A mechanism of translocation of cytosolic Heat shock protein 27 (Hsp27) to surface of cancer cells

• Main Authors: Wu, Hsin-yi, 吳欣怡
• Other Authors: Liao, Kuang-Wen
• Format: Others
• Language: en_US
• Published: 2013
• Online Access: http://ndltd.ncl.edu.tw/handle/56552821425898105739

碩士 === 國立交通大學 === 分子醫學與生物工程研究所 === 101 === Stress or heat shock proteins (HSPs) are the most conserved proteins present in both prokaryotes and eukaryotes. Their expressions are induced in response to a wide of physiological and environmental insults. Intracellular heat shock protein (Hsp) 27 is ubiquitously expressed in various cell types and is involved in actin polymerization, and inhibition of mitochondrial apoptosis. Recent researches show that Heat shock proteins (Hsps) are overexpressed in a wide range of human cancers and are implicated in tumor cell proliferation, differentiation, invasion, metastasis, death, and recognition by the immune system. In cancer cells, the expression of Hsp27 is abnormally high, and Hsp27 may participate in oncogenesis and in chemoresistance. In addition, current research has shown that Hsp 27 were located in the cytoplasm or nucleus. In this study, we found that Hsp27 is overexpressed on outer surface of human cancer cells but not normal human cells. However, the mechanisms of Hsp27 translocation to cancer cell surface are not defined yet. Our results suggest that PKC-□ and NF-κB signaling pathway negative mediated Hsp27 translocation to cancer cell surface by phosphorylation at Hsp27 serine 15. Moreover, HSP27 only when phosphorylated at serine 78 were overexpression on the cell surfaces.