Susceptibilities of UK and mainland European samples of Trialeurodes vaporariorum (Westwood) to the neonicotinoid insecticide imidacloprid were investigated over a 7 year period. All 24 strains collected between 1997 and 2003 showed similar baseline levels of susceptibility to that of a known susceptible laboratory strain when exposed to a diagnostic concentration (128 mg L(-1)) of formulated imidacloprid. Two samples collected during 2004, one from the UK and one from The Netherlands, demonstrated reduced susceptibility at this concentration. Using dose-response assays, the presence of resistant individuals was disclosed in both these strains; some individuals were unaffected at doses high enough to induce phytotoxic effects. This report represents the first confirmed cases of neonicotinoid resistance inducing control failures in T. vaporariorum, and highlights a need for careful vigilance to sustain the effectiveness of imidacloprid and related neonicotinoid insecticides.
Transglutaminase 2 (TG2) is the most widely distributed and most abundantly expressed member of the transglutaminase family of enzymes, a group of intracellular and extracellular proteins that catalyze the Ca2+-dependent posttranslational modification of proteins. It is a unique member of the transglutaminase family owing to its specialized biochemical, structural and functional elements, ubiquitous tissue distribution and subcellular localization, and substrate specificity. The broad substrate specificity of TG2 and its flexible interaction with numerous other gene products may account for its multiple biological functions. In addition to the classic Ca2+-dependent transamidation of proteins, which is a hallmark of transglutaminase enzymes, additional Ca2+-independent enzymatic and nonenzymatic activities of TG2 have been identified. Many such activities have been directly or indirectly implicated in diverse cellular physiological events, including cell growth and differentiation, cell adhesion and morphology, extracellular matrix stabilization, wound healing, cellular development, receptor-mediated endocytosis, apoptosis, and disease pathology. Given the wide range of activities of the transglutaminase gene family it has been suggested that, in the absence of active versions of TG2, its function could be compensated for by other members of the transglutaminase family. It is in the light of this assertion that we review, herein, TG2 activities and the possibilities and premises for compensation for its absence.
In diabetes mellitus the progression of atherosclerosis is accelerated. The interaction of glucose with atherogenic lipoproteins may be relevant to the mechanisms responsible for this vascular damage. The aim of this study was to examine the effect of glucose-modified low density lipoprotein (LDL) on human monocyte chemotaxis and to investigate the roles of oxidation and glycation in the generation of chemotactic LDL. Cu(II)-mediated LDL oxidation was potentiated by glucose in a dose-dependent manner and increased its chemotactic activity. Incubation with glucose alone, under conditions where very little oxidation was observed, also increased the chemotactic property of LDL. Neither diethylenetriamine pentaacetic acid (DETAPAC) nor aminoguanidine, which both inhibited LDL oxidation, completely inhibited the chemotactic activity of glycated oxidised LDL. The results suggest that both oxidation and glycation contribute to increased chemotactic activity.
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