RESUMEN
BACKGROUND: A large percentage of Liverpool Somalis have vitamin D deficiency and low calcium excretion. The dietary habits of Liverpool Somalis were investigated with respect to food items containing calcium and vitamin D. METHODS: A questionnaire, administered by a Somali field worker, assessed the intake of food of 60 adult (45 females and 15 males; mean age 42 years) and 10 child (seven females and three males; mean age 10 years) Somali volunteers. Questions concerned personal details, health (bone and muscle problems) and dietary habits including the frequency of consumption of food items containing substantial amounts of calcium and vitamin D. Results Most subjects reported bone and muscle pain. Eating habits reflected traditional customs. Foods containing substantial amounts of calcium and vitamin D were consumed infrequently. Milk was only consumed in tea. Those self-reporting bone pain consumed eggs, cheese and beans rarely. CONCLUSION: The food choices of these individuals with regard to bone health is a cause for concern and indicates a likelihood of low calcium and vitamin D intake.
Asunto(s)
Calcio de la Dieta/administración & dosificación , Calcio/deficiencia , Conducta Alimentaria , Deficiencia de Vitamina D/epidemiología , Vitamina D/administración & dosificación , Adulto , Huesos/metabolismo , Calcio de la Dieta/orina , Niño , Inglaterra/epidemiología , Femenino , Humanos , Masculino , Músculo Esquelético/metabolismo , Dolor/etiología , Factores de Riesgo , Somalia/etnología , Luz Solar , Encuestas y Cuestionarios , Deficiencia de Vitamina D/etiologíaRESUMEN
In Saccharomyces cerevisiae cells, high external osmolarity leads to the activation of a p38-related mitogen-activated protein (MAP) kinase though Pbs2. Pbs2 tagged with green fluorescent protein (Pbs2-GFP) is evenly distributed in the cytoplasm but excluded from the nucleus before and after exposure to stress. Here we show that a catalytically inactive form of Pbs2 attains a highly polarised localization during osmostress. This phenomenon depends of the osmosensor Sho1 and on a functional Cdc42 GTPase. Cdc42, but not the actin cytoskeleton, influences Sho1-dependent activation of the MAP kinase. Sho1 itself accumulates at sites of polar growth, but independently of stress conditions and Cdc42. These observations allow us to define the sequence of events that occurs during propogation of osmostress signals.
Asunto(s)
Proteínas de la Membrana/metabolismo , Quinasas de Proteína Quinasa Activadas por Mitógenos/análisis , Proteínas de Saccharomyces cerevisiae , Saccharomyces cerevisiae/metabolismo , Proteína de Unión al GTP cdc42 de Saccharomyces cerevisiae/metabolismo , Actinas/metabolismo , División Celular , Citoesqueleto/metabolismo , Activación Enzimática , Proteínas Fúngicas/metabolismo , Péptidos y Proteínas de Señalización Intracelular , Quinasas Quinasa Quinasa PAM/metabolismo , Quinasas de Proteína Quinasa Activadas por Mitógenos/genética , Proteínas Quinasas Activadas por Mitógenos/metabolismo , Mutagénesis , Concentración Osmolar , Fosfatos/metabolismo , Proteínas Serina-Treonina Quinasas/metabolismo , Saccharomyces cerevisiae/genética , Transducción de SeñalRESUMEN
Sister chromatid cohesion is established during DNA replication and depends on a multiprotein complex called cohesin. At the onset of anaphase the cohesive structures that hold sisters together must be destroyed to allow segregation of sisters. In the budding yeast Saccharomyces cerevisiae loss of sister chromatid cohesion depends on a separating protein (separin) called Esp1. At the metaphase to anaphase transition, separin is activated by proteolysis of its inhibitory subunit (securin) called Pds1. This process is mediated by the anaphase promoting complex and an accessory protein Cdc20. In meiosis a single round of DNA replication is followed by two successive rounds of segregation. Thus loss of cohesion is spun out over two divisions. By studying the mechanisms that initiate anaphase in meiotic division we show that the yeast securin Pds1p is present in meiotic nuclei and is destroyed at the onset of each meiotic division. We also show that securin destruction depends on Cdc20p which accumulates within nuclei around the time of Pds1p's disappearance.