}}
{{CMG}}
== Overview ==
'''Bone morphogenetic protein 2''' or '''BMP-2''' is a protein that belongs to the [[Transforming growth factor beta|TGF-β]] superfamily of proteins. It, like other [[bone morphogenetic proteins]], plays an important role in the development of bone and cartilage. It is involved in the Hedgehog pathway, TGF-beta signaling pathway, and the Cytokine-cytokine receptor interaction. It is involved also in cardiac cell differentiation and [[epithelial-mesenchymal transition|epithelial to mesenchymal transition]].


BMP-2 and [[BMP7|BMP-7]] are osteogenic BMPs: they have been demonstrated to potently induce [[osteoblast]] [[cellular differentiation|differentiation]] in a variety of cell types.
== Function ==


==Medical Uses==
BMP-2 like other [[bone morphogenetic proteins]],<ref name="pmid15621726">{{cite journal | vauthors = Chen D, Zhao M, Mundy GR | title = Bone morphogenetic proteins | journal = Growth Factors | volume = 22 | issue = 4 | pages = 233–41  | date = December 2004 | pmid = 15621726 | doi = 10.1080/08977190412331279890 }}</ref> plays an important role in the development of bone and cartilage. It is involved in the [[hedgehog signaling pathway|hedgehog pathway]], [[TGF beta signaling pathway]], and in [[cytokine receptor|cytokine]]-cytokine receptor interaction. It is also involved in cardiac cell differentiation and [[epithelial-mesenchymal transition|epithelial to mesenchymal transition]].
Bone morphogenetic protein 2 has been shown to stimulate the production of bone and [[recombinant]] human protein (rhBMP-2) and is currently available for [[orthopaedic]] usage in the [[United States]]. Implantation of BMP-2 in a [[collagen]] sponge induces new bone formation and can be used for the treatment of bony defects, delayed union, and non-union.


==Further reading==
Like many other proteins from the BMP family, BMP-2 has been demonstrated to potently induce [[osteoblast]] [[cellular differentiation|differentiation]] in a variety of cell types.<ref name="pmid12168799">{{cite journal | vauthors = Marie PJ, Debiais F, Haÿ E | title = Regulation of human cranial osteoblast phenotype by FGF-2, FGFR-2 and BMP-2 signaling | journal = Histol. Histopathol. | volume = 17 | issue = 3 | pages = 877–85 | year = 2002 | pmid = 12168799 | doi =  | url = http://www.hh.um.es/Abstracts/Vol_17/17_3/17_3_877.htm }}</ref>
{{reflist|2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Nickel J, Dreyer MK, Kirsch T, Sebald W |title=The crystal structure of the BMP-2:BMPR-IA complex and the generation of BMP-2 antagonists. |journal=The Journal of bone and joint surgery. American volume |volume=83-A Suppl 1 |issue= Pt 1 |pages= S7-14 |year= 2001 |pmid= 11263668 |doi=  }}
*{{cite journal  | author=Kawamura C, Kizaki M, Ikeda Y |title=Bone morphogenetic protein (BMP)-2 induces apoptosis in human myeloma cells. |journal=Leuk. Lymphoma |volume=43 |issue= 3 |pages= 635-9 |year= 2003 |pmid= 12002771 |doi=  }}
*{{cite journal | author=Marie PJ, Debiais F, Haÿ E |title=Regulation of human cranial osteoblast phenotype by FGF-2, FGFR-2 and BMP-2 signaling. |journal=Histol. Histopathol. |volume=17 |issue= 3 |pages= 877-85 |year= 2003 |pmid= 12168799 |doi=  }}
}}
{{refend}}


==External links==
== Interactions ==
* Online Mendelian Inheritance in Man record: {{OMIM|112261}}


