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华东六省一市生物化学与分子生物学会2008年学术交流会

作者： Qing-Liang Zheng Jian Chen Yao-Zhou Zhang College of life science Zhejiang Sci-Tech University,Hang zhou 310018,China

We previously demonstrated that serine protease inhibitor BmSPI could strongly inhibit subtilisin *** order to characterrize the localization of BmSPI,the recombinant protein was expressed in Escherichia coli BL21(DE3)*** recombinant BmSPI was injected into the hypodermis of New Zealand white rabbit for producing polyclonal antibody,after affinity purification combined with reversed-phase *** titer of the antibody was determined above 1:106000 by *** using the immunocytochemistry method,we found the BmSPI localized in clusters near the membrane and through out the cytoplasm,but not in the *** studies of the ice slices for the 5th-instar larva indicated that BmSPI localized in a broad rang of tissues,mainly in the *** result was confirmed by the Western Blotting analysis and the real-time fluorescent quantificational RT-PCR against the total RNA from different tissues of the 5th-instar larva and four developmental stages(ovum,larva,pupae,moth), and the results indicated the expression level was the highest in the epidermis,but in the fat body was the ***,the expression levels vary in the different stage,with the highest in the larva and the lowest in the *** results may facilitate further understanding of the physiological function of BmSPI inhibitor.

关键词： Kazal-type Bombyx mori expression purification polyclonal antibody serine protease inhibitor real-time RT-PCR IHC

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serine protease inhibitors LmSPN2 and LmSPN3 co-regulate embryonic diapause in Locusta migratoria manilensis(Meyen)via the Toll pathway

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Journal of Integrative Agriculture 2023年第12期22卷 3720-3730页

作者： FENG Shi-qian ZHANG Neng CHEN Jun ZHANG Dao-gang ZHU Kai-hui CAI Ni TU Xiong-bing ZHANG Ze-hua State Key Laboratory for Biology of Plant Diseases and Insect Pests Institute of Plant ProtectionChinese Academy of Agricultural SciencesBeijing 100193P.R.China

Female adults of the migratory locust,Locusta migratoria manilensis(Meyen),can sense seasonal photoperiod changes,which induces embryonic diapause as a key strategy to *** protease inhibitor genes(SPNs)were thought to play key roles during diapause,while few SPNs were functionally ***2 was one of those genes differentially expressed between diapause and non-diapause eggs;however,its biological function remained to be ***,we conducted RNAi knockdown of LmSPN2,resulting in a significant decrease of the egg diapause rate by 29.7%.Using yeast two-hybrid assays,co-immunoprecipitation,and pull-down methods,we found an interaction between LmSPN2 and LmSPN3,which was proved to be mediated by a glutamate(E331)binding site of *** knockdown of LmSPN3 resulted in a significant increase in diapause rate by 14.6%,indicating an inverse function of LmSPN2 and LmSPN3 on diapause *** knockdown of two SPN genes resulted in a 26.4%reduction in diapause rate,indicating that LmSPN2 was the dominant regulatory ***,we found four Toll pathway genes(easter,spätzle,pelle,and dorsal)upregulated significantly after the knockdown of LmSPN2 while downregulated after the knockdown of ***,we speculate that two SPNs regulate diapause through the Toll *** results indicated that LmSPN2 positively regulates locust egg entry into diapause,while LmSPN3 is a negative regulator of embryonic commitment to *** interaction is mediated by the binding site of E331 and influences egg diapause through the Toll *** mechanistic understanding of diapause regulation expands our understanding of insect developmental regulation and provides functional targets for developing locust management strategies.

关键词： Locusta migratoria insect diapause regulation Toll pathway protein interaction serine protease inhibitor

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Application of scorpion venom peptides in tumor and virus research

Application of scorpion venom peptides in tumor and virus re...

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第12届生物毒素研究及医药应用学术大会

作者： Yu Song Zheng Fan Zhenhuan Zhao Wei Hong Zhengyang Zeng Nicolai E.Savaskan Wenxin Li Yingliang Wu Zhijian Cao State Key Laboratory of Virology College of Life Sciences Wuhan University Department of Neurosurgery University Hospital Erlangen Friedrich-Alexander University (FAU)of Erlangen-Nürnberg

A new peptide precursor,termed Sj7170,was characterized from the venomous gland cDNA library of the scorpion ***7170 was deduced to be a 62 amino acid peptide cross-linked by five disulfide *** recombinant Sj7170 peptide（rSj7170）with a chromatographic purity was produced by prokaryotic expression *** inhibition assay in vitro and in vivoshowed that rSj7170 specifically inhibited the activity of α-chymotrypsin at micromole *** addition,Sj7170 not only promoted cell proliferation and colony formation by up-regulating the expression of cyclinD1 in vitro,but also enhanced tumor growth in nude ***,Sj7170 accelerated cellular migration and invasion by increasing the expression of the transcription factor Snail and then inducing the epithelial-mesenchymal ***,Sj7170 changed cell morphology and cytoskeleton of U87 cells by GTPase *** together,Sj7170 is a unique dual-functional peptide:a specific α-chymotrypsin inhibitor and a potent tumorigenesis/*** work not only opens an avenue of developing new modulators of tumorigenesis/metastasis from serine protease inhibitors,but also strengthens the functional link between protease inhibitors and tumor *** brain tumors are hallmarked by fast proliferation and their ability to destruct the brain microenvironment for their growth *** chemotherapeutic strategies are currently lacking which combat this deadly disease *** glioma-specific chloride ion channel（GCC）represents a specific target for therapy and Chlorotoxin（CTX）,a peptide derived from scorpion venom has been shown to be efficacious and specific in blocking glioma CI- channel ***,we report on one new derivative（termed CA4） based on the CTX peptide sequence with high potency against glioma cell ***4 is effective in reducing glioma cell proliferation and cell ***,we found that CA4 and CTX are selective and s

关键词： Scorpion venom peptide serine protease inhibitor Glioblastoma Antiviral peptide HBV HCV Endosomal escape Signal pathway

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