02418nas a2200265   4500008004100000022001400041245011200055210006900167260007300236300001200309490000900321520145600330653001901786653001901805653002501824653002201849653002501871100002001896700002801916700002001944700001801964700002401982700002102006856012502027       2005                        eng d  a0304-416500aIn vivo and in vitro effect of capsicum annum proteinase inhibitors on helicoverpa armigera gut proteinases0 aIn vivo and in vitro effect of capsicum annum proteinase inhibit  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcMAR  a156-1670 v17223 a<p>Two proteinase inhibitors (PIs), CapA1 and CapA2, were purified from Capsicum annum Linn. Var. Phule Jyoti leaves and assessed for their in vitro and in vivo activity against Helicoverpa armigera gut proteinases (HGPs). Both the inhibitors exhibited molecular weights of about 12 kDa with inhibitory activity against bovine trypsin and chymotrypsin indicating presence of probable two-inhibitor repeats of PIN II family. CapA1 and CapA2 inhibited 60-80% HGP (azocaseinolytic) activity of fourth instar larvae feeding on various host plants while 45-65% inhibition of HGP activity of various instars (II to VI) larvae reared on artificial diet. The partial purification of HGP isoforms, their characterization with synthetic inhibitors and inhibition by C. annum PIs revealed that most of the trypsin-like activity (68-91%) of HGPs was sensitive to C. annum PIs while 39-85% chymotrypsin-like activity of HGPs was insensitive to these inhibitors. The feeding of C. annum leaf extracts and two purified PIs in various doses to H. armigera larvae for two successive generations through artificial diet demonstrated their potential in inhibiting larval growth and development, delay in pupation period and dramatic reduction in fecundity and fertility. This is the first report-demonstrating efficacy of C. annum PIs against insect gut proteinases as well as larval growth and development of H. armigera. (c) 2004 Elsevier B.V. All rights reserved.</p>10aCapsicum annum10agut proteinase10aHelicoverpa armigera10ainsect resistance10aProteinase inhibitor1 aTamhane, V., A.1 aChougule, Nanasaheb, P.1 aGiri, Ashok, P.1 aDixit, A., R.1 aSainani, Mohini, N.1 aGupta, Vidya, S.  uhttps://library.ncl.res.in/content/vivo-and-vitro-effect-capsicum-annum-proteinase-inhibitors-helicoverpa-armigera-gut-002009nas a2200253   4500008004100000022001400041245007800055210006900133260006700202300001200269490000700281520116500288653001501453653001701468653002501485653001401510653001201524100002401536700002001560700002201580700002101602700002001623856011201643       2013                        eng d  a0962-107500aDifferential protease activity augments polyphagy in helicoverpa armigera0 aDifferential protease activity augments polyphagy in helicoverpa  a111 RIVER ST, HOBOKEN 07030-5774, NJ USAbWILEY-BLACKWELLcJUN  a258-2720 v223 a<p>Helicoverpa armigera (Lepidoptera: Noctuidae) and other polyphagous agricultural pests are extending their plant host range and emerging as serious agents in restraining crop productivity. Dynamic regulation, coupled with a diversity of digestive and detoxifying enzymes, play a crucial role in the adaptation of polyphagous insects. To investigate the functional intricacy of serine proteases in the development and polyphagy of H.armigera, we profiled the expression of eight trypsin-like and four chymotrypsin-like phylogenetically diverse mRNAs from different life stages of H.armigera reared on nutritionally distinct host plants. These analyses revealed diet- and stage-specific protease expression patterns. The trypsins expressed showed structural variations, which might result in differential substrate specificity and interaction with inhibitors. Protease profiles in the presence of inhibitors and their mass spectrometric analyses revealed insight into their differential activity. These findings emphasize the differential expression of serine proteases and their consequences for digestive physiology in promoting polyphagy in H.armigera.</p>10aadaptation10achymotrypsin10aHelicoverpa armigera10apolyphagy10aTrypsin1 aChikate, Yojana, R.1 aTamhane, V., A.1 aJoshi, Rakesh, S.1 aGupta, Vidya, S.1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/differential-protease-activity-augments-polyphagy-helicoverpa-armigera-0