42 research outputs found

    Feelings and Perceptions of Women in the Pregnancy-Puerperal Cycle Who Survived Severe Maternal Morbidity

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    This study aimed to understand severe maternal morbidity from the perspective of women who experienced it. The methodological precepts of qualitative research were adopted and the Collective Subject Discourse was the methodological framework chosen. A total of 16 women who experienced severe maternal morbidity were interviewed. Results were discussed based on four themes: describing the desire and plan for having a child; acknowledging the health problem and its influence on pregnancy and on the conceptus; overcoming the initial shock postpartum, and experiencing the risk situation: desires, frustration, and overcoming. This study will contribute to qualifying nursing care, specifically acknowledging the diversity and breadth of the needs presented by women in situations of severe morbidity during the pregnancy-puerperal cycle.Se tuvo por objetivo comprender la experiencia relativa a morbosidad materna grave, a partir de un grupo de mujeres que experimentó ese problema. Se adoptaron los preceptos metodológicos de la investigación cualitativa, siendo el Discurso del Sujeto Colectivo el referencial metodológico. Fueron entrevistadas 16 mujeres que experimentaron morbosidad materna grave. Los resultados fueron discutidos a partir de cuatro temas: describiendo el deseo y la planificación para tener un hijo; percibiendo su problema de salud, su influencia en la gestación y en el concepto; pasando por el choque inicial del post-parto; y, experimentando la situación de riesgo: deseos, frustraciones y superación. Se espera que este trabajo pueda contribuir para calificar la asistencia de enfermería, especialmente reconocer la diversidad y amplitud de las necesidades que las mujeres presentan en situaciones de morbosidad grave durante el ciclo de embarazo y puerperio.Objetivou-se compreender a experiência relativa à morbidade materna grave, a partir de um grupo de mulheres que vivenciou esse problema. Adotaram-se os preceitos metodológicos da pesquisa qualitativa, sendo o Discurso do Sujeito Coletivo o referencial metodológico. Foram entrevistadas 16 mulheres que vivenciaram a morbidade materna grave. Os resultados foram discutidos a partir de quatro temas: descrevendo o desejo e o planejamento para ter um filho, percebendo seu problema de saúde, sua influência na gestação e para o concepto, passando pelo choque inicial no pós-parto e experienciando a situação de risco: desejos, frustrações e superação. Espera-se que este trabalho possa contribuir para qualificar a assistência de enfermagem, especialmente para reconhecer a diversidade e amplitude de necessidades que mulheres apresentam em situações de morbidade grave, durante o ciclo gravídico puerperal

    Discovery of Nuclear-Encoded Genes for the Neurotoxin Saxitoxin in Dinoflagellates

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    Saxitoxin is a potent neurotoxin that occurs in aquatic environments worldwide. Ingestion of vector species can lead to paralytic shellfish poisoning, a severe human illness that may lead to paralysis and death. In freshwaters, the toxin is produced by prokaryotic cyanobacteria; in marine waters, it is associated with eukaryotic dinoflagellates. However, several studies suggest that saxitoxin is not produced by dinoflagellates themselves, but by co-cultured bacteria. Here, we show that genes required for saxitoxin synthesis are encoded in the nuclear genomes of dinoflagellates. We sequenced >1.2×106 mRNA transcripts from the two saxitoxin-producing dinoflagellate strains Alexandrium fundyense CCMP1719 and A. minutum CCMP113 using high-throughput sequencing technology. In addition, we used in silico transcriptome analyses, RACE, qPCR and conventional PCR coupled with Sanger sequencing. These approaches successfully identified genes required for saxitoxin-synthesis in the two transcriptomes. We focused on sxtA, the unique starting gene of saxitoxin synthesis, and show that the dinoflagellate transcripts of sxtA have the same domain structure as the cyanobacterial sxtA genes. But, in contrast to the bacterial homologs, the dinoflagellate transcripts are monocistronic, have a higher GC content, occur in multiple copies, contain typical dinoflagellate spliced-leader sequences and eukaryotic polyA-tails. Further, we investigated 28 saxitoxin-producing and non-producing dinoflagellate strains from six different genera for the presence of genomic sxtA homologs. Our results show very good agreement between the presence of sxtA and saxitoxin-synthesis, except in three strains of A. tamarense, for which we amplified sxtA, but did not detect the toxin. Our work opens for possibilities to develop molecular tools to detect saxitoxin-producing dinoflagellates in the environment

