| Grant number: | 13/26088-1 |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |
| Start date: | March 01, 2015 |
| End date: | October 31, 2015 |
| Field of knowledge: | Biological Sciences - Biophysics - Molecular Biophysics |
| Agreement: | Coordination of Improvement of Higher Education Personnel (CAPES) |
| Principal Investigator: | Antonio José da Costa Filho |
| Grantee: | Assuero Faria Garcia |
| Host Institution: | Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto (FFCLRP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil |
Abstract Alkaline phosphatases are enzymes that catalyze the hydrolysis of phosphomonoesters, thus producing phosphate and alcohol. These enzymes are dimers in solution and are found in the great majority of organisms. In humans, four alkaline phosphatases have been identified so far. Three of them are tissue-nonspecific alkaline phosphatases (TNAP) and can be expressed in any tissue in the body. In mammals, this enzyme is associated with a genetic disorder that can lead to different levels of failure of the bone mineralization (hypophosphatasia). The mechanisms used by TNAPs to permform their functions are still not completely understood, but it is believed that TNAPs somehow contribute to the increase of organic phosphate concentrations, promote bone mineralization, decreases concentration of extracellular phosphate, amongst others. TNAP is localized at the external part of the plasma membrane by means of a GPI (glycosylphosphatidylinositol) anchor. It is also frequently found associated with lipid rafts. Due to its biological relevance, TNAP has attracted attention of scientists from areas ranging from public health to basic Science, such as molecular biophysics. In this context, we propose in this project to use our expertise in the field of molecular biology and molecular biophysics to address the effects of lipid composition in the anchoring mechanism of TNAP and its natural mutants related to hypophosphatasia, as well as the effects of membrane models in the catalytic activity. To do so we will make use of a combined approach that will provide new insights about the TNAP structural features and its action mechanism, and it will be an important advance on basic Science and public health. (AU) | |
| News published in Agência FAPESP Newsletter about the scholarship: | |
| More itemsLess items | |
| TITULO | |
| Articles published in other media outlets ( ): | |
| More itemsLess items | |
| VEICULO: TITULO (DATA) | |
| VEICULO: TITULO (DATA) | |