Body dissatisfaction and disordered eating among Portuguese and Spanish adolescents: The role of individual characteristics and internalisation of sociocultural ideals

The aim of this study was to explore the differences in patterns of risk factors for body dissatisfaction and disordered eating attitudes in both female and male adolescents from Portugal and Spain. The sample included 455 adolescents aged 12-16 years (M = 13.28, SD = 0.65) from two urban areas of each country. Body mass index, self-reported selfesteem, perfectionism, internalisation of sociocultural ideals, body dissatisfaction and disordered eating attitudes were assessed. Path analyses provided partial support for a cross-cultural model of body dissatisfaction and disordered eating in Western countries due to the presence of certain differences in the patterns of relationships across sex and country. The findings suggest the importance not only of identifying cultural specificities, even in “neighbouring” countries, but also of developing a global and comprehensive preventive approach that focuses on the influence of the ideal of beauty transmitted by Western societies

Snake Venom L-Amino Acid Oxidases: Some Consideration About their Functional Characterization

Snake Venom L-amino acid oxidases (LAAOs E.C. 1.4.3.2) are flavoenzymes broadly found in various snake venom compositions. LAAOs have become an attractive subject for molecular biology, biochemistry, physiology and medicine due to their actions on various cells and biological effects on platelets, apoptosis, hemorrhage and others. In this review we try to summarize some of these reports, with special emphasis on apoptosis, anti-protozoa, bactericidal and anti-viral activities.CNPqFINEPFAPESP, Brazi

ESI-MS/MS Identification of a Bradykinin-Potentiating Peptide from Amazon Bothrops atrox Snake Venom Using a Hybrid Qq-oaTOF Mass Spectrometer

Submitted by EMERSON LEAL ([email protected]) on 2016-07-05T14:51:42Z No. of bitstreams: 1 ESI-MS MS Identification of a Bradykinin.pdf: 322142 bytes, checksum: 5b32610ed4596f572c944fea47014170 (MD5)Approved for entry into archive by EMERSON LEAL ([email protected]) on 2016-07-14T15:26:16Z (GMT) No. of bitstreams: 1 ESI-MS MS Identification of a Bradykinin.pdf: 322142 bytes, checksum: 5b32610ed4596f572c944fea47014170 (MD5)Made available in DSpace on 2016-07-14T15:26:16Z (GMT). No. of bitstreams: 1 ESI-MS MS Identification of a Bradykinin.pdf: 322142 bytes, checksum: 5b32610ed4596f572c944fea47014170 (MD5) Previous issue date: 2013Made available in DSpace on 2016-07-15T18:40:38Z (GMT). No. of bitstreams: 3 ESI-MS MS Identification of a Bradykinin.pdf.txt: 21633 bytes, checksum: 54e00469ca67e58fb4b3385fb3bd3091 (MD5) ESI-MS MS Identification of a Bradykinin.pdf: 322142 bytes, checksum: 5b32610ed4596f572c944fea47014170 (MD5) license.txt: 2991 bytes, checksum: 5a560609d32a3863062d77ff32785d58 (MD5) Previous issue date: 2013Fundação Oswaldo Cruz. Fiocruz Rondônia. Center of Biomolecules Study Applied to Health. Porto Velho, RO, Brasil.Fundação Oswaldo Cruz. Fiocruz Rondônia. Center of Biomolecules Study Applied to Health. Porto Velho, RO, Brasil.Waters Corporation. MS Applications Development Laboratory. Alphaville, SP, Brasil.Fundação Oswaldo Cruz. Fiocruz Rondônia. Center of Biomolecules Study Applied to Health. Porto Velho, RO, Brasil.Fundação Oswaldo Cruz. Fiocruz Rondônia. Center of Biomolecules Study Applied to Health. Porto Velho, RO, Brasil.Fundação Oswaldo Cruz. Fiocruz Rondônia. Center of Biomolecules Study Applied to Health. Porto Velho, RO, Brasil.Fundação Oswaldo Cruz. Fiocruz Rondônia. Center of Biomolecules Study Applied to Health. Porto Velho, RO, Brasil / Federal University of Rondônia. Medicine Department. Porto Velho, RO, Brasil.Fundação Oswaldo Cruz. Fiocruz Rondônia. Center of Biomolecules Study Applied to Health. Porto Velho, RO, Brasil.Fundação Oswaldo Cruz. Fiocruz Rondônia. Center of Biomolecules Study Applied to Health. Porto Velho, RO, Brasil / Federal University of Rondônia. Medicine Department. Porto Velho, RO, Brasil.Fundação Oswaldo Cruz. Fiocruz Rondônia. Center of Biomolecules Study Applied to Health. Porto Velho, RO, Brasil. / Federal University of Rondônia. Medicine Department. Porto Velho, RO, Brasil.A bradykinin-potentiating peptide (BPP) from Amazon Bothrops atrox venom with m/z 1384.7386 was identified and characterized by collision induced dissociation (CID) using an ESI-MS/MS spectra obtained in positive ion mode on a hybrid Qq-oaTOF mass spectrometer, Xevo G2 QTof MS (Waters, Manchester, UK). De novo peptide sequence analysis of the CID fragmentation spectra showed the amino acid sequence ZKWPRPGPEIPP, with a pyroglutamic acid and theoretical monoisotopic m/z 1384.7378, which is similar to experimental data, showing a mass accuracy of 0.6 ppm. The peptide is homologous to other BPP from Bothrops moojeni and was named as BPP-BAX12

