The BMP-2 mutant L51P: a BMP receptor IA binding-deficient inhibitor of noggin

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作者
Hany Mohamed Khattab
Satoshi Kubota
Masaharu Takigawa
Takuo Kuboki
Walter Sebald
机构
[1] Fayoum University,Department of Prosthodontics, Faculty of Oral and Dental Medicine
[2] Okayama University Graduate School of Medicine,Advanced Research Center for Oral and Craniofacial Sciences
[3] Dentistry and Pharmaceutical Sciences,Department of Biochemistry and Molecular Dentistry
[4] Okayama University Graduate School of Medicine,Department of Oral Rehabilitation and Regenerative Medicine
[5] Dentistry and Pharmaceutical Sciences,Physiological Chemistry II
[6] Okayama University Graduate School of Medicine,undefined
[7] Dentistry and Pharmaceutical Sciences,undefined
[8] Theodor-Boveri-Institute for Biocenter of Würzburg University,undefined
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关键词
BMP-2; BMP antagonist; L51P; BMP negative feedback;
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摘要
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.
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页码:199 / 205
页数:6
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