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

Snake venom L-Amino acid oxidases: trends in pharmacology and biochemistry

Submitted by Claudete Queiroz ([email protected]) on 2016-05-03T18:02:40Z No. of bitstreams: 1 Snake Venom L-Amino Acid Oxidases Trends in - Pharmacology and Biochemistry.pdf: 3419937 bytes, checksum: 77270860cee91bddcc146303c805335c (MD5)Approved for entry into archive by EMERSON LEAL ([email protected]) on 2016-05-17T14:23:25Z (GMT) No. of bitstreams: 1 Snake Venom L-Amino Acid Oxidases Trends in - Pharmacology and Biochemistry.pdf: 3419937 bytes, checksum: 77270860cee91bddcc146303c805335c (MD5)Made available in DSpace on 2016-05-17T14:23:25Z (GMT). No. of bitstreams: 1 Snake Venom L-Amino Acid Oxidases Trends in - Pharmacology and Biochemistry.pdf: 3419937 bytes, checksum: 77270860cee91bddcc146303c805335c (MD5) Previous issue date: 2014Universidade Federal de Uberlândia. Faculdade de Ciências Integradas do Pontal. Departamento de Genética e Bioquímica. Uberlândia, MG, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Universidade Federal de Uberlândia. Faculdade de Ciências Integradas do Pontal. Departamento de Genética e Bioquímica. Uberlândia, MG, Brazil.Universidade de São Paulo. Faculdade de Ciências Farmacêuticas de Ribeirão Preto. Departamento de Análises Clínicas, Toxicológicas e Bromatológicas. Ribeirão Preto, SP, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Universidade Federal de Uberlândia. Faculdade de Ciências Integradas do Pontal. Departamento de Genética e Bioquímica. Uberlândia, 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 à Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.L-amino acid oxidases are enzymes found in several organisms, including venoms of snakes, where they contribute to the toxicity of ophidian envenomation. Their toxicity is primarily due to enzymatic activity, but other mechanisms have been proposed recently which require further investigation. L-amino acid oxidases exert biological and pharmacological effects, including actions on platelet aggregation and the induction of apoptosis, hemorrhage, and cytotoxicity. These proteins present a high biotechnological potential for the development of antimicrobial, antitumor, and antiprotozoan agents. This review provides an overview of the biochemical properties and pharmacological effects of snake venom L-amino acid oxidases, their structure/activity relationship, and supposed mechanisms of action described so far

Evidence-based guidelines: MAGNIMS consensus guidelines on the use of MRI in multiple sclerosis - Clinical implementation in the diagnostic process

The clinical use of MRI in patients with multiple sclerosis (MS) has advanced markedly over the past few years. Technical improvements and continuously emerging data from clinical trials and observational studies have contributed to the enhanced performance of this tool for achieving a prompt diagnosis in patients with MS. The aim of this article is to provide guidelines for the implementation of MRI of the brain and spinal cord in the diagnosis of patients who are suspected of having MS. These guidelines are based on an extensive review of the recent literature, as well as on the personal experience of the members of the MAGNIMS (Magnetic Resonance Imaging in MS) network. We address the indications, timing, coverage, reporting and interpretation of MRI studies in patients with suspected MS. Our recommendations are intended to help radiologists and neurologists standardize and optimize the use of MRI in clinical practice for the diagnosis of MS