Armoede en doelmatigheid van de sociale zekerheid in Europa

Abstract Background Wasp venoms constitute a molecular reservoir of new pharmacological substances such as peptides and proteins, biological property holders, many of which are yet to be identified. Exploring these sources may lead to the discovery of molecules hitherto unknown. This study describes, for the first time in hymenopteran venoms, the identification of an enzymatically inactive phospholipase A2 (PLA2) from the venom of the social wasp Polybia occidentalis. Methods P. occidentalis venom was fractioned by molecular exclusion and reverse phase chromatography. For the biochemical characterization of the protein, 1D and 2D SDS-PAGE were performed, along with phospholipase activity assays on synthetic substrates, MALDI-TOF mass spectrometry and sequencing by Edman degradation. Results The protein, called PocTX, was isolated using two chromatographic steps. Based on the phospholipase activity assay, electrophoresis and mass spectrometry, the protein presented a high degree of purity, with a mass of 13,896.47 Da and a basic pI. After sequencing by the Edman degradation method, it was found that the protein showed a high identity with snake venom PLA2 homologues. Conclusion This is the first report of an enzymatically inactive PLA2 isolated from wasp venom, similar to snake PLA2 homologues

Biochemical and functional characterization of parawixia bistriata spider venom with potential proteolytic and larvicidal activities

Submitted by Claudete Queiroz ([email protected]) on 2016-05-03T17:35:46Z No. of bitstreams: 1 Biochemical and Functional Characterization of Parawixia bistriata Spider Venom with Potential Proteolytic and Larvicidal Activities.pdf: 2345310 bytes, checksum: 7b597bf6e451a2c576d5aa2c50136e25 (MD5)Approved for entry into archive by EMERSON LEAL ([email protected]) on 2016-05-16T21:12:26Z (GMT) No. of bitstreams: 1 Biochemical and Functional Characterization of Parawixia bistriata Spider Venom with Potential Proteolytic and Larvicidal Activities.pdf: 2345310 bytes, checksum: 7b597bf6e451a2c576d5aa2c50136e25 (MD5)Made available in DSpace on 2016-05-16T21:12:26Z (GMT). No. of bitstreams: 1 Biochemical and Functional Characterization of Parawixia bistriata Spider Venom with Potential Proteolytic and Larvicidal Activities.pdf: 2345310 bytes, checksum: 7b597bf6e451a2c576d5aa2c50136e25 (MD5) Previous issue date: 2014Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Departamento de Biologia. Laboratório de Entomologia Médica. Laboratório de Bioecologia de Insetos. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Departamento de Biologia. Laboratório de Entomologia Médica. Laboratório de Bioecologia de Insetos. Porto Velho, RO, Brazil.Universidades Federal de Lavras. Departamento de Química. Lavras, MG, Brazil.Universidade Federal de São João del Rei. Departamento de Química, Biotecnologia e Engenharia de Bioprocessos. Ouro Branco, MG, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Toxins purified from the venom of spiders have high potential to be studied pharmacologically and biochemically. These biomolecules may have biotechnological and therapeutic applications. This study aimed to evaluate the protein content of Parawixia bistriata venom and functionally characterize its proteins that have potential for biotechnological applications. The crude venom showed no phospholipase, hemorrhagic, or anti-Leishmania activities attesting to low genotoxicity and discrete antifungal activity for C. albicans. However the following activities were observed: anticoagulation, edema, myotoxicity and proteolysis on casein, azo-collagen, and fibrinogen. The chromatographic and electrophoretic profiles of the proteins revealed a predominance of acidic, neutral, and polar proteins, highlighting the presence of proteins with high molecular masses. Five fractions were collected using cation exchange chromatography, with the P4 fraction standing out as that of the highest purity. All fractions showed proteolytic activity. The crude venom and fractions P1, P2, and P3 showed larvicidal effects on A. aegypti. Fraction P4 showed the presence of a possible metalloprotease (60 kDa) that has high proteolytic activity on azo-collagen and was inhibited by EDTA. The results presented in this study demonstrate the presence of proteins in the venom of P. bistriata with potential for biotechnological applications