{{Template:TGF beta signaling}}
Bone morphogenetic protein 2 has been shown to [[Protein-protein interaction|interact]] with [[BMPR1A]].<ref name=pmid11263668>{{cite journal | vauthors = Nickel J, Dreyer MK, Kirsch T, Sebald W | title = The crystal structure of the BMP-2:BMPR-IA complex and the generation of BMP-2 antagonists | journal = J Bone Joint Surg Am | volume = 83-A Suppl 1 | issue = Pt 1 | pages = S7-14 | year = 2001 | pmid = 11263668 | doi =  }}</ref><ref name=pmid10692589>{{cite journal | vauthors = Kirsch T, Nickel J, Sebald W | title = Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2 | journal = FEBS Lett. | volume = 468 | issue = 2-3 | pages = 215–9  | date = February 2000 | pmid = 10692589 | doi = 10.1016/S0014-5793(00)01214-X }}</ref><ref name=pmid10880444>{{cite journal | vauthors = Kirsch T, Nickel J, Sebald W | title = BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II | journal = EMBO J. | volume = 19 | issue = 13 | pages = 3314–24  | date = July 2000 | pmid = 10880444 | pmc = 313944 | doi = 10.1093/emboj/19.13.3314 }}</ref><ref name=pmid10712517>{{cite journal | vauthors = Gilboa L, Nohe A, Geissendörfer T, Sebald W, Henis YI, Knaus P | title = Bone morphogenetic protein receptor complexes on the surface of live cells: a new oligomerization mode for serine/threonine kinase receptors | journal = Mol. Biol. Cell | volume = 11 | issue = 3 | pages = 1023–35  | date = March 2000 | pmid = 10712517 | pmc = 14828 | doi = 10.1091/mbc.11.3.1023 }}</ref>


[[Category:drug]]
== Clinical use and complications ==
[[Category:Developmental biology]]
{{See also|Bone morphogenetic protein#Clinical uses}}
Bone morphogenetic protein 2 is shown to stimulate the production of bone.<ref name="urist1965">{{cite journal | vauthors = Urist MR | title = Bone: formation by autoinduction | journal = Science | volume = 150 | issue = 3698 | pages = 893–9 | year = 1965 | pmid = 5319761 | doi = 10.1126/science.150.3698.893 | authorlink = Marshall R. Urist }}</ref><ref name="pmid14623404">{{cite journal | vauthors = Geiger M, Li RH, Friess W | title = Collagen sponges for bone regeneration with rhBMP-2 | journal = Adv. Drug Deliv. Rev. | volume = 55 | issue = 12 | pages = 1613–29  | date = November 2003 | pmid = 14623404 | doi = 10.1016/j.addr.2003.08.010 }}</ref> [[Recombinant DNA|Recombinant]] human protein (rhBMP-2) is currently available for [[orthopaedic]] usage in the [[United States]].<ref name="pmid15155165">{{cite journal | vauthors = Khan SN, Lane JM | title = The use of recombinant human bone morphogenetic protein-2 (rhBMP-2) in orthopaedic applications | journal = Expert Opin Biol Ther | volume = 4 | issue = 5 | pages = 741–8  | date = May 2004 | pmid = 15155165 | doi = 10.1517/14712598.4.5.741 }}</ref> Implantation of BMP-2 is performed using a variety of [[biomaterial]] carriers ("metals, ceramics, polymers, and composites"<ref name="AgrawalARev16">{{cite journal |title=A review on carrier systems for bone morphogenetic protein-2 |journal=Journal of Biomedical Materials Research Part B: Applied Biomaterials |author=Agrawal, V |author2=Sinha, M. |volume=Early View |year=2016 |doi=10.1002/jbm.b.33599 |pmid=26728994}}</ref>) and delivery systems ("hydrogel, microsphere, nanoparticles, and fibers"<ref name="AgrawalARev16" />). While used primarily in orthopedic procedures such as spinal fusion,<ref name="pmid19411467">{{cite journal | vauthors = Burkus JK, Gornet MF, Schuler TC, Kleeman TJ, Zdeblick TA | title = Six-year outcomes of anterior lumbar interbody arthrodesis with use of interbody fusion cages and recombinant human bone morphogenetic protein-2 | journal = J Bone Joint Surg Am | volume = 91 | issue = 5 | pages = 1181–9  | date = May 2009 | pmid = 19411467 | doi = 10.2106/JBJS.G.01485 }}</ref><ref name="pmid16732630">{{cite journal | vauthors = Subach BR, Haid RW, Rodts GE, Kaiser MG | title = Bone morphogenetic protein in spinal fusion: overview and clinical update | journal = Neurosurg Focus | volume = 10 | issue = 4 | pages = E3 | year = 2001 | pmid = 16732630 | doi = 10.3171/foc.2001.10.4.4 }}</ref> BMP-2 has also found its way into the field of dentistry.<ref name="pmid14737759">{{cite journal | vauthors = Allegrini S, Yoshimoto M, Salles MB, König B | title = Bone regeneration in rabbit sinus lifting associated with bovine BMP | journal = J. Biomed. Mater. Res. Part B Appl. Biomater. | volume = 68 | issue = 2 | pages = 127–31  | date = February 2004 | pmid = 14737759 | doi = 10.1002/jbm.b.20006 }}</ref><ref name="pmid17092225">{{cite journal | vauthors = Schlegel KA, Thorwarth M, Plesinac A, Wiltfang J, Rupprecht S | title = Expression of bone matrix proteins during the osseus healing of topical conditioned implants: an experimental study | journal = Clin Oral Implants Res | volume = 17 | issue = 6 | pages = 666–72  | date = December 2006 | pmid = 17092225 | doi = 10.1111/j.1600-0501.2006.01214.x }}</ref><ref name="pmid16164462">{{cite journal | vauthors = Schliephake H, Aref A, Scharnweber D, Bierbaum S, Roessler S, Sewing A | title = Effect of immobilized bone morphogenic protein 2 coating of titanium implants on peri-implant bone formation | journal = Clin Oral Implants Res | volume = 16 | issue = 5 | pages = 563–9  | date = October 2005 | pmid = 16164462 | doi = 10.1111/j.1600-0501.2005.01143.x }}</ref>
 
