The Structural and Chemical Role of Fetuin-A in Biomineralization

• Antragsteller: Dr. Wolf-Alexander Heiß
• Fachliche Zuordnung: Biochemie
• Förderung: Förderung von 2005 bis 2009
• Projektkennung: Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 5455056

Our work is focused on the ¿2 HS-glycoprotein / fetuin-A that is probably the most important systemic inhibitor of calcification. Fetuin-A deficient mice on a calcification sensitive DBA/2 genetic background develop massive calcifications throughout the body. After having identified the protein surface area that mediates the attachment to basic calcium phosphate surfaces, we also observed that the inhibition of mineral formation is based on colloidal fetuin-A mineral aggregates. We studied those particles using scattering methods and TEM. Within the next two years we will: · study the transformation of early amorphous fetuin-A mineral aggregates (calciprotein particles, CPP) to crystalline mature CPPs · produce CPPs and variants thereof for in vivo studies · model the docking of fetuin-A to apatite surfaces · develop an assay for the assessment of calcification risk in blood and support the development of synthetic inhibitors

• DFG-Verfahren: Schwerpunktprogramme
• Teilprojekt zu: SPP 1117: Prinzipien der Biomineralisation