Bone morphogenetic protein

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Bone morphogenetic proteins, particularly bone morphogenetic protein 2 and bone morphogenetic protein 7 have become key to tissue engineering requiring new bone formation as with non union of fractures.

Bone morphogenetic protein(BMP) activity was first characterised in 1965[1] and is now known to be due to a group of proteins of the transforming growth factor beta family that regulate transcription and act as growth factors. They have roles in embryonic heart, neural and cartilage development and many cellular functions as well as bone formation. SMAD (Smad, mothers against decapentaplegic) transcription factors are the immediate downstream molecules of BMP receptors. Bone induction by BMP-3 (osteogenin) was described in other mammals in 1989[2]. There are now around 20 BMP family members. Their receptors are serine/threonine kinases, with type I and II subtypes. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate the SMAD transcriptional regulators. After release from the receptor, the phosphorylated SMAD proteins associate with a related SMAD protein in a complex that translocates into the nucleus and participates in gene transcription with other transcription factors. They have multiple actual and potential therapeutic applications.