• Journal of Life Science
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• v.25 no.6
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• pp.715-723
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• 2015

Insects represent the largest class within the animal kingdom in terms of species number. Humans had been utilized insect in the broad area, including food, agriculture, industry, pharmaceuticals and so on. At present, insects are emerging as a leading group for identifying and extracting novel bioactive substances due to enormous number and a high nutritional value. Insects rely on a suite of systemic response to resist infection such as immune cells, hemocytes, activation of enzymes cascades, and antimicrobial peptide/protein. Among the substances, antimicrobial peptides (AMPs) are main components of potent antimircrobial innate defense system into the insect hemolymph. AMPs raise influential candidate as avenue to resolve the development of antibiotic-resistant microbial organism. Insect AMPs are classified into four main classes: cecropins, insect defensins, glycine/proline-rich peptides. Insect AMPs have been purified, over 150. In this review, AMPs derived from several insects were summarized including honey bee, dung beetle, butterfly and longicorn beetle. These peptides almost exhibited potent antimicrobial activities against human microbial pathogens without causing remarkable hemolysis to erythrocytes excluding melittin, and their mode of action(s) are based on disruption of the plasma membrane or fungal apoptosis. Therefore, study of insect AMPs is expected to be useful for designing novel therapeutic antimicrobial applications.

• Korean journal of applied entomology
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• v.60 no.3
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• pp.263-268
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• 2021

The venom of honeybees (Apis mellifera L.) is used to treat many diseases because of its anti-inflammatory and analgesic effects. Bee venom consists of several biologically active molecules and exhibits remarkable anti-cancer effects. However, biological amines, which exhibit diverse functionality such as anti-inflammatory and antibacterial effects, have not been previously reported in bee venom. In this study, we determined the content of putrescine in bee venom by using ultra-performance liquid chromatography. The specificity, accuracy, and precision of the assay were assessed, and the assay validated. The linearity of the putrescine assay was r ≥ 0.99, indicating a moderate level of putrescine in the bee venom. The limit of detection and limit of quantification were both 0.9 ㎍/mL, while the rate of recovery was 96.4%-99.9%. The relative standard deviation (RSD) of the intra-day precision and inter-day precision of the putrescine assay were 0.16% - 0.23% and 0.09% - 0.36%, respectively, with the RSD ≤ 5% indicating excellent precision. Thus, the linearity, limit of detection, limit of quantification, and recovery rate of the putrescine assay were satisfactory. The analysis of the bee venom showed that the putrescine content was 3.1 ± 0.09 mg/g. This study provides fundamental data on putrescine content in bee venom, which will prove useful in further studies of its bioactivity.

• Journal of Life Science
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• v.22 no.1
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• pp.41-48
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• 2012

Bee venom (BV) has been used in medicine to treat a variety of diseases including arthritis, rheumatism, and various cancers. Recent reports indicate that BV has anti-angiogenic effects, but the precise molecular mechanism underlying the effects of BV against colorectal cancer remains to be elucidated. We examined the effects of BV and its major components (melittin and apamin) on tumor angiogenesis and found that BV significantly decreased protein levels of hypoxia-inducible factor-$1{\alpha}$ (HIF-$1{\alpha}$), an important factor involved in angiogenesis and tumor progression, in human colorectal carcinoma HCT116 cells. BV also suppressed the transcription of HIF-$1{\alpha}$ under hypoxia, leading to a decrease in the expression of vascular endothelial growth factor (VEGF), a major target gene of HIF-$1{\alpha}$. We also found that these effects were mainly elicited by apamin, but not melittin. BV specifically inhibited the phosphorylation of ERK1/2 without changing the total levels of this protein, but had no effect on kinases of p38/JNK and AKT. Our results suggest that BV may inhibit human colorectal cancer progression and angiogenesis by inhibiting HIF-$1{\alpha}$ and VEGF expression, thereby providing a novel potential mechanism for the anticancer action of BV.