• Title/Summary/Keyword: aminopeptidase N(APN)

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Identification of Two Isoforms of Aminopeptidase N in Aedes aegypti Larval Midgut

  • Pootanakit, Kusol;Angsuthanasombat, Chanan;Panyim, Sakol
    • BMB Reports
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    • v.36 no.5
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    • pp.508-513
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    • 2003
  • The bacterium Bacillus thuringiensis produces toxin inclusions that are deleterious to target insect larvae. These toxins are believed to interact with a specific receptor protein(s) that is present on the gut epithelial cells of the larvae. In various insect species (in particular those belonging to the lepidopteran class), aminopeptidase N (APN) is one of the two receptor proteins that are considered to be involved in toxin-receptor interactions. However, in mosquitoes, the nature and identity of the receptor protein is unknown. Here, using RT-PCR, we identified two isoforms of the APN transcripts in the Aedes aegypti mosquito larval midgut. These results are congruent with a previous report of multiple isoforms of the APN gene expression in lepidopteran larvae. Which of the two isoforms (or other yet unidentified receptor proteins) is involved in the killing of mosquito larvae remains to be elucidated.

Screening of Biological Activities in Fern Plants Native to Jeju Island (제주도에 자생하는 양치식물의 생리활성 검색)

  • Oh, Soon-Ja;Hong, Sung-Soo;Kim, Yeon-Hee;Koh, Seok-Chan
    • Korean Journal of Plant Resources
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    • v.21 no.1
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    • pp.12-18
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    • 2008
  • Antioxidative activity and inhibitory activity of angiotensin I converting enzyme(ACE), aminopeptidase N(APN) and $\alpha$-amylase were investigated in the methanol extracts from 25 fern plants native to Jeju Island, in order to screen the plant species containing bioactive materials for functional foods or medicines. The antioxidative activity was higher in Cytomium fortunei(41.9%) and Rumohra standishii(34.1%) than in leaves of Thea sinensis(30.9%), a small tree for antioxidative beverage. Inhibitory activities of ACE and APN were relatively high in Cytomium fortunei as 26.7% and 28.2% respectively. $\alpha$-Amylase inhibitory activity was higher than 50% in 10 species. Particularly, Cytomium fortunei(87.4%) and Dryopteris erythrosora(71.6%) showed the inhibitory activities higher than those of other form plants. Of 25 fern plants investigated here, Cytomium fortunei showed not only the highest antioxidative activity but also the highest inhibitory activity of ACE, APN and $\alpha$-amylase. It suggests that Cytomium fortunei could be potentially used as a resource of bioactive materials for fuctional foods or medicines.

The N-terminal Region of the Porcine Epidemic Diarrhea Virus Spike Protein is Important for the Receptor Binding (PED 바이러스 Spike 단백질의 세포 수용체 결합 부위 확인)

  • Lee, Dong-Kyu;Cha, Se-Yeoun;Lee, Chang-Hee
    • Microbiology and Biotechnology Letters
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    • v.39 no.2
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    • pp.140-145
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    • 2011
  • Porcine epidemic diarrhea virus (PEDV) infection causes acute enteritis with lethal watery diarrhea resulting in a high mortality rate in piglets. As with the other members of group 1 coronaviruses, PEDV also utilizes the host aminopeptidase N (APN) as the major cellular receptor for entry into target cells. The coronavirus spike (S) protein is known to interact with the cellular surface for viral attachment and the S1 domain of all characterized coronaviruses contains a receptor-binding domain (RBD) that mediates a specific high-affinity interaction with their respective cellular receptors. Although the RBDs of several coronaviruses have been mapped, the location of the PEDV RBD has to date not been defined. As a first step toward the identification of the region of the S protein of the PEDV that is critical for recognition with the cellular receptor, we generated a series of S1-truncated variants and examined their abilities to bind to the porcine APN (pAPN) receptor. Our data indicate that the N-terminus of the S1 domain is required for pAPN association. The results from the present study may assist in our understanding of the molecular interactions between the PEDV S protein and the pAPN receptor.

Antioxidative activity, including Inhibitory activities of ACE, APN and $\alpha$-amylase, in Theaceae Plants Native to Jeju Island (제주도 자생 차나무과 식물의 ACE, APN, $\alpha$-amylase 저해 활성 및 항산화활성에 대한 연구)

  • Oh, Soon-Ja;Lee, Jin-Ho;Ko, Kwang-Sup;Shin, Dong-Bum;Koh, Seok-Chan
    • Korean Journal of Plant Resources
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    • v.23 no.5
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    • pp.406-414
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    • 2010
  • Antioxidative activity, including inhibitory activities of angiotensin I converting enzyme(ACE), aminopeptidase N(APN) and $\alpha$-amylase, was investigated in the methanol extracts from Theaceae plants native to Jeju island, in order to select the plant species containing bioactive materials for functional food or medicines. ACE inhibitory activity was above 50% in Ternstroemia japonica(stem bark) and Cleyera japonica(leaf), and APN inhibitory activity was low to be positive only in C. japonica(leaf, stem bark) and T. japonica(stem bark). $\alpha$-Amylase inhibitory activity was above 30% in Camellia japonica(fruit), Eurya emarginata(stem), T. japonica(stem bark) and Thea sinensis(stem). The antioxidative activity, estimated by the DPPH radical scavenging capacity, was above 30% in C. japonica(stem bark), T. japonica(stem bark) and T. sinensis(leaf). Particularly, the antioxidative activity analyzed by dot-blot test was very high in C. japonica(stem bark) relatively to those of other plants, and remained high in the low concentration($1.25\;{\mu}g/m{\ell}$). From the TLC analysis of antioxidative compounds, EGC(Rf 0.26) was found to have high activity in stem bark of C. japonica and EGCG(Rf 0.09) was found to have high activity in stem bark of C. japonica, E. emarginata, and T. japonica. Five bands (Rf 0.54, 0.46,0.44, 0.16, 0.03) which were not identified as compared with catechins were detected as polyphenolic compounds on the TLC plates sprayed with the Folin-Ciocalteu solution or the Ferric chloride-alcohol solution. These results suggests that Theaceae plants except E. japonica could be potentially used as a resource of bioactive materials for functional foods or medicines and further research is reguired to identify the bioactive substances and determine the functions of them.