TY - JOUR
T1 - The BMP-2 mutant L51P
T2 - a BMP receptor IA binding-deficient inhibitor of noggin
AU - Khattab, Hany Mohamed
AU - Kubota, Satoshi
AU - Takigawa, Masaharu
AU - Kuboki, Takuo
AU - Sebald, Walter
N1 - Publisher Copyright:
© 2018, The Japanese Society for Bone and Mineral Research and Springer Japan KK, part of Springer Nature.
PY - 2019/3/15
Y1 - 2019/3/15
N2 - 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.
AB - 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.
KW - BMP antagonist
KW - BMP negative feedback
KW - BMP-2
KW - L51P
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U2 - 10.1007/s00774-018-0925-0
DO - 10.1007/s00774-018-0925-0
M3 - Review article
C2 - 29667005
AN - SCOPUS:85045475648
VL - 37
SP - 199
EP - 205
JO - Journal of Bone and Mineral Metabolism
JF - Journal of Bone and Mineral Metabolism
SN - 0914-8779
IS - 2
ER -