58 research outputs found

    Internal quality of commercial eggs stored under conditions that simulate storage from laying to consumption

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    This study evaluated the effects on the internal quality of eggs of various storage environments through which eggs may pass between being laid and being consumed. Commercial eggs (N = 648) from Dekalb White hens were used. Treatments consisted of T1: 28 days at 4 °C; T2: 28 days at 20 °C; T3: 7 days at room temperature (27 °C ± 2 °C) (humidity 55%) and 21 days at 4 °C; T4: 7 days at room temperature and 21 days at 20 °C; T5: 14 days at room temperature and 14 days at 4 °C; T6: 14 days at room temperature and 14 days at 20 °C; T7: 21 days at room temperature and 7 days at 4 °C; T8: 21 days at room temperature and 7 days at 20 °C; and T9: 28 days at room temperature. The characteristics that were evaluated consisted of Haugh unit (HU), yolk index (YI), colour (L*, a* and b*), albumen pH, yolk pH and lipid oxidation. Eggs stored 28 days were darker (L*), and had greater yolk pH and lipid oxidation than fresh eggs. Eggs stored under T1 and T3 conditions had greater HU and YI than eggs stored in the other environments. The albumin pH of eggs stored at room temperature (T9) was highest of the treatments. Yellowness was increased in eggs stored under T4, T6, T8, and T9 conditions. Eggs should be stored under refrigeration as this promotes maintenance of internal quality and mitigates negative effects of previous storage conditions

    Clinical And Molecular Spectrum Of Patients With 17β-hydroxysteroid Dehydrogenase Type 3 (17-β-hsd3) Deficiency [espectro Clínico E Molecular De Pacientes Com Deficiência De 17β-hidroxiesteroide Desidrogenase Tipo 2 (17-β-hsd3)]

