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2018 | 58 | 1 |

Tytuł artykułu

Effects of specific inhibitors on the gene expression of a digestive trypsin in Pieris brassicae L. (Lepidoptera: Pieridae)

Treść / Zawartość

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Protein digestion in insects relies on several groups of proteases, among which trypsin plays a prominent role. In the current study, larvae of Pieris brassicae L. were fed radish leaves treated with 1 mM concentrations of three specific inhibitors of trypsin: AEBSF.HCl [4-(2- -aminoethyl)-benzenesulfonyl fluoride, monohydrochloride], TLCK (N-a-tosyl-l-lysine chloromethyl ketone) and SBTI (Soybean Trypsin Inhibitor) to find their potential effects on gene expression of trypsin. Initially, RT-PCR analysis revealed a gene of 748 bp responsible for synthesizing the digestive trypsin in P. brassicae larvae. Also, qRT-PCR data indicated a statistically greater expression of trypsin gene in the larvae fed 1 mM concentrations of AEBSF.HCl, TLCK and SBTI than the control. Results of the current study indicated that synthetic inhibitors can not only negatively affect the gene expression of P. brassicae trypsin, but also the insect can activate a compensatory mechanism against interruption of protein digestion by inducing more expression of the gene and producing more trypsin into the midgut lumen.

Wydawca

-

Rocznik

Tom

58

Numer

1

Opis fizyczny

p.96-101,fig.,ref.

Twórcy

autor
  • Department of Plant Protection, Faculty of Agricultural Sciences, University of Guilan, Rasht, Iran
autor
  • Department of Plant Protection, Faculty of Agricultural Sciences, University of Guilan, Rasht, Iran
autor
  • Department of Plant Protection, Faculty of Agricultural Sciences, University of Guilan, Rasht, Iran
autor
  • Department of Plant Protection, College of Agriculture and Natural Resources, University of Tehran, Karaj, Iran

Bibliografia

  • Broadway R.M. 1995. Are insects resistant to plant proteinase inhibitors? Journal of Insect Physiology 41 (2): 107–116. DOI: https://doi.org/10.1016/0022-1910(94)00101-l
  • Broadway R.M., Villani M.G. 1995. Does host range influence susceptibility of herbivorous insects to non-host plant proteinase inhibitors? Entomologia Experimentalis et Applicata 76 (3): 303–312. DOI: https://doi.org/10.1111/j.1570-7458.1995.tb01974.x
  • Klowden M.J. 2007. Physiological Systems in Insects. 2nd ed. Elsevier, New York, 688 pp.
  • Lazarevic J., Jankovic-Tomanic M. 2015. Dietary and phylogenetic correlates of digestive trypsin activity in insect pests. Entomologia Experimentalis et Applicata 157 (2): 123–151. DOI: https://doi.org/10.1111/eea.12349
  • Livak K.J., Schmittgen T.D. 2001. Analysis of relative gene expression data using real time quantitative PCR and 2−DDCt method. Methods 25 (4): 402–408. DOI: https://doi.org/10.1006/meth.2001.1262
  • Lu M., Du X., Cao S.S., Liu P., Li J. 2013. Molecular cloning and characterization of the first caspase in the striped stem borer, Chilo suppressalis. International Journal of Molecular Sciences 14 (5): 10229–10241. DOI: https://doi.org/10.3390/ijms140510229
  • Nation J.L. 2008. Insect Physiology and Biochemistry. 2nd ed. CRC Press, London, 560 pp.
  • Peterson A.M., Barillas-Mury C.V., Wells M.A. 1994. Sequence of three cDNAs encoding an alkaline midgut trypsin from Manduca sexta. Insect Biochemistry and Molecular Biology 24 (5): 463–471. DOI: https://doi.org/10.1016/0965-1748-(94)90041-8
  • Sharifloo A., Zibaee A., Sendi J.J., Talebi Jahroumi K. 2017. Biochemical characterization of a digestive trypsin in the midgut of large cabbage white butterfly, Pieris brassicae L. (Lepidoptera: Pieridae). Bulletin of Entomological Research: 1–9. DOI: https://doi.org/10.1017/s0007485317001067
  • Terra W.R., Ferriera C. 2012. Biochemistry and molecular biology of digestion. Insect Molecular Biology and Biochemistry: 365–418. DOI: https://doi.org/10.1016/B978-0-12-384747-8.10011-X
  • Zhu Y.C., Kramer K.K., Oppert B., Dowdy A.K. 2000. cDNAs of aminopeptidase-like protein genes from Plodia interpunctella strains with different susceptibilities to Bacillus thuringiensis toxins. Insect Biochemistry and Molecular Biology 30 (3): 215–224. DOI: https://doi.org/10.1016/s0965-1748-(99)00118-6

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

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