Phatchariya Phannasil, Ph.D.
|Ph.D. (Biochemistry), Mahidol University, 2015
Tel. 02-441-9003-7 Ext. 1312, 1357
Email: email@example.com, firstname.lastname@example.org
Field of Research: Molecular Therapies in β-Thalassemia, Cancer Therapies
β-Thalassemia is a common hematological disease in Thailand resulting from mutations in β-globin gene. The reduction of β-chain synthesis causes a globin chain imbalance leading to ineffective erythropoiesis, hemolysis and microcytic hypochromic anemia. Nowadays, blood transfusion and iron chelation therapy are regular treatment for severe anemia. Iron overload eventually found and iron accumulation leads to heart problem, endocrine deficiencies and liver damage. The severity of β-thalassemia depends on the degree of β-globin reduction and unbounded excess α-globin chain. Reduction of α-globin expression may be an alternative therapy of β-thalassemia patients. Therefore, our researches are focused on molecular therapies in β-Thalassemia. These include investigation of miRNA to inhibit α-globin chain synthesis and studying on gene expression during erythropoiesis in β-thalassemia.
2. Cancer Therapies
Cancer is a public health issue because of its high incidence. Lacking of effective treatments leads to high mortality rate of cancer patients. Therefore, the investigation of therapeutic targets remains to be discovered and our main challenge for cancer therapy is to (1) investigate the more specific targets to discriminate between malignant and normal cells and (2) study on the natural products for cancer treatment.
1. Phannasil, P., Thuwajit, C., Warnnissorn, M., Wallace, J. C., MacDonald, M. J., & Jitrapakdee, S. (2015). Pyruvate carboxylase is up-regulated in breast cancer and essential to support growth and invasion of MDA-MB-231 cells. PloS one, 10(6), e0129848.
2. Phannasil, P., Israr-ul, H. A., El Azzouny, M., Longacre, M. J., Rattanapornsompong, K., Burant, C. F., … & Jitrapakdee, S. (2017). Mass spectrometry analysis shows the biosynthetic pathways supported by pyruvate carboxylase in highly invasive breast cancer cells. Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease, 1863(2), 537-551.