02159nas a2200241   4500008004100000022001400041245006700055210006700122260010600189300001200295490000700307520131200314653001501626653002001641653002501661653002601686653001101712100002801723700002001751700002401771700002101795856010101816       2005                        eng d  a0965-174800aGene expression patterns of helicoverpa armigera gut proteases0 aGene expression patterns of helicoverpa armigera gut proteases  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcAPR  a355-3670 v353 a<p>Relative quantification of reported gut proteinase cDNAs from Helicoverpa armigera larvae fed on various host plants (cotton, chickpea, pigeonpea, tomato and okra), non-host plant Pis (winged bean, bitter gourd, ground nut, and capsicum) and during larval development has been carried out using semi-quantitative RT-PCR. Five trypsin-like and three chymotrypsin-like proteinases were categorized as insensitive or sensitive to most of the proteinase inhibitors (Pis) and insensitive/sensitive to specific Pis based on their expression analysis. These results were supported by amino acid sequence analysis, where diverged amino acids were observed in the regions, which are reported to be involved in typical trypsin trypsin inhibitor interactions and critical for proteinase inhibitor resistance. Among exopeptidases (five aminopeptidase and three carboxypeptidase), HaAmi4 and HaAmi5 of aminopeptidase and HaCar1 of carboxypeptidase exhibited considerable differential expression. Elastase and cathepsin B-like proteinases were expressed at negligible levels. The proteases identified in the study would be ideal candidates for further interactions studies with protease inhibitors to understand the structural reasons of protease inhibitor insensitivity (c) 2005 Elsevier Ltd. All rights reserved.</p>10aexpression10agut proteinases10aHelicoverpa armigera10aProteinase inhibitors10aRT-PCR1 aChougule, Nanasaheb, P.1 aGiri, Ashok, P.1 aSainani, Mohini, N.1 aGupta, Vidya, S.  uhttps://library.ncl.res.in/content/gene-expression-patterns-helicoverpa-armigera-gut-proteases-002364nas a2200253   4500008004100000022001400041245022000055210006900275260010600344300001400450490000700464520128900471653002301760653002501783653002801808653002301836653001801859653002601877100001801903700002001921700002401941700002101965856012401986       2005                        eng d  a0031-942200aHigher accumulation of proteinase inhibitors in flowers than leaves and fruits as a possible basis for differential feeding preference of Helicoverpa armigera on tomato (Lycopersicon esculentum Mill, Cv. Dhanashree)0 aHigher accumulation of proteinase inhibitors in flowers than lea  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcNOV  a2659-26670 v663 a<p>Tomato (Lycopersicon esculentum, Mill; cultivar- Dhanashree) proteinase inhibitors (Pis) were tested for their trypsin inhibitory (TT) and Helicoverpa armigera gut proteinases inhibitory (HGPI) activity in different organs of the tomato plants. Analysis of TI and HGPI distribution in various parts of the plant showed that flowers accumulated about 300 and 1000 times higher levels of TI while 700 and 400 times higher levels of HGPI as compared to those in leaves and fruits, respectively. Field observation that H. armigera larvae infest leaves and fruits but not the flowers could be at least partially attributed to the protective role-played by the higher levels of Pis in the flower tissue. Tomato Pis inhibited about 50-80% HGP activity of H. armigera larvae feeding on various host plants including tomato, of larvae exposed to non-host plant Pis and of various larval instars. Tomato Pis were found to be highly stable to insect proteinases wherein incubation of inhibitor with HGP even for 3 h at optimum conditions did not affect inhibitory activity. Bioassay using H. armigera larvae fed on artificial diet containing tomato PIs revealed adverse effect on larval growth, pupae development, adult formation and fecundity. (c) 2005 Elsevier Ltd. All rights reserved.</p>10aaccumulation of PI10aHelicoverpa armigera10aLycopersicon esculentum10aMidgut proteinases10aPlant defense10aProteinase inhibitors1 aDamle, M., S.1 aGiri, Ashok, P.1 aSainani, Mohini, N.1 aGupta, Vidya, S.  uhttps://library.ncl.res.in/content/higher-accumulation-proteinase-inhibitors-flowers-leaves-and-fruits-possible-basis-0