Hsp27 Reduces Phosphorylated Tau and Prevents Cell Death in the Human Neuroblastoma Cell Line SH-SY5Y

• Published in: Bulletin of the Korean Chemical Society Vol. 34; no. 5; pp. 1503 - 1507
• Main Authors: Ahn, Junseong, Kim, Hyeseon, Park, Jong-Sang
• Format: Journal Article
• Language: English
• Published: 대한화학회 20.05.2013
• Subjects: 화학
• ISSN: 0253-2964; 1229-5949
• DOI: 10.5012/bkcs.2013.34.5.1503

The two major symptoms characterizing Alzheimer’s disease are the formation of amyloid-β extracellular deposits in the form of senile plaques and intracellular neurofibrillary tangles (NFTs) that consist of pathological hyperphosphorylated tau protein aggregated into insoluble paired helical filaments (PHFs). Neurons of the central nervous system have appreciable amounts of tau protein, a microtubule-associated protein. To maintain an optimal operation of nerves, the microtubules are stabilized, which is necessary to support cell structure and cellular processes. When the modified tau protein becomes dysfunctional, the cells containing misfolded tau cannot maintain cell structure. One of the pathological hallmarks of Alzheimer’s disease is hyperphosphorylated tau protein. This paper shows that the small heat shock protein from humans (Hsp27) reduces hyperphosphorylated tau and prevents hyperphosphorylated tau-induced cell death of the human neuroblastoma cell line SH-SY5Y. KCI Citation Count: 1