What Is a Bone Morphogenetic Protein?
Bone morphogenetic proteins (BMPs), also known as bone morphogenetic proteins, are a group of highly conserved functional proteins with similar structures, belonging to the TGF-beita family. BMP can stimulate DNA synthesis and cell replication, thereby promoting the directional differentiation of mesenchymal cells into osteoblasts.
Bone morphogenetic protein
- Chinese name
- Bone morphogenetic protein
- Foreign name
- bone morphogenetic protein, BMP
- Short name
- BMP
- Subject
- life sciences
- nickname
- Bone morphogenetic protein
- Bone morphogenetic proteins (BMPs), also known as bone morphogenetic proteins, are a group of highly conserved functional proteins with similar structures, belonging to the TGF-beita family. BMP can stimulate DNA synthesis and cell replication, thereby promoting the directional differentiation of mesenchymal cells into osteoblasts.
- Bone morphogenetic proteins (BMPs), also known as bone morphogenetic proteins, are a group of highly conserved functional proteins with similar structures, belonging to the TGF- family. BMP can stimulate DNA synthesis and cell replication, thereby promoting the directional differentiation of mesenchymal cells into osteoblasts. It is also the main factor that induces bone and cartilage formation in vivo and is expressed during limb growth, endochondral ossification, early fractures, and cartilage repair, and plays an important role in embryo development and regeneration and repair of bones. Today, the BMP family has 43 members, which are widely present in the tissues of embryos, blood cells, kidneys, and spleen of pigs, cattle, sheep, rabbits, mice, and humans, and have high homology among different species. BMP not only participates in the regulation of bones, but also plays a role in the development of fat, kidneys, liver, bones and nervous system.
- In 1889, Senn first used demineralized bone to repair inflammatory bone defects in humans and dogs, demonstrating that decalcified bovine bone can be used to treat osteomyelitis. In 1931, Huggins discovered that the urinary tract epidermis could induce new bone formation ectopically, and reported for the first time the process of osteoinduction experiments. In 1945, Lacroix extracted "osteoblasts" from bone mass that can induce osteogenesis of rabbit muscle. He put forward the hypothesis of osteoinduction and named it osteogenic protein. In 1965, Urist discovered that when decalcified bone matrix gelatin (DBM) was injected into muscles, muscle mesenchymal cells could be transformed into bone cells, and ectopic induced osteogenesis occurred. Urist thought at the time that this decalcified bone might contain an inducing factor that could induce the mesenchymal cells that swim around the blood vessels to turn into irreversible osteoblasts, which could produce cartilage and bone tissue in bones or tissues other than bones . The inducing factor is a bone morphogenetic protein. With the development of molecular biology and genetic engineering, in 1988, Wozney et al. First carried out BMP cDNA cloning research. They cloned hBMP-1, BMP-2a (BMP-2) and BMP-2b using recombinant DNA technology. (Ie BMP-4) and BMP-3 cDNA, and expressed in eukaryotic cells and prokaryotic cells of Escherichia coli. In 1990, Celeste et al reported the cloning research of BMP-5, BMP-6, and BMP-7, and suggested that the cloned BMPs be named BMP-1, BMP-2, BMP-3, BMP-4, and BMP- 5. BMP -6, BMP -7. At the same time, Ozkaynak reported the cloning study of osteogeneic protein-1 (OP-1). The gene and amino acid sequences of OP-1 and BMP-7 were compared to prove that they are the same polypeptide. In 1992 (zkaynak also reported the cloning study of OP-2 cDNA. By 1996 it had been developed into BMP-13, and the corresponding cDNA clone had been obtained.
- The BMP monomer consists of a signal peptide, a pre-functional region, and a mature peptide.Its structure is similar to a flat curved surface, and usually includes a long -helix and two pairs of reverses from the ends of the -helix. Parallel beta strands. This structure can be described as a hand with four fingers, that is, each chain represents a finger, and the -helix is similar to a wrist joint. Each monomer contains an ordered sequence of 7 cysteine residues, of which 6 cysteine residues form a disulfide bond within 3 monomer structures with each other, through a characteristic " "Cysteine knot" motif (1 disulfide bond through the ring structure formed by the other 2 disulfide bonds) to maintain the integrity of the monomer structure; the remaining cysteine residue is involved in the formation of two Disulfide bonds between monomers to stabilize the dimer structure. Mature BMP proteins are homo- or heterodimers linked by disulfide bonds, all of which are molecularly active. After being released outside the cell, they bind to the corresponding receptors on the surface of the target cell and play a role [1]
- After being secreted, BMP can not only bind to extracellular matrix and soluble antagonists, but also interact with protein receptors on the surface of various cell membranes. Not only does it have unique structural and physicochemical properties that are different from other bone growth factors, but also the gene location and osteogenesis mechanisms of different members of its family are different. BMP mainly works by relying on two signaling pathways, namely the Smad pathway and p38-MAPK pathway, and the signal transduction process is controlled by four levels of regulation: extracellular antagonists, membrane receptors, cytoplasmic microenvironment and transcription levels. In terms of treatment, BMP can not only mediate osteogenesis alone, but also can be mixed with other bone growth factors, thereby enhancing its curative effect. One of the shortcomings of bone growth factor is its short half-life and easy degradation in the body. Therefore, slow-release technology is often used for local application to delay its decay [1] .