Incorporation of Heparin-Binding Domains to BMP9 to Enhance Extracellular Matrix Retention and Osteogenic Signaling
Session Number
2
Advisor(s)
Dr. Tong-Chuan He, Dr. Yi Zhu, Dr. Yuting Liang, University of Chicago
Location
B116
Discipline
Medical and Health Sciences
Start Date
15-4-2026 11:10 AM
End Date
15-4-2026 11:55 AM
Abstract
BMP9 (Bone morphogenetic protein 9) is a potent inducer of stem cell osteogenesis differentiation, however, it does not naturally contain heparin-binding (HB) domains which is essential for extracellular matrix (ECM) interaction, intercellular signaling and localized growth. In contrast, although BMP2 exhibits relatively lower osteogenic potency, it possesses an inherent N-terminal HB domain that facilitates optimal ECM anchoring. Thus, gene editing may help edit those desired heparin-binding sequences into BMP9. By evaluating and comparing the HB domains from five other growth factors, the HB domain from FGF2 was selected as the most effective. Furthermore, a recombinant adenovirus vector will be used to overexpress the heparin-binding modified BMP9, to compare its osteogenesis potential with that of wild type BMP9, and to elucidate the underlying molecular mechanisms.
Incorporation of Heparin-Binding Domains to BMP9 to Enhance Extracellular Matrix Retention and Osteogenic Signaling
B116
BMP9 (Bone morphogenetic protein 9) is a potent inducer of stem cell osteogenesis differentiation, however, it does not naturally contain heparin-binding (HB) domains which is essential for extracellular matrix (ECM) interaction, intercellular signaling and localized growth. In contrast, although BMP2 exhibits relatively lower osteogenic potency, it possesses an inherent N-terminal HB domain that facilitates optimal ECM anchoring. Thus, gene editing may help edit those desired heparin-binding sequences into BMP9. By evaluating and comparing the HB domains from five other growth factors, the HB domain from FGF2 was selected as the most effective. Furthermore, a recombinant adenovirus vector will be used to overexpress the heparin-binding modified BMP9, to compare its osteogenesis potential with that of wild type BMP9, and to elucidate the underlying molecular mechanisms.