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language
eng
Author
EDAMATSU, TAKEO
FUJIEDA, AYAKO
FUJIOKA, MASAKI
WADA, TSUTOMU
Description
Abstract. Protein-bound polysaccharide-K (PSK) is extracted from Coriolus versicolor (CM101). PSK is a biological response modifier (BRM), and its mechanism of action is partly mediated by modulating host immune systems; however, recent studies showed antiproliferative activity of PSK. Therefore, we examined the mechanism underlying the antiproliferative activity of PSK using seven different human malignant cell lines (WiDr, HT29, SW480, KATOⅢ, AGS, HL-60 and U937), and PSK was found to inhibit the proliferation of HL-60 cells most profoundly. Therefore, HL-60 cells were used to elucidate the mechanism of the antiproliferative activity. Western blotting was performed to detect phosphorylated p38 mitogen-activated protein kinase (MAPK). A p38 MAPK inhibitor, SB203580, was used to examine the roles in PSK-induced apoptosis and growth inhibition. Flow cytometry was performed for mitochondrial membrane potential detection. PSK activated caspase-3 and induced p38 MAPK phosphorylation. Co-treatment with SB203580 blocked PSK-induced apoptosis, caspase-3 activation and growth inhibition. PSK induced apoptosis via the mitochondrial pathway. The depolarization of mitochondria induced by PSK was reversed by co-treatment with SB203580. The present study revealed that PSK induced apoptosis in HL-60 cells via a mitochondrial and p38 MAPK-dependent pathway.
Subject
protein-bound polysaccharide-K
apoptosis
mitochondrial pathway
p38 mitogen-activated protein kinase
HL-60 cell
Journal Title
ONCOLOGY REPORTS
Volume
30
Start Page
99
End Page
104
ISSN
1021-335X
Published Date
2013-4-22
DOI
Publisher
Spandidos Publications
NII Type
Journal Article
Format
PDF
Text Version
出版社版
Gyoseki ID
e22437
OAI-PMH Set
Faculty of Medicine