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- 저자 : Cong-Fen Zhang (검색결과 3 건)
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Three homologous genes encoding functional D8-sphingolipid desaturase in Populus tomentosa
Shu-Fen Li,Zan-Min Hu,Guo-Jun Zhang,Ying-Chun Yuan,Cong-Hui Wang,Wu-Jun Gao,Chuan-Liang Deng,Long-Dou Lu 한국유전학회 2014 Genes & Genomics Vol.36 No.3
Δ8-sphingolipid desaturase is characterized by itsability to catalyze desaturation at the C8 position of the longchainbase of sphingolipids in plants. No previous studieshave been conducted on genes encoding Δ8-sphingolipiddesaturases in the woody plant Populus tomentosa. In thisstudy, three genes that encode Δ8-sphingolipid desaturasewere isolated fromP. tomentosa. Among these genes, PtD8Aand PtD8B showed high sequence similarity; whereas PtD8Cexhibited large sequence divergence.RT-PCRresults showedthat PtD8A and PtD8B were expressed in all tissues detected,whereas PtD8C was not expressed in roots. Heterologousexpression in yeast revealed that PtD8A/B/C were functionalΔ8-sphingolipid desaturases, and can catalyze the C18-phytosphingeninedesaturation to produce 8(Z)- and 8(E)-C18-phytosphingenine.However, the conversion rate and ratios ofthe two products differed. Compared with control cells,transgenic yeasts expressing PtD8A/B/C exhibited enhancedaluminum tolerance. Our findings further elucidated thebiochemical functions and evolutionary history ofΔ8-sphingolipid desaturases in plants. Candidate genes forbreeding new poplar germplasm resources with enhancedtolerance ability to aluminium were also provided.
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Sulfakinin inhibits activity of digestive enzymes in the brown planthopper, Nilaparvata lugens
Guo Di,Zhang Su,Zhang Yi-Jie,Ma Jun-Yu,Gao Cong-Fen,Wu Shun-Fan 한국응용곤충학회 2020 Journal of Asia-Pacific Entomology Vol.23 No.4
In animals, feeding can regulate release of digestive enzymes. Digestive enzymes are produced and released in response to specific ratios of nutrients, so the quality and quantity of food ingested are important factors in the secretion and activity of digestive enzymes. In general, the enzyme activity and secretion in the fed insects are relatively higher than that in the unfed insects. Neuropeptides and peptide hormones are important regulators of enzyme activity. In several insects, the neuropeptide sulfakinin (SK) is known to be a regulator of feeding and digestion similar to cholecystokinin in mammals. However, the roles of diet and SK in regulation of activity of digestive enzymes in the important pest insect, the brown planthopper (Nilaparvata lugens), are unknown. In this study, we identified six genes encoding different digestive enzymes and cloned three of these. We found that enzymatic activity and transcriptional levels of digestive enzymatic activity genes were upregulated by refeeding animals for 5 h after 24 h starvation. Furthermore, injection of N. lugens SK reduces digestive enzyme activity and leads to a downregulation of digestive enzyme gene transcripts. This study provides new views into the action of diet and SK in regulation of digestive enzymes in (hemimetabolous) insects. Taken together with the roles of SK in inducing satiety, our data strongly suggest that SK signaling is important in regulation of food ingestion and processing.
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Li-Shang Dai,Cen Qian, LeiWang,Guo-Qing Wei,Qiu-Ning Liu,Yu Sun,Cong-Fen Zhang,Jun Li,Dong-Ran Liu,Bao-Jian Zhu,Chao-Liang Liu 한국응용곤충학회 2015 Journal of Asia-Pacific Entomology Vol.18 No.4
Peptidoglycan recognition proteins (PGRPs) are conserved proteins in animals from insects to mammals and play an important role in immune response by recognizing peptidoglycan on microbial surfaces. In this study, a PGRP gene from Antheraea pernyi, named Ap-PGRP-A, was isolated and characterized. Sequence analysis revealed that the full-length cDNA of Ap-PGRP-A was 961 bp, containing a 40 bp 5′-untranslated sequence, a 339 bp 3′-untranslated region and an open reading frame of 582 bp. This gene encoded a putative protein of 193 amino acid residues. Phylogenetic analysis indicated that Ap-PGRP-A had the closest protein sequence similarity to Antheraea mylitta PGRP. The recombinant protein was successfully expressed in Escherichia coli cells and a rabbit anti-Ap-PGRP-A antibody was also prepared. Real-time quantitative reverse transcription-PCR analysis showed that Ap-PGRP-A was extensively expressed in the fat body, midgut, hemocyte,malpighian tubule and epidermis of A. pernyi, especially in the fat body and midgut. The expression levels of Ap-PGRP-A were significantly up-regulated by three types of microorganisms, and Ap-PGRP-A expression was more sensitive in response to the Gram-negative bacterium E. coli than the Gram-positive bacterium Bacillus subtilis or the fungus Beauveria bassiana. These data indicate that Ap-PGRP-A may play a role in the innate immune responses of A. pernyi.
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