    Characterization of Bothrops jararaca coagulation inhibitor (BjI) and presence of similar protein in plasma of other animals

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    BjI, a protein isolated from Bothrops jararaca snake blood, inhibits the coagulant activity of thrombin. This protein presents two bands of 109 and 138 kDa by SDS-PAGE under reducing conditions. in order to verify the presence of BjI-like proteins in plasma of other animals (reptiles and non-reptiles), we raised a specific polyclonal antibody in mice to it, and we verified immunological cross-reaction by western blotting, considering as positive reactions the development of bands with either 109 or 138 kDa. Similar proteins were identified in Bothrops neuwiedi and Crotalus durissus terrificus snakes. in contrast, no BjI-like protein in other classes of animals was noticeable, nor in other snakes tested. Interestingly, a prolonged thrombin time was found only in snake plasmas that showed similar BjI proteins. BjI bound to two proteins of B. jararaca venom, identified by western blotting. the N-terminal of the B. jararaca venom proteins showed similarity with thrombin-like proteins isolated from other snake venoms. in conclusion, there are similar proteins to BjI in plasmas of B. neuwiedi and Crotalus durissus terrificus, and these proteins also prolong thrombin time. Moreover, these results evidence the presence of target enzymes in snake venom for plasma BjI. (C) 2004 Elsevier B.V. All rights reserved.Inst Butantan, Lab Fisiopatol, BR-05503900 São Paulo, BrazilUNIFESP, Dept Bioquim, São Paulo, BrazilUNIFESP, Dept Bioquim, São Paulo, BrazilWeb of Scienc

    Simultaneous isolation of platelet factor 4 and glycoprotein IIb-IIIa complex from rabbit platelets, and characterization of specific chicken antibodies to assay them

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    Rabbits are frequently used as models for studying coagulation and platelet disorders. However, few reports on literature have dealt with the purification and characterization of rabbit platelet proteins. Herein a protocol for the simultaneous purification of rabbit platelet factor 4 (PF4) and platelet glycoprotein IIb-IIIa (GPIIb-IIIa, integrin alpha(IIb)beta(3)) is described. Specific antibodies were raised in laying chicken, which were used for assaying PF4 by ELISA, and GPIIb-IIIa by direct immunofluorescence and flow cytometry. Furthermore, the binding of monoclonal antibodies specific for GPIIb-IIIa complex (P2), ligand-induced binding site of GPIIIa (LIBS1) and rabbit P-selectin (12A7), as well as of polyclonal IgY specific for rabbit GPIIb-IIIa, was compared in quiescent and thrombin-activated platelets. Polyclonal anti-rabbit PF4 IgY was a specific and sensitive probe that could be used for assaying PF4 in plasma samples. GPIIb-IIIa expression was increased in thrombin-activated platelets, as evaluated by flow cytometric analysis using P2 and polyclonal antibodies raised in chickens. Rabbit GPIIb-IIIa also exhibited a conformational modification that caused the appearance of ligand-induced binding sites. Increased P-selectin expression, used as a positive control, was also noticeable in thrombin-activated platelets. These data evidence that antibodies raised in laying chickens specific to rabbit PF4 and GPIIb-IIIa, as well as certain monoclonal antibodies specific for human GPIIb-IIIa, may be used for investigating rabbit platelet physiology. (C) 2003 Elsevier B.V. All rights reserved.Inst Butantan, Lab Pathophysiol, BR-05503900 São Paulo, SP, BrazilInst Butantan, Immunopathol Lab, BR-05503900 São Paulo, SP, BrazilPro Sangue Fdn, Hemoctr, Lab Thrombo Hemorrhag Dis, São Paulo, BrazilUniversidade Federal de São Paulo, Dept Biochem, São Paulo, SP, BrazilUniversidade Federal de São Paulo, Dept Biophys, São Paulo, SP, BrazilUniversidade Federal de São Paulo, Dept Biochem, São Paulo, SP, BrazilUniversidade Federal de São Paulo, Dept Biophys, São Paulo, SP, BrazilWeb of Scienc
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