Biology:Bone morphogenetic protein 2

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

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]

BMP-2 may be involved in white adipogenesis[4][5] and may have metabolic effects.[4][5]

Interactions

Bone morphogenetic protein 2 has been shown to interact with BMPR1A.[6][7][8][9]

Clinical use and complications

Bone morphogenetic protein 2 is shown to stimulate the production of bone.[10][11] Recombinant human protein (rhBMP-2) is currently available for orthopaedic usage in the United States .[12] Implantation of BMP-2 is performed using a variety of biomaterial carriers ("metals, ceramics, polymers, and composites"[13]) and delivery systems ("hydrogel, microsphere, nanoparticles, and fibers"[13]). While used primarily in orthopedic procedures such as spinal fusion,[14][15] BMP-2 has also found its way into the field of dentistry.[16][17][18]

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.[14] 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.[15]

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.[19][20] 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."[13]

References

  1. ↑ "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. August 1990. doi:10.1016/S0021-9258(19)38285-7. PMID 2376592. 
  2. ↑ "Bone morphogenetic proteins". Growth Factors 22 (4): 233–41. December 2004. doi:10.1080/08977190412331279890. PMID 15621726. 
  3. ↑ "Regulation of human cranial osteoblast phenotype by FGF-2, FGFR-2 and BMP-2 signaling". Histol. Histopathol. 17 (3): 877–85. 2002. doi:10.14670/HH-17.877. PMID 12168799. http://www.hh.um.es/Abstracts/Vol_17/17_3/17_3_877.htm. 
  4. ↑ 4.0 4.1 "Schnurri-2 controls BMP-dependent adipogenesis via interaction with Smad proteins". Developmental Cell 10 (4): 461–71. April 2006. doi:10.1016/j.devcel.2006.02.016. PMID 16580992. 
  5. ↑ 5.0 5.1 "Beyond the bone: Bone morphogenetic protein signaling in adipose tissue". Obesity Reviews 20 (5): 648–658. January 2019. doi:10.1111/obr.12822. PMID 30609449. 
  6. ↑ "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. 2001. PMID 11263668. 
  7. ↑ "Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2". FEBS Lett. 468 (2–3): 215–9. February 2000. doi:10.1016/S0014-5793(00)01214-X. PMID 10692589. 
  8. ↑ "BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II". EMBO J. 19 (13): 3314–24. July 2000. doi:10.1093/emboj/19.13.3314. PMID 10880444. 
  9. ↑ "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. March 2000. doi:10.1091/mbc.11.3.1023. PMID 10712517. 
  10. ↑ "Bone: formation by autoinduction". Science 150 (3698): 893–9. 1965. doi:10.1126/science.150.3698.893. PMID 5319761. Bibcode: 1965Sci...150..893U. 
  11. ↑ "Collagen sponges for bone regeneration with rhBMP-2". Adv. Drug Deliv. Rev. 55 (12): 1613–29. November 2003. doi:10.1016/j.addr.2003.08.010. PMID 14623404. 
  12. ↑ "The use of recombinant human bone morphogenetic protein-2 (rhBMP-2) in orthopaedic applications". Expert Opin Biol Ther 4 (5): 741–8. May 2004. doi:10.1517/14712598.4.5.741. PMID 15155165. 
  13. ↑ 13.0 13.1 13.2 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 (4): 904–925. doi:10.1002/jbm.b.33599. PMID 26728994. 
  14. ↑ 14.0 14.1 "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. May 2009. doi:10.2106/JBJS.G.01485. PMID 19411467. 
  15. ↑ 15.0 15.1 "Bone morphogenetic protein in spinal fusion: overview and clinical update". Neurosurg Focus 10 (4): 1–6. 2001. doi:10.3171/foc.2001.10.4.4. PMID 16732630. 
  16. ↑ "Bone regeneration in rabbit sinus lifting associated with bovine BMP". Journal of Biomedical Materials Research Part B: Applied Biomaterials 68 (2): 127–31. February 2004. doi:10.1002/jbm.b.20006. PMID 14737759. 
  17. ↑ "Expression of bone matrix proteins during the osseus healing of topical conditioned implants: an experimental study". Clinical Oral Implants Research 17 (6): 666–72. December 2006. doi:10.1111/j.1600-0501.2006.01214.x. PMID 17092225. 
  18. ↑ "Effect of immobilized bone morphogenic protein 2 coating of titanium implants on peri-implant bone formation". Clinical Oral Implants Research 16 (5): 563–9. October 2005. doi:10.1111/j.1600-0501.2005.01143.x. PMID 16164462. 
  19. ↑ 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). http://med.stanford.edu/ism/2011/june/carragee-spine-0628.html. 
  20. ↑ "A critical review of recombinant human bone morphogenetic protein-2 trials in spinal surgery: emerging safety concerns and lessons learned". Spine J 11 (6): 471–91. June 2011. doi:10.1016/j.spinee.2011.04.023. PMID 21729796. http://www.spine.org/Documents/TSJJune2011_Carragee_etal_CriticalRev.pdf. 

Further reading

  • "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. 2001. PMID 11263668. 
  • "Bone morphogenetic protein (BMP)-2 induces apoptosis in human myeloma cells". Leuk. Lymphoma 43 (3): 635–9. 2002. doi:10.1080/10428190290012182. PMID 12002771. 
  • "Regulation of human cranial osteoblast phenotype by FGF-2, FGFR-2 and BMP-2 signaling". Histol. Histopathol. 17 (3): 877–85. 2002. doi:10.14670/HH-17.877. PMID 12168799. 

External links



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