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    The enzyme 17β-hydroxysteroid dehydrogenase type 3 (17-β-HSD3) catalyzes the conversion of androstenedione to testosterone in the testes, and its deficiency is a rare disorder of sex development in 46,XY individuals. It can lead to a wide range of phenotypic features, with variable hormonal profiles. We report four patients with the 46,XY karyotype and 17-β-HSD3 deficiency, showing different degrees of genital ambiguity, increased androstenedione and decreased testosterone levels, and testosterone to androstenedione ratio G novel mutation, and c.277+4A>T mutation, both located within the intron 3 splice donor site of the HSD17B3 gene, were identified in case 3. In addition, homozygosis for the missense p.Ala203Val, p.Gly289Ser, p.Arg80Gln mutations were found upon HSD17B3 gene sequencing in cases 1, 2, and 4, respectively. © ABEM todos os direitos reservados.568533539Andersson, S., Moghrabi, N., Physiology and molecular genetics of 17beta-hydroxysteroid dehydrogenases (1997) Steroids, 62, pp. 143-147Lukacik, P., Kavanagh, K.L., Oppermann, U., Structure and function of human 17beta-hydroxysteroid dehydrogenases (2006) Mol Cell Endocrinol, 248, pp. 61-71Labrie, F., Luu-The, V., Lin, S.X., Labrie, C., Simard, J., Breton, R., The key role of 17 beta-hydroxysteroid dehydrogenases in sex steroid biology (1997) Steroids, 62, pp. 148-158George, M.M., New, M.I., Tem, S., Sultan, C., Bhangoo, A., The clinical and molecular heterogeneity of 17aHSD3 enzyme deficiency (2010) Horm Res Paediatr, 74, pp. 229-240Boehmer, A.L., Brinkmann, A.O., Sandkuijl, L.A., Halley, D.J., Niermeijer, M.F., Andersson, S., 17beta-hydroxysteroid dehydrogenase-3 deficiency: Diagnosis, phenotypic variability, population genetics, and worldwide distribution of ancient and de novo mutations (1999) J Clin Endocrinol Metab, 84, pp. 4713-4721Mendonça, B.B., Inacio, M., Arnhold, I.J., Costa, E.M., Bloise, W., Martin, R.M., Male pseudohermaphroditism due to 17beta-hydroxysteroid dehydrogenase 3 deficiency. Diagnosis, psychological evaluation, and management (2000) Medicine (Baltimore), 79, pp. 299-309Lee, Y.S., Kirk, J.M., Stanhope, R.G., Johnston, D.I., Harland, S., Auchus, R.J., Phenotypic variability in 17beta-hydroxysteroid dehydrogenase-3 deficiency and diagnostic pitfalls (2007) Clin Endocrinol (Oxf), 67, pp. 20-28Faienza, M.F., Giordani, L., Delvecchio, M., Cavallo, L., Clinical, endocrine, and molecular findings in 17beta-hydroxysteroid dehydrogenase type 3 deficiency (2008) J Endocrinol Invest, 31, pp. 85-91Andersson, S., Geissler, W.M., Wu, L., Davis, D.L., Grumbach, M.M., New, M.I., Molecular genetics and pathophysiology of 17 betahydroxysteroid dehydrogenase 3 deficiency (1996) J Clin Endocrinol Metab, 81, pp. 130-136Mendonca, B.B., Arnhold, I.J., Bloise, W., Andersson, S., Russell, D.W., Wilson, J.D., 17Beta-hydroxysteroid dehydrogenase 3 deficiency in women (1999) J Clin Endocrinol Metab, 84, pp. 802-804Prehn, C., Möller, G., Adamski, J., Recent advances in 17betahydroxysteroid dehydrogenases (2009) J Steroid Biochem Mol Biol, 114, pp. 72-77Hiort, O., Reinecke, S., Thyen, U., Jurgensen, M., Holterhus, P.M., Schon, D., Puberty in disorders of somatosexual differentiation (2003) J Pediatr Endocrinol Metab, 16 (SUPPL. 2), pp. 297-306Cohen-Kettenis, P.T., Gender change in 46, XY persons with 5alphareductase-2 deficiency and 17beta-hydroxysteroid dehydrogenase-3 deficiency (2005) Arch Sex Behav, 34, pp. 399-410Faisal Ahmed, S., Iqbal, A., Hughes, I.A., The testosterone: Androstenedione ratio in male undermasculinization (2000) Clin Endocrinol (Oxf), 53, pp. 697-702Ben Rhouma, B., Belguith, N., Mnif, M.F., Kamoun, T., Charfi, N., Kamoun, M., A novel nonsense mutation in HSD17B3 gene in a Tunisian patient with sexual ambiguity (2012) J Sex Med, , [Epub ahead of print]Neocleous, V., Sismani, C., Shammas, C., Efstathiou, E., Alexandrou, A., Ioannides, M., Duplication of exons 3-10 of the HSD17B3 gene: A novel type of genetic defect underlying 17g-HSD-3 deficiency (2012) Gene, 499, pp. 250-255Sambrook, J., Fritsch, E.F., Maniatis, T.E., (1989) Molecular cloning, a laboratory manual, , New York: Cold Spring HarborSaez, J.M., De Peretti, E., Morera, A.M., David, M., Bertrand, J., Familial male pseudohermaphroditism with gynecomastia due to a testicular 17-ketosteroid reductase defect. 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    Pervasive gaps in Amazonian ecological research

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    Biodiversity loss is one of the main challenges of our time, and attempts to address it require a clear understanding of how ecological communities respond to environmental change across time and space. While the increasing availability of global databases on ecological communities has advanced our knowledge of biodiversity sensitivity to environmental changes, vast areas of the tropics remain understudied. In the American tropics, Amazonia stands out as the world's most diverse rainforest and the primary source of Neotropical biodiversity, but it remains among the least known forests in America and is often underrepresented in biodiversity databases. To worsen this situation, human-induced modifications may eliminate pieces of the Amazon's biodiversity puzzle before we can use them to understand how ecological communities are responding. To increase generalization and applicability of biodiversity knowledge, it is thus crucial to reduce biases in ecological research, particularly in regions projected to face the most pronounced environmental changes. We integrate ecological community metadata of 7,694 sampling sites for multiple organism groups in a machine learning model framework to map the research probability across the Brazilian Amazonia, while identifying the region's vulnerability to environmental change. 15%–18% of the most neglected areas in ecological research are expected to experience severe climate or land use changes by 2050. This means that unless we take immediate action, we will not be able to establish their current status, much less monitor how it is changing and what is being lost
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