SUNGKYUNKWAN UNIVERSITY SCHOOL OF MEDICINE

Alzheimer’s Disease (AD) is a typical neurodegenerative disease caused by increased amyloid b-protein (Ab) production. One of main genetic cause of AD is mutations in presenilin protein, which increases the production of Ab. We previously reported for the first time that presenilin mutation induces calcium signaling dysfunction (Yoo et al., Neuron, 2000). We also reported that presenilin mutation decreases one of major lipid component in plasma membrane (PIP2), which resulted in the decreased TRPM7 channel activity (Landman et al., PNAS, 2006). Currently, we study the molecular mechanism for the regulation of Ab production in relation to calcium signaling. Based on our research results, we also try to find a new target for therapeutic drugs for AD.

 

Yoo et al. (2000) Presenilin-mediated modulation of capacitative calcium entry. Neuron 27:561-572.

Landman et al. (2006) Presenilin mutations linked to familial Alzheimer’s disease cause an imbalance in phosphatidyl-4,5-bisphosphate metabolism. PNAS, 103:19524-19529.

Kang et al. (2013) Modulation of lipid kinase PI4KIIa activity and lipid raft association of presenilin 1 underlies g-secretase inhibition by ginsenoside. J. Biol. Chem., 288:20868.

Chun et al. (2015) O-GlcNAcylation promotes non-amyloidogenic processing of amyloid-b protein precursor via inhibition of endocytosis from the plasma membrane. J. Alzheimer’s Disease 44:261.

 

(Tel) +82-31-299-6103,  (Email) schung@skku.edu