The Bone Morphogenetic Proteins (BMPs) were first discovered and named by Marshall Urist in 1965 as a mix of proteins that appeared to be responsible for bone regeneration. In the decades since, these cytokines have become one of the most important families of growth factors for therapeutic and medicinal purposes!
There are 20 growth factors that have been named as BMPs, and many are also members of the TGF-β superfamily of proteins, but not all are technically considered “bone morphogenetic proteins” or even directly affect bones. For instance, BMP1 is a misidentified protein with chordinase and procollagen proteinase activities (Kessler, 1996). Several others have no bone related roles at all, such as BMP8 (involved in reproductive cells), BMP10 (involved in cardiac development) and BMP15 (involved in ovarian physiology) (Bessa, 2008). Also, BMP12, 13 and 14 are actually involved in cartilage development, rather than bone development (Bessa, 2008). Typically, only BMP2-11 are actually considered to be true BMPs.
However, even the true BMPs play a wider role in the body than simply bone development. BMP2 has been shown to play a part in heart morphogenesis and in neural stem cells (White, 2001). BMP2 is also involved in the Hedgehog Signaling Pathway and the TGF-β signaling pathway. BMP4 is critical in the development of tooth and limbs and in fracture repair, specifically in endochondral bone formation in humans. It has also been shown to be an important factor in muscle development (Christ, 2002) and ureteric bud development (Michos, 2007). BMP7 is directly responsible for the induction of a wide range of osteogenic genes. It has also been used therapeutically as a treatment for kidney disease and may also be able to treat some forms of infertility. BMP4 and 7 are also directly affected by the Noggin growth factors.
BMPs are typically homo or heterodimers linked via disulphide bridges. The BMP2/4 group, BMP7 and some others (BMP9/10 and BMP 12-14) also have over 50% amino acid homology (Bessa, 2008). BMPs form a conserved motif of seven cysteines, which is involved in the formation of six intrachain disulphide bonds and a single interchain bond, necessary to dimer formation (Bessa, 2008). BMPs bind to serine-threonine kinase receptors on the surface of the cell, but only STKI and STKII appear to play significant roles in BMP binding or signaling.
At Goldbio, we have recombinant BMP2, BMP4 and BMP7 available for research, although currently, only BMP2 is a biologically active protein. Our BMP4 and BMP7, while inactive proteins, are still useful in the lab as a means to effectively stimulate antibodies or as controls for Western blots. For more information about these products or any of our products, you can email us at: email@example.com.
Kessler E, Takahara K, Biniaminov L, et al. 1996; Bone morphogenetic protein-1: the type I procollagen C-proteinase.Science 271: 360–362.
Bessa, P. C., Casal, M., & Reis, R. L. (2008). Bone morphogenetic proteins in tissue engineering: the road from the laboratory to the clinic, part I (basic concepts). Journal of tissue engineering and regenerative medicine, 2(1), 1-13.
White PM, Morrison SJ, Orimoto K, et al. 2001; Neural crest stem cells undergo cell-intrinsic developmental changes in sensitivity to instructive differentiation signals. Neuron 29: 57–71.
Michos, O., Gonçalves, A., Lopez-Rios, J., Tiecke, E., Naillat, F., Beier, K., & Zeller, R. (2007). Reduction of BMP4 activity by gremlin 1 enables ureteric bud outgrowth and GDNF/WNT11 feedback signalling during kidney branching morphogenesis. Development, 134(13), 2397-2405.
Christ, B., & Brand-Saberi, B. (2002). Limb muscle development. International Journal of Developmental Biology, 46(7), 905-914.
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