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      Proteomic analysis of the venom of the social wasp Apoica pallens (Hymenoptera: Vespidae)

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          Abstract

          ABSTRACT Wasps are a diverse group of insects that possess a sting apparatus associated with a venom gland, which is used for predation and colony defense. The biochemistry of Hymenoptera venom has been evaluated in relation to allergy and immunology, and proteomics has been shown to be a powerful tool for the identification of compounds with pharmacological potential. Data on wasps venom the of genus Apoica are scarce, so the objective of the present work was to identify the venom proteins of the eusocial wasp Apoica pallens, as a first step towards further investigation of applied uses of the venom and its protein constituents. The venom proteins were separated by two-dimensional gel electrophoresis, followed by MALDI-TOF/TOF mass spectrometry. A total of 259 spots were detected, with molecular weights from 4.9 to 141 kDa. Thirty of these proteins were identified and classified into eight functional categories: allergen, enzyme, metabolism, structural, environmental response, proteoglycan, active in DNA and RNA, and unknown function. Due to the few available proteomic data for wasp venom, many proteins could not be identified, which makes studies with proteomic analysis of Hymenoptera venom even more important.

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          Most cited references70

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          Complex cocktails: the evolutionary novelty of venoms.

          Venoms have evolved on numerous occasions throughout the animal kingdom. These 'biochemical weapon systems' typically function to facilitate, or protect the producing animal from, predation. Most venomous animals remain unstudied despite venoms providing model systems for investigating predator-prey interactions, molecular evolution, functional convergence, and novel targets for pharmaceutical discovery. Through advances in 'omic' technologies, venom composition data have recently become available for several venomous lineages, revealing considerable complexity in the processes responsible for generating the genetic and functional diversity observed in many venoms. Here, we review these recent advances and highlight the ecological and evolutionary novelty of venom systems. Copyright © 2012 Elsevier Ltd. All rights reserved.
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            Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha.

            Mammalian tissues express three immunologically distinct peroxiredoxin (Prx) proteins (Prx I, II, and III), which are the products of distinct genes. With the use of recombinant proteins Prx I, II, and III, all have now been shown to possess peroxidase activity and to rely on Trx as a source of reducing equivalents for the reduction of H2O2. Prx I and II are cytosolic proteins, whereas Prx III is localized in mitochondria. Transient overexpression of Prx I or II in cultured cells showed that they were able to eliminate the intracellular H2O2 generated in response to growth factors. Moreover, the activation of nuclear factor kappaB (NFkappaB) induced by extracellularly added H2O2 or tumor necrosis factor-alpha was blocked by overproduction of Prx II. These results suggest that, together with glutathione peroxidase and catalase, Prx enzymes likely play an important role in eliminating peroxides generated during metabolism. In addition, Prx I and II might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentration of H2O2.
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              Transgelin: an actin-binding protein and tumour suppressor.

              Transgelin is a shape change sensitive 22 kDa actin-binding protein of the calponin family. It contains a C-terminal calponin-like module (CLIK(23)) and an upstream positively charged amino acid region required for actin binding. Transgelin is ubiquitous to vascular and visceral smooth muscle and is an early marker of smooth muscle differentiation, where its expression is driven by CArG box, smooth muscle gene promoter. It is also present in fibroblasts, and some epithelium where expression is likely driven by TGF-beta1. Transgelin null mice reveal that, whilst it is not required for smooth muscle development, transgelin may be involved in calcium-independent smooth muscle contraction. Recent evidence suggests that transgelin acts as a tumour suppressor. Its expression is lost in prostate, breast and colon cancers. This is consistent with suppression of the metallo matrix protease-9 (MMP-9) by transgelin, where MMP-9 is upregulated in these common cancers.
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                Author and article information

                Contributors
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Journal
                rbent
                Revista Brasileira de Entomologia
                Rev. Bras. entomol.
                Sociedade Brasileira De Entomologia (São Paulo, SP, Brazil )
                1806-9665
                December 2019
                : 63
                : 4
                : 322-330
                Affiliations
                [2] Dourados Mato Grosso do Sul orgnameUniversidade Estadual de Mato Grosso do Sul orgdiv1Programa de Pós-Graduação em Recursos Naturais Brazil
                [1] Dourados Mato Grosso do Sul orgnameUniversidade Federal da Grande Dourados orgdiv1Programa de Pós-Graduação em Entomologia e Conservação da Biodiversidade Brazil
                [4] Viçosa Minas Gerais orgnameUniversidade Federal de Viçosa orgdiv1Departamento de Biologia Geral Brazil
                [3] Bacabal Maranhão orgnameUniversidade Federal do Maranhão orgdiv1Coordenação de Ciências Naturais Biologia Brazil
                [5] Dourados MS orgnameLaboratório de Ecologia Comportamental - LABECO Brazil
                Article
                S0085-56262019000400322 S0085-5626(19)06300400322
                10.1016/j.rbe.2019.10.001
                000ad913-1fba-4f46-a4cb-1506599d638b

                This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

                History
                : 02 October 2019
                : 05 June 2019
                Page count
                Figures: 0, Tables: 0, Equations: 0, References: 90, Pages: 9
                Product

                SciELO Brazil

                Categories
                Biology, Ecology and Diversity

                Proteins,Mass spectrometry,MALDI-TOF/TOF,Wasps
                Proteins, Mass spectrometry, MALDI-TOF/TOF, Wasps

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