The use of dual tapered threaded fusion cages and recombinant human bone morphogenetic protein-2 on an absorbable collagen sponge obtained and maintained intervertebral spinal fusion, improved clinical outcomes, and reduced pain after anterior lumbar interbody arthrodesis in patients with degenerative lumbar disc disease.<ref name="pmid19411467" /> As an adjuvant to allograft bone or as a replacement for harvested autograft, bone morphogenetic proteins (BMPs) appear to improve fusion rates after spinal arthrodesis in both animal models and humans, while reducing the donor-site morbidity previously associated with such procedures.<ref name="pmid16732630" />
 
A study published in 2011 noted "reports of frequent and occasionally catastrophic complications associated with use of [BMP-2] in spinal fusion surgeries", with a level of risk far in excess of estimates reported in earlier studies.<ref>{{cite news | url = http://med.stanford.edu/ism/2011/june/carragee-spine-0628.html | newspaper = Inside Stanford Medicine | publisher = Stanford School of Medicine | title = Medtronic's spinal fusion product shown to be harmful in bold review by medical journal and its Stanford editors | author = Richter R | date = 2011-06-28 | accessdate = 2012-06-25 | deadurl = yes | archiveurl = https://web.archive.org/web/20120423014645/http://med.stanford.edu/ism/2011/june/carragee-spine-0628.html | archivedate = 2012-04-23 | df =  }}</ref><ref name="pmid21729796">{{cite journal | vauthors = Carragee EJ, Hurwitz EL, Weiner BK | title = A critical review of recombinant human bone morphogenetic protein-2 trials in spinal surgery: emerging safety concerns and lessons learned | journal = Spine J | volume = 11 | issue = 6 | pages = 471–91 | date = June 2011 | pmid = 21729796 | doi = 10.1016/j.spinee.2011.04.023 | url = http://www.spine.org/Documents/TSJJune2011_Carragee_etal_CriticalRev.pdf | deadurl = yes | archiveurl = https://web.archive.org/web/20111110075333/http://www.spine.org/Documents/TSJJune2011_Carragee_etal_CriticalRev.pdf | archivedate = 2011-11-10 | df =  }}</ref> An additional review by Agrawal and Sinha of BMP-2 and its common delivery systems in early 2016 showed how "problems like ectopic growth, lesser protein delivery, [and] inactivation of the protein" reveal a further need "to modify the available carrier systems as well as explore other biomaterials with desired properties."<ref name="AgrawalARev16" />
 
== References ==
{{Reflist|35em}}
 
== Further reading ==
{{Refbegin}}
* {{cite journal | vauthors = Nickel J, Dreyer MK, Kirsch T, Sebald W | title = The crystal structure of the BMP-2:BMPR-IA complex and the generation of BMP-2 antagonists | journal = J Bone Joint Surg Am | volume = 83-A Suppl 1 | issue = Pt 1 | pages = S7-14 | year = 2001 | pmid = 11263668 | doi =  }}
* {{cite journal | vauthors = Kawamura C, Kizaki M, Ikeda Y | title = Bone morphogenetic protein (BMP)-2 induces apoptosis in human myeloma cells | journal = Leuk. Lymphoma | volume = 43 | issue = 3 | pages = 635–9 | year = 2002 | pmid = 12002771 | doi = 10.1080/10428190290012182 }}
* {{cite journal | vauthors = Marie PJ, Debiais F, Haÿ E | title = Regulation of human cranial osteoblast phenotype by FGF-2, FGFR-2 and BMP-2 signaling | journal = Histol. Histopathol. | volume = 17 | issue = 3 | pages = 877–85 | year = 2002 | pmid = 12168799 | doi =  }}
{{Refend}}
 
== External links ==
* {{MeshName|bone+morphogenetic+protein+2|3=bone morphogenetic protein 2}}
* {{UCSC gene info|BMP2}}
 
