02663nas a2200301 4500008004100000022001400041245023700055210006900292260009500361300001000456490000700466520151000473653001101983653001601994653001702010653001002027653001402037653002002051653002202071653002702093653002402120100001602144700001502160700001702175700002802192700001602220856012502236 2006 eng d a0048-357500aFlufenoxuron, an acylurea insect growth regulator, alters development of Tribolium castaneum (Herbst) (Coleoptera :tenebrionidae) by modulating levels of chitin, soluble protein content, and HSP70 and p34(cdc2) in the larval tissues0 aFlufenoxuron an acylurea insect growth regulator alters developm a525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USAbACADEMIC PRESS INC ELSEVIER SCIENCEcJUN a84-900 v853 a

The effect of sublethal concentrations, 0.00141% (LC20), 0.00251% (LC30), and 0.0036% (LC40) of a dispersible formulation of an acylurea insect growth regulator, flufenoxuron (Cascade) on certain biochemical parameters in the larvae of Tribolium castaneum was investigated. When neonates were fed on diet treated with sublethal concentrations for 24 It, it was observed that at all concentrations tested, there was a significant reduction in chitin content on the 15th day of development. Total soluble protein content at LC20 and LC30 decreased with increasing age of the larvae. At LC20 and LC40 concentrations there was a progressive increase in the protein: chitin ratio as a function of increase in age of the larvae. SDS-PAGE analysis of the larval tissue extracts indicated gross quantitative changes in some of the protein bands (MW 50-97 kDa). Western blot analysis revealed significant increase in the level of HSP70 in the extracts of larvae fed on LC30 treated diet, on the 7th and 10th day of development in the decreasing order. Conversely, a significant decrease in the hyper-phosphorylated form of p34(cdc2) kinase due to flufenoxuron treatment indicating modulation of cell cycle regulation was observed. Thus, sublethal concentrations of flufenoxuron alter expression of developmentally regulated proteins, HSP70 and p34(cdc2) and chitin formation in a stage-specific manner thereby resulting developmental abnormalities in T castaneum. (c) 2005 Elsevier Inc. All rights reserved.

10achitin10aDevelopment10aflufenoxuron10aHSP7010ap34(cdc2)10aphosphotyrosine10asublethal effects10atotal soluble proteins10aTribolium castaneum1 aSalokhe, S.1 aSarkar, A.1 aKulkarni, A.1 aMukherjee, Samindra, N.1 aPal, J., K. uhttp://library.ncl.res.in/content/flufenoxuron-acylurea-insect-growth-regulator-alters-development-tribolium-castaneum-001984nas a2200265 4500008004100000022001400041245006200055210006100117260010600178300001000284490000700294520110800301653001401409653001401423653003201437653001601469653001601485653001701501653002001518100002201538700002201560700002201582700002001604856009401624 2015 eng d a0965-174800aCathepsins of lepidopteran insects: aspects and prospects0 aCathepsins of lepidopteran insects aspects and prospects aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcSEP a51-590 v643 a

Molecular understanding of lepidopteran physiology has revealed that proteases consist of one of the central regulatory/reacting system for insect growth and survival. Among the various proteases, cathepsins are the most crucial cellular proteases, which play vital roles during insect development. In the present review, we have discussed various aspects of the lepidopteran insect cathepsins, emphasizing their roles in processes like development, growth, metamorphosis, apoptosis and immunity. Cathepsins are categorized into different types on the basis of their sequence diversification, leading to variation in structure and catalytic function. Cathepsins exhibit tissue and stage specific expression pattern which is fine-tuned by a delicate balance of expression, compartmentalization, zymogen activation, inhibition by protein inhibitors and degradation. The indispensability of cathepsins as cellular proteases in the above mentioned processes proposes them as novel targets for designing effective and specific insect controlling strategies. (C) 2015 Elsevier Ltd. All rights reserved.

10aApoptosis10aCathepsin10aCysteine/aspartate protease10aDevelopment10aLepidoptera10aPest control10aStress response1 aSaikhedkar, Nidhi1 aSummanwar, Aarohi1 aJoshi, Rakesh, S.1 aGiri, Ashok, P. uhttp://library.ncl.res.in/content/cathepsins-lepidopteran-insects-aspects-and-prospects-001918nas a2200241 4500008004100000022001400041245007400055210006900129260000800198490000700206520118700213653002001400653001901420653001601439653003101455653001201486100001501498700001601513700001801529700001501547700001401562856010001576 2021 eng d a0962-107500aGlycosyltransferases: the multifaceted enzymatic regulator in insects0 aGlycosyltransferases the multifaceted enzymatic regulator in ins cAPR0 v303 a

Glycosyltransferases (GTs) catalyse the reaction of glyco-conjugation of various biomolecules by transferring the saccharide moieties from an activated nucleotide sugar to nucleophilic glycosyl acceptor. In insects, GTs show diverse temporal and site-specific expression patterns and thus play significant roles in forming the complex biomolecular structures that are necessary for insect survival, growth and development. Several insects exhibit GT-mediated detoxification as a key defence strategy against plant allelochemicals and xenobiotic compounds, as well as a mechanism for pesticide cross-resistance. Also, these enzymes act as crucial effectors and modulators in various developmental processes of insects such as eye development, UV shielding, cuticle formation, epithelial development and other specialized functions. Furthermore, many of the known insect GTs have been shown to play a fundamental role in other physiological processes like body pigmentation, cuticular tanning, chemosensation and stress response. This review provides a detailed overview of the multifaceted functionality of insect GTs and summarizes numerous case studies associated with it.

10aAllelochemicals10aDetoxification10aDevelopment10aglycosyltransferases (GTs)10ainsects1 aNagare, M.1 aAyachit, M.1 aAgnihotri, A.1 aSchwab, W.1 aJoshi, R. uhttp://library.ncl.res.in/content/glycosyltransferases-multifaceted-enzymatic-regulator-insects