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

  • Hany Mohamed Khattab
  • Satoshi Kubota
  • Masaharu Takigawa
  • Takuo Kuboki
  • Walter Sebald
Review Article
  • 5 Downloads

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.

Keywords

BMP-2 BMP antagonist L51P BMP negative feedback 

Abbreviation

BMP

Bone morphogenetic protein

BRI

BMP receptor type I

BRII

BMP receptor type II

CCN

Cysteine-rich 61, connective tissue growth factor, nephroblastoma-overexpressed

Notes

Acknowledgements

The author would like to thank all his colleagues in the Department of Oral Rehabilitation and Regenerative Medicine, the Department of Biochemistry and Molecular Dentistry, and the Department of Advanced Research Center for Oral and Craniofacial Sciences, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama, Japan, for their generous hosting and all kind assistances during the time taken to accomplish this review. The author also would like to thank Dr. Kristin Sainani A. Professor at Stanford University for her technical assistance.

Compliance with ethical standards

Conflict of interest

The authors declare that there is no conflict of interest.

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Copyright information

© The Japanese Society for Bone and Mineral Research and Springer Japan KK, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Department of Prosthodontics, Faculty of Oral and Dental MedicineFayoum UniversityFayoumEgypt
  2. 2.Advanced Research Center for Oral and Craniofacial SciencesOkayama University Graduate School of Medicine, Dentistry and Pharmaceutical SciencesOkayamaJapan
  3. 3.Department of Biochemistry and Molecular DentistryOkayama University Graduate School of Medicine, Dentistry and Pharmaceutical SciencesOkayamaJapan
  4. 4.Department of Oral Rehabilitation and Regenerative MedicineOkayama University Graduate School of Medicine, Dentistry and Pharmaceutical SciencesOkayamaJapan
  5. 5.Physiological Chemistry IITheodor-Boveri-Institute for Biocenter of Würzburg UniversityWürzburgGermany

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