• International Journal of Industrial Entomology and Biomaterials
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• v.12 no.2
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• pp.69-73
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• 2006

To elucidate the composition of bumblebee (Bomb us terrestris) venom (BBV) and the anti-inflammatory effect of BBV. The major components of BBV by LC chromatography and SDS-PAGE were identified. The production of nitric oxide (NO) and proinflammatory cytokines was examined by lipopolysaccharide (LPS) in a macrophage cell line, RAW 264.7 cells, with BBV. BBV inhibits LPS-induced NO in a dose dependent manner. We also found that BBV inhibits proinflammatory cytokine, tumor necrosis factor (TNF)-${\alpha}$ and interleukin (IL)-6 production. These findings mean that BBV can be used in controlling macrophages mediated inflammation related disease. Additional studies on the pharmacological aspects of the individual components of BBV are recommended for future trials.

• International Journal of Industrial Entomology and Biomaterials
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• v.25 no.1
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• pp.115-121
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• 2012

The bumblebee Bombus terrestris is widely used in greenhouses to pollinate crops. Here, we report the molecular cloning and characterization of chymotrypsin inhibitor and chitin-binding protein homologs from B. terrestris. Two cDNAs encoding chymotrypsin inhibitor (Bt-CI) and chitin-binding protein (Bt-CBP) homologs were cloned from B. terrestris. Gene sequence analysis showed that Bt-CI gene consists of three exons encoding 75 amino acids, including a predicted 20-amino acid signal peptide, while Bt-CBP consists of two exons encoding 78 amino acids, including a predicted 26-amino acid signal peptide. The mature Bt-CI and Bt-CBP peptides contain ten and six conserved cysteine residues, respectively. Database searches using the deduced sequences of Bt-CI and Bt-CBP showed similarity to those from B. impatiens (96% peptide sequence identities). Bt-CI and Bt-CBP were expressed in both the venom gland and fat body of B. terrestris worker bees. The recombinant Bt-CI and Bt-CBP peptides were expressed in baculovirus-infected insect cells. Taken together, our findings describe the molecular characterization of Bt-CI and Bt-CBP from B. terrestris.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2005.11a
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• pp.69-69
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• 2005