• 한국응용약물학회:학술대회논문집
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• 한국응용약물학회 2006년도 Proceedings of The Convention
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• pp.103-115
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• 2006

$\beta$-Glucan is a glucose polymer that has linkage of $\beta$-(1,3), -(1,4) and -(1,6). As exclusively found in fungal and bacterial cell wall, not in animal, $\beta$-glucans are recognized by innate immune system. Dendritic cells (DC) or macrophages possesses pattern recognition molecule (PRM) for binding $\beta$-glucan as pathogen-associated molecular pattern (PAMP). Recently $\beta$-glucan receptor was cloned from DC and named as dectin-l which belongs to type II C-type lectin family. Human dectin-1 is consisted 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 could recognize variety of beta-1,3 and/or beta-1,6 glucan linkages, but not alpha-glucans. In our macrophage cell line culture system, dectin-1 mRNA was detected in RA W264.7 cells by reverse transcription-polymerase chain reaction (RT-PCR). Dectin-1 was also detected in the murine organs of spleen, thymus, lung and intestines. Treatment of RA W264.7 cells with $\beta$-glucans of Ganoderma lucidum (GLG) resulted in increased expression of IL-6 and TNF-$\alpha$ in the presence of LPS. However, GLG alone did not increase IL-6 nor TNF-$\alpha$. These results suggest that receptor dectin-1 cooperate with CD14 to activate signal transduction that is very critical in immunoresponse.

• 한국약용작물학회:학술대회논문집
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• 한국약용작물학회 2006년도 Proceedings of The Convention of The Korean Society of Applied Pharmacology
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• pp.103-115
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• 2006

[ ${\beta}-Glucan$ ] is a glucose polymer that has linkage of ${\beta}-(1,3)$, -(1,4) and -(1,6). As exclusively found in fungal and bacterial cell wall, not in animal, ${\beta}-glucans$ are recognized by innate immune system. Dendritic cells (DC) or macrophages possesses pattern recognition molecule (PRM) for binding ${\beta}-glucans$ as pathogen-associated molecular pattern (PAMP). Recently ${\beta}-glucans$ receptor was cloned from DC and named as dectin-l which belongs to type II C-type lectin family. Human dectin-l is consisted of 7 exons and 6 introns. The polypeptide of dectin-l has 247 amino acids and has cytoplasmic, transmembrane, stalk and carbohydrate recognition domains. Dectin-l could recognize variety of beta-l,3 and/or beta-l,6 glucan linkages, but not alpha-glucans. In our macrophage cell line culture system, dectin-l mRNA was detected in RA W264.7 cells by reverse transcription-polymerase chain reaction (RT-PCR). Dectin-l was also detected in the murine organs of spleen, thymus, lung and intestines. Treatment of RA W264.7 cells with ${\beta}-glucans$ of Ganoderma lucidum (GLG) resulted in increased expression of IL-6 and $TNF-{\alpha}$ in the presence of LPS. However, GLG alone did not increase IL-6 nor $TNF-{\alpha}$ These results suggest that receptor dectin-l cooperate with CD14 to activate signal transduction that is very critical in immunoresponse.

• Asian Pacific Journal of Cancer Prevention
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• 제17권2호
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• pp.455-461
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• 2016

Galectins are ${\beta}$-galactoside binding lectins that contain one or more carbohydrate recognition domains. As a consequence of sugar-binding properties, galectins exhibit a variety of interactions with glycoproteins, thus playing important roles in various pathological processes. A number of studies have shown roles of galectins in cancer. Galectin-7 is a prototype member of the galectin family implicated in epithelial stratification and cell migration. It can act as a potent dual regulator in different types of cancer. Galectin-7 may contribute either to neoplastic transformation and tumour progression through regulation of cell growth, cell cycle, angiogenesis, apoptosis and cell migration or may have a protective effect in cancer depending on the tissue type. A perusal of the literature indicates particular roles of galectin-7 in carcinomas and melanomas, while contributions await greater exploration in other types of cancers including sarcomas and leukemia. This review collectively summarizes available literature on expression and roles of galectin-7 in different cancers.