RT Journal Article
ID 7a7974b85d93a9cc
A1 Sung, Su Kyoung
A1 Kim, Mi Jeong
A1 Lee, Dong Hee
A1 Choung, Se Young
A1 Kim, Byong Kak
A1 Kim, Ha Won
T1 β-Glucan of Ganoderma lucidum (W.Curt.:Fr.) Lloyd (Aphyllophoromycetideae) Cooperatively Induces Tumor Necrosis Factor-α and Interleukin-6 with Lipopolysaccharide by Binding to Dectin-1
JF International Journal of Medicinal Mushrooms
JO IJM
YR 2005
FD 2005-05-03
VO 7
IS 1&2
SP 193
OP 200
AB β-Glucan is a glucose polymer that has linkage of β-(1,3), -(1,4) and -(1,6). Exclusively found in fungal and bacterial, not in animal, cell walls, β-glucans are recognized by the innate immune system. Dendritic cells (DC) or macrophages possess pattern recognition molecules (PRM) for binding β-glucan in the pathogen-associated molecular pattern (PAMP). Recently, β-glucan receptor was cloned from DC and named dectin-1, which belongs to the type II C-type lectin family. Human dectin-1 consists of 7 exons and 6 introns.The polypeptide of dectin-1 has 247 amino acids and has cytoplasmic, transmembrane, stalk, and carbohydrate recognition domains. Dectin-1 can recognize a variety of β-1,3 and/or β-1,6 glucan linkages, but not α-glucans. In our macrophage cell line culture system, dectin-1 mRNAwas detected in RAW264.7 cells by a reverse transcription/polymerase chain reaction (RT-PCR). Dectin-1 was also detected in the murine organs of spleen, thymus, lung, and intestine. Treatment of RAW264.7 cells with β-glucans of Ganoderma lucidum (GLG) resulted in increased expression of IL-6 and TNF-α in the presence of LPS. However, GLG alone did not increase IL-6 or TNF-α. These results suggest that receptor dectin-1 cooperates with CD14 to activate signal transduction, which is very critical in immunoresponses.
PB Begell House
LK https://www.dl.begellhouse.com/journals/708ae68d64b17c52,2cbf07a603004731,7a7974b85d93a9cc.html