Activation of J77A.1 macrophages by three phospholipases A2 isolated from bothrops atrox snake venom

Submitted by Claudete Queiroz ([email protected]) on 2016-05-03T17:00:14Z No. of bitstreams: 1 Activation of J77A.1 Macrophages by Three Phospholipases A2 Isolated from Bothrops atrox Snake Venom.pdf: 2090853 bytes, checksum: 0669d064c65a39c61c661542c067ee9b (MD5)Approved for entry into archive by EMERSON LEAL ([email protected]) on 2016-05-10T14:32:57Z (GMT) No. of bitstreams: 1 Activation of J77A.1 Macrophages by Three Phospholipases A2 Isolated from Bothrops atrox Snake Venom.pdf: 2090853 bytes, checksum: 0669d064c65a39c61c661542c067ee9b (MD5)Made available in DSpace on 2016-05-10T14:32:57Z (GMT). No. of bitstreams: 1 Activation of J77A.1 Macrophages by Three Phospholipases A2 Isolated from Bothrops atrox Snake Venom.pdf: 2090853 bytes, checksum: 0669d064c65a39c61c661542c067ee9b (MD5) Previous issue date: 2014Fundação Oswaldo Cruz. Laboratório de Imunofarmacologia Aplicada à Saúde. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Laboratório de Imunofarmacologia Aplicada à Saúde. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Laboratório de Imunofarmacologia Aplicada à Saúde. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Laboratório de Imunofarmacologia Aplicada à Saúde. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Laboratório de Imunofarmacologia Aplicada à Saúde. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Laboratório de Imunofarmacologia Aplicada à Saúde. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Laboratório de Imunofarmacologia Aplicada à Saúde. Porto Velho, RO, Brazil. / Fundação Oswaldo Cruz. Centro de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Laboratório de Imunofarmacologia Aplicada à Saúde. Porto Velho, RO, Brazil. / Fundação Oswaldo Cruz. Centro de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.In the present study, we investigated the in vitro effects of two basic myotoxic phospholipases A2 (PLA2), BaTX-I, a catalytically inactive Lys-49 variant, and BaTX-II, a catalytically active Asp-49, and of one acidic myotoxic PLA2, BaPLA2, a catalytically active Asp-49, isolated from Bothrops atrox snake venom, on the activation of J774A.1 macrophages. At noncytotoxic concentrations, the toxins did not affect the adhesion of the macrophages, nor their ability to detach. The data obtained showed that only BaTXI stimulated complement receptor-mediated phagocytosis. However, BaTX-I, BaTX-II, and BaPLA2 induced the release of the superoxide anion by J774A.1 macrophages. Additionally, only BaTX-I raised the lysosomal volume of macrophages after 15 min of incubation. After 30 min, all the phospholipases increased this parameter, which was not observed within 60 min. Moreover, BaTX-I, BaTX-II, and BaPLA2 increased the number of lipid bodies on macrophages submitted to phagocytosis and not submitted to phagocytosis. However, BaTX-II and BaPLA2 induced the release of TNF- by J774A.1 macrophages. Taken together, the data show that, despite differences in enzymatic activity, the three toxins induced inflammatory events and whether the enzyme is acidic or basic does not seem to contribute to these effects