{{PDB Gallery|geneid=650}}
{{TGF beta signaling}}
{{TGFβ receptor superfamily modulators}}
 
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{{DEFAULTSORT:Bone Morphogenetic Protein 2}}
[[Category:Bone morphogenetic protein]]
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Latest revision as of 07:41, 23 July 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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n/a

UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Bone morphogenetic protein 2 or BMP-2 belongs to the TGF-β superfamily of proteins.[1]

Function

BMP-2 like other bone morphogenetic proteins,[2] plays an important role in the development of bone and cartilage. It is involved in the hedgehog pathway, TGF beta signaling pathway, and in cytokine-cytokine receptor interaction. It is also involved in cardiac cell differentiation and epithelial to mesenchymal transition.

Like many other proteins from the BMP family, BMP-2 has been demonstrated to potently induce osteoblast differentiation in a variety of cell types.[3]

Interactions

Bone morphogenetic protein 2 has been shown to interact with BMPR1A.[4][5][6][7]

Clinical use and complications

See also: Bone morphogenetic protein § Clinical uses

Bone morphogenetic protein 2 is shown to stimulate the production of bone.[8][9] Recombinant human protein (rhBMP-2) is currently available for orthopaedic usage in the United States.[10] Implantation of BMP-2 is performed using a variety of biomaterial carriers ("metals, ceramics, polymers, and composites"[11]) and delivery systems ("hydrogel, microsphere, nanoparticles, and fibers"[11]). While used primarily in orthopedic procedures such as spinal fusion,[12][13] BMP-2 has also found its way into the field of dentistry.[14][15][16]

The use of dual tapered threaded fusion cages and recombinant human bone morphogenetic protein-2 on an absorbable collagen sponge obtained and maintained intervertebral spinal fusion, improved clinical outcomes, and reduced pain after anterior lumbar interbody arthrodesis in patients with degenerative lumbar disc disease.[12] As an adjuvant to allograft bone or as a replacement for harvested autograft, bone morphogenetic proteins (BMPs) appear to improve fusion rates after spinal arthrodesis in both animal models and humans, while reducing the donor-site morbidity previously associated with such procedures.[13]

A study published in 2011 noted "reports of frequent and occasionally catastrophic complications associated with use of [BMP-2] in spinal fusion surgeries", with a level of risk far in excess of estimates reported in earlier studies.[17][18] An additional review by Agrawal and Sinha of BMP-2 and its common delivery systems in early 2016 showed how "problems like ectopic growth, lesser protein delivery, [and] inactivation of the protein" reveal a further need "to modify the available carrier systems as well as explore other biomaterials with desired properties."[11]

