1. The BMP-2 mutant L51P: a BMP receptor IA binding-deficient inhibitor of noggin
- Author
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Hany Mohamed Khattab, Masaharu Takigawa, Walter Sebald, Satoshi Kubota, and Takuo Kuboki
- Subjects
0301 basic medicine ,animal structures ,Endocrinology, Diabetes and Metabolism ,medicine.medical_treatment ,Bone Morphogenetic Protein 2 ,030209 endocrinology & metabolism ,Bone morphogenetic protein 2 ,03 medical and health sciences ,0302 clinical medicine ,Endocrinology ,medicine ,Animals ,Humans ,Orthopedics and Sports Medicine ,Noggin ,Bone regeneration ,Receptor ,Bone Morphogenetic Protein Receptors, Type I ,BMP receptor binding ,Chemistry ,Growth factor ,General Medicine ,Cell biology ,embryonic structures ,Mutant Proteins ,030101 anatomy & morphology ,Chordin ,Carrier Proteins ,Gremlin (protein) ,Protein Binding ,Signal Transduction - Abstract
The antagonist-specific regulation in tissue engineering constitutes important attempts to achieve an improved and rapid bone regeneration by controlling the natural biological response of the natural body growth factors. L51P is molecularly engineered bone morphogentic protein-2 (BMP-2) variant with a substitution of the 51st leucine with a proline residue. L51P is deficient in BMP receptor binding, but maintains its structure and affinity for inhibitory proteins such as noggin, chordin, and gremlin. These modifications convert the BMP-2 variant L51P into a receptor-inactive inhibitor of BMP antagonists. This current approach may prevent the uncontrolled bone overgrowth using high concentration of BMPs and thus regulates the possible growth factor's high-dose side effects. Exploring of L51P biological functions is required to broad our understanding of BMP mutant biological functions and their potential clinical applications. The progress of L51P researches would hopefully lead to the development of multiple applications for using the L51P in bone and fracture healing disorders.
- Published
- 2018