Molecular cloning and structural modelling of gamma-phospholipase A2 inhibitors from Bothrops atrox and Micrurus lemniscatus snakes

O artigo encontra-se disponível para download no site do Editor.Submitted by EMERSON LEAL ([email protected]) on 2019-06-10T20:24:46Z No. of bitstreams: 1 Molecular cloning and structural modelling of gamma-phospholipase A2 inhibitors from Bothrops atrox and Micrurus lemniscatus snakes.pdf: 1752222 bytes, checksum: 310894a14a1b6c8b7285e668e031e864 (MD5)Approved for entry into archive by EMERSON LEAL ([email protected]) on 2019-06-11T19:58:11Z (GMT) No. of bitstreams: 1 Molecular cloning and structural modelling of gamma-phospholipase A2 inhibitors from Bothrops atrox and Micrurus lemniscatus snakes.pdf: 1752222 bytes, checksum: 310894a14a1b6c8b7285e668e031e864 (MD5)Made available in DSpace on 2019-06-11T19:58:11Z (GMT). No. of bitstreams: 1 Molecular cloning and structural modelling of gamma-phospholipase A2 inhibitors from Bothrops atrox and Micrurus lemniscatus snakes.pdf: 1752222 bytes, checksum: 310894a14a1b6c8b7285e668e031e864 (MD5) Previous issue date: 2017Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Porto Velho, RO, Brasil / Universidade Federal de Rondônia. Departamento de Medicina. Porto Velho, RO, Brasil.Universidade Estadual Paulista. Instituto de Biociências. Departamento de Física e Biofísica. Botucatu, SP, Brasil.Universidade Estadual Paulista. Instituto de Biociências. Departamento de Física e Biofísica. Botucatu, SP, Brasil.Universidade Estadual Paulista. Instituto de Biociências. Departamento de Física e Biofísica. Botucatu, SP, Brasil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Porto Velho, RO, Brasil / Universidade Federal de Rondônia. Departamento de Medicina. Porto Velho, RO, Brasil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Porto Velho, RO, Brasil / Universidade Federal de Rondônia. Departamento de Medicina. Porto Velho, RO, Brasil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Porto Velho, RO, Brasil / Universidade Federal de Rondônia. Departamento de Medicina. Porto Velho, RO, Brasil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Porto Velho, RO, Brasil / Universidade Federal de Rondônia. Departamento de Medicina. Porto Velho, RO, Brasil / Virginia Commonwealth University. Center for the Study of Biological Complexity, Life Sciences. Richmond, USA.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Porto Velho, RO, Brasil / Universidade Federal de Rondônia. Departamento de Medicina. Porto Velho, RO, Brasil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Porto Velho, RO, Brasil / Universidade Federal de Rondônia. Departamento de Medicina. Porto Velho, RO, Brasil.Universidade Estadual Paulista. Instituto de Biociências. Departamento de Física e Biofísica. Botucatu, SP, Brasil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Porto Velho, RO, Brasil / Universidade Federal de Rondônia. Departamento de Medicina. Porto Velho, RO, Brasil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas a Saúde. Porto Velho, RO, Brasil / Universidade Federal de Rondônia. Departamento de Medicina. Porto Velho, RO, Brasil. / Centro Universitário São Lucas. Porto Velho, RO, Brasil.Phospholipases A2 inhibitors (PLIs) produced by venomous and non-venomous snakαes play essential role in this resistance. These endogenous inhibitors may be classified by their fold in PLIα, PLIβ and PLIγ. Phospholipases A2 (PLA2s) develop myonecrosis in snake envenomation, a consequence that is not efficiently neutralized by antivenom treatment. This work aimed to identify and characterize two PLIs from Amazonian snake species, Bothrops atrox and Micrurus lemniscatus. Liver tissues RNA of specimens from each species were isolated and amplified by RT-PCR using PCR primers based on known PLIγ gene sequences, followed by cloning and sequencing of amplified fragments. Sequence similarity studies showed elevated identity with inhibitor PLIγ gene sequences from other snake species. Molecular models of translated inhibitors’ gene sequences resemble canonical three finger fold from PLIγ and support the hypothesis that the decapeptide (residues 107–116) may be responsible for PLA2 inhibition. Structural studies and action mechanism of these PLIs may provide necessary information to evaluate their potential as antivenom or as complement of the current ophidian accident treatment