References

  1. ↑ Sampath TK, Coughlin JE, Whetstone RM, Banach D, Corbett C, Ridge RJ, Ozkaynak E, Oppermann H, Rueger DC (August 1990). "Bovine osteogenic protein is composed of dimers of OP-1 and BMP-2A, two members of the transforming growth factor-beta superfamily". J. Biol. Chem. 265 (22): 13198–205. PMID 2376592.
  2. ↑ Chen D, Zhao M, Mundy GR (December 2004). "Bone morphogenetic proteins". Growth Factors. 22 (4): 233–41. doi:10.1080/08977190412331279890. PMID 15621726.
  3. ↑ Marie PJ, Debiais F, Haÿ E (2002). "Regulation of human cranial osteoblast phenotype by FGF-2, FGFR-2 and BMP-2 signaling". Histol. Histopathol. 17 (3): 877–85. PMID 12168799.
  4. ↑ Nickel J, Dreyer MK, Kirsch T, Sebald W (2001). "The crystal structure of the BMP-2:BMPR-IA complex and the generation of BMP-2 antagonists". J Bone Joint Surg Am. 83-A Suppl 1 (Pt 1): S7–14. PMID 11263668.
  5. ↑ Kirsch T, Nickel J, Sebald W (February 2000). "Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2". FEBS Lett. 468 (2–3): 215–9. doi:10.1016/S0014-5793(00)01214-X. PMID 10692589.
  6. ↑ Kirsch T, Nickel J, Sebald W (July 2000). "BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II". EMBO J. 19 (13): 3314–24. doi:10.1093/emboj/19.13.3314. PMC 313944. PMID 10880444.
  7. ↑ Gilboa L, Nohe A, Geissendörfer T, Sebald W, Henis YI, Knaus P (March 2000). "Bone morphogenetic protein receptor complexes on the surface of live cells: a new oligomerization mode for serine/threonine kinase receptors". Mol. Biol. Cell. 11 (3): 1023–35. doi:10.1091/mbc.11.3.1023. PMC 14828. PMID 10712517.
  8. ↑ Urist MR (1965). "Bone: formation by autoinduction". Science. 150 (3698): 893–9. doi:10.1126/science.150.3698.893. PMID 5319761.
  9. ↑ Geiger M, Li RH, Friess W (November 2003). "Collagen sponges for bone regeneration with rhBMP-2". Adv. Drug Deliv. Rev. 55 (12): 1613–29. doi:10.1016/j.addr.2003.08.010. PMID 14623404.
  10. ↑ Khan SN, Lane JM (May 2004). "The use of recombinant human bone morphogenetic protein-2 (rhBMP-2) in orthopaedic applications". Expert Opin Biol Ther. 4 (5): 741–8. doi:10.1517/14712598.4.5.741. PMID 15155165.
  11. ↑ 11.0 11.1 11.2 Agrawal, V; Sinha, M. (2016). "A review on carrier systems for bone morphogenetic protein-2". Journal of Biomedical Materials Research Part B: Applied Biomaterials. Early View. doi:10.1002/jbm.b.33599. PMID 26728994.
  12. ↑ 12.0 12.1 Burkus JK, Gornet MF, Schuler TC, Kleeman TJ, Zdeblick TA (May 2009). "Six-year outcomes of anterior lumbar interbody arthrodesis with use of interbody fusion cages and recombinant human bone morphogenetic protein-2". J Bone Joint Surg Am. 91 (5): 1181–9. doi:10.2106/JBJS.G.01485. PMID 19411467.
  13. ↑ 13.0 13.1 Subach BR, Haid RW, Rodts GE, Kaiser MG (2001). "Bone morphogenetic protein in spinal fusion: overview and clinical update". Neurosurg Focus. 10 (4): E3. doi:10.3171/foc.2001.10.4.4. PMID 16732630.
  14. ↑ Allegrini S, Yoshimoto M, Salles MB, König B (February 2004). "Bone regeneration in rabbit sinus lifting associated with bovine BMP". J. Biomed. Mater. Res. Part B Appl. Biomater. 68 (2): 127–31. doi:10.1002/jbm.b.20006. PMID 14737759.
  15. ↑ Schlegel KA, Thorwarth M, Plesinac A, Wiltfang J, Rupprecht S (December 2006). "Expression of bone matrix proteins during the osseus healing of topical conditioned implants: an experimental study". Clin Oral Implants Res. 17 (6): 666–72. doi:10.1111/j.1600-0501.2006.01214.x. PMID 17092225.
  16. ↑ Schliephake H, Aref A, Scharnweber D, Bierbaum S, Roessler S, Sewing A (October 2005). "Effect of immobilized bone morphogenic protein 2 coating of titanium implants on peri-implant bone formation". Clin Oral Implants Res. 16 (5): 563–9. doi:10.1111/j.1600-0501.2005.01143.x. PMID 16164462.
  17. ↑ Richter R (2011-06-28). "Medtronic's spinal fusion product shown to be harmful in bold review by medical journal and its Stanford editors". Inside Stanford Medicine. Stanford School of Medicine. Archived from the original on 2012-04-23. Retrieved 2012-06-25.
  18. ↑ Carragee EJ, Hurwitz EL, Weiner BK (June 2011). "A critical review of recombinant human bone morphogenetic protein-2 trials in spinal surgery: emerging safety concerns and lessons learned" (PDF). Spine J. 11 (6): 471–91. doi:10.1016/j.spinee.2011.04.023. PMID 21729796. Archived from the original (PDF) on 2011-11-10.

Further reading

  • Nickel J, Dreyer MK, Kirsch T, Sebald W (2001). "The crystal structure of the BMP-2:BMPR-IA complex and the generation of BMP-2 antagonists". J Bone Joint Surg Am. 83-A Suppl 1 (Pt 1): S7–14. PMID 11263668.
  • Kawamura C, Kizaki M, Ikeda Y (2002). "Bone morphogenetic protein (BMP)-2 induces apoptosis in human myeloma cells". Leuk. Lymphoma. 43 (3): 635–9. doi:10.1080/10428190290012182. PMID 12002771.
  • Marie PJ, Debiais F, Haÿ E (2002). "Regulation of human cranial osteoblast phenotype by FGF-2, FGFR-2 and BMP-2 signaling". Histol. Histopathol. 17 (3): 877–85. PMID 12168799.

External links

Retrieved from "https://www.wikidoc.org/index.php?title=Bone_morphogenetic_protein_2&oldid=1419752"