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INTRODUCTION AND HYPOTHESIS: The objective was to perform a systematic review of the literature to examine original research on the role of diet in fecal incontinence (FI) with a dual focus on dietary differences in FI and dietary treatments for FI. METHODS: We searched the PubMed and Embase databases for any peer-reviewed original research in English on the role of diet in FI. RESULTS: We identified 172 unique citations. After title review and exclusion of articles not reporting original research, 9 publications were included in the final review: 4 focused on dietary differences and 5 focused on dietary treatments for FI. Limited evidence indicates that macro- and micronutrient intake does not differ significantly in those with and without FI. However, certain foods were perceived to improve or exacerbate FI symptoms and these varied and were adjusted as part of self-care practices. A high-fiber diet may reduce incontinence frequency. CONCLUSIONS: Data on the pathogenesis of FI from a dietary perspective are scant. Based on the limited data, dietary differences between those with and without FI provide little insight with the exception of fiber. Further studies are needed to elucidate treatments for FI using fiber and dietary modifications.
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Dieta/efectos adversos , Incontinencia Fecal/dietoterapia , Incontinencia Fecal/etiología , HumanosRESUMEN
AIM: To determine the association between self-reported adherence to anticholinergic medication and clinical outcomes in women with overactive bladder (OAB). METHODS: A prospective study of women with OAB treated with fesoterodine for 8 weeks. Adherence to medication was measured using the Medication Adherence Self-report Inventory (MASRI). A self reported adherence rate of ≥80% was considered adherent. The association between self-reported adherence and clinical outcomes (Global Index of Improvement, Global impression of Severity, urinary symptom and quality of life scores) was examined. We hypothesized that adherent women would have greater improvement in urinary symptoms and quality of life than non-adherent women. RESULTS: Based on the MASRI, 115 (62.5%) women were adherent and 69 (37.5%) were non-adherent to anticholinergic medication at 8weeks. Adherent women were more likely to report overall improvement in their symptoms compared to non-adherent women (84% vs. 24%, P < 0.001). Significantly more non-adherent women described their bladder symptoms as "moderate" or "severe" at 8 weeks compared to adherent women (74% vs. 44%, P = 0.03). At 8 weeks, adherent women reported significantly greater improvement (change) in urinary symptoms from baseline to 8 weeks than non-adherent women (-13.3 ± 25.8 vs. 2.5 ± 14.4, P = 0.04). Similarly, adherent women reported greater improvement in quality of life scores than non-adherent women (- 7.9 ± 24.0 vs. -1.8 ± 11.9, P = 0.003). CONCLUSION: Self-reported non-adherence, as measured by the MASRI, is associated with clinically meaningful outcomes in women with OAB. This further validates the MASRI as a clinically useful tool for measuring adherence to anticholinergic medications in women with OAB. Neurourol. Urodynam. 35:738-742, 2016. © 2015 Wiley Periodicals, Inc.
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Compuestos de Bencidrilo/uso terapéutico , Cumplimiento de la Medicación , Antagonistas Muscarínicos/uso terapéutico , Vejiga Urinaria Hiperactiva/tratamiento farmacológico , Agentes Urológicos/uso terapéutico , Anciano , Femenino , Humanos , Persona de Mediana Edad , Calidad de Vida , Autoinforme , Resultado del TratamientoRESUMEN
Protein arginylation is an emerging post-translational modification that targets a number of metabolic enzymes; however, the mechanisms and downstream effects of this modification are unknown. Here we show that lack of arginylation renders cells vulnerable to purine nucleotide synthesis inhibitors and affects the related glycine and serine biosynthesis pathways. We show that the purine nucleotide biosynthesis enzyme PRPS2 is selectively arginylated, unlike its close homologue PRPS1, and that arginylation of PRPS2 directly facilitates its biological activity. Moreover, selective arginylation of PRPS2 but not PRPS1 is regulated through a coding sequence-dependent mechanism that combines elements of mRNA secondary structure with lysine residues encoded near the N-terminus of PRPS1. This mechanism promotes arginylation-specific degradation of PRPS1 and selective retention of arginylated PRPS2 in vivo. We therefore demonstrate that arginylation affects both the activity and stability of a major metabolic enzyme.
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Aminoaciltransferasas/genética , Arginina/metabolismo , Nucleótidos de Purina/biosíntesis , ARN Mensajero/metabolismo , Ribosa-Fosfato Pirofosfoquinasa/metabolismo , Aminoaciltransferasas/metabolismo , Animales , Western Blotting , Línea Celular , Glicina/biosíntesis , Células HEK293 , Humanos , Lisina/metabolismo , Ratones , Ratones Noqueados , Estructura Molecular , Procesamiento Proteico-Postraduccional , Reacción en Cadena de la Polimerasa de Transcriptasa Inversa , Serina/biosíntesis , UbiquitinaciónRESUMEN
Polycomb Group (PcG) proteins are crucial for epigenetic inheritance of cell identity and are functionally conserved from Drosophila to humans. PcG proteins regulate expression of homeotic genes and are essential for axial body patterning during development. Earlier we showed that transcription factor YY1 functions as a PcG protein. YY1 also physically interacts with YAF2, a homolog of RYBP. Here we characterize the mechanism and physiologic relevance of this interaction. We found phenotypic and biochemical correction of dRYBP mutant flies by mouse YAF2 demonstrating functional conservation across species. Further biochemical analysis revealed that YAF2 bridges interaction between YY1 and the PRC1 complex. ChIP assays in HeLa cells showed that YAF2 is responsible for PcG recruitment to DNA, which is mediated by YY1 DNA binding. Knock-down of YY1 abrogated PcG recruitment, which was not compensated by exogenous YAF2 demonstrating that YY1 DNA binding is a priori necessary for Polycomb assembly on chromatin. Finally, we found that although YAF2 and RYBP regulate a similar number of Polycomb target genes, there are very few genes that are regulated by both implying functional distinction between the two proteins. We present a model of YAF2-dependent and independent PcG DNA recruitment by YY1.
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Silenciador del Gen , Proteínas Musculares/metabolismo , Complejo Represivo Polycomb 1/metabolismo , Proteínas Represoras/metabolismo , Factor de Transcripción YY1/metabolismo , Animales , Cromatina/metabolismo , ADN/metabolismo , Drosophila/genética , Proteínas de Drosophila/genética , Proteínas de Drosophila/metabolismo , Células HEK293 , Células HeLa , Humanos , Ratones , Proteínas Musculares/química , Proteínas Musculares/fisiología , Mutación , Fenotipo , Dominios y Motivos de Interacción de Proteínas , Proteínas Represoras/química , Proteínas Represoras/genética , Proteínas Represoras/fisiología , Factor de Transcripción YY1/químicaRESUMEN
At each heartbeat, cardiac myocytes are activated by a cytoplasmic Ca(2+) transient in great part due to Ca(2+) release from the sarcoplasmic reticulum via ryanodine receptors (RyRs) clustered within calcium release units (peripheral couplings/dyads). A Ca(2+) transient also occurs in the nucleoplasm, following the cytoplasmic transient with some delay. Under conditions where the InsP3 production is stimulated, these Ca(2+) transients are regulated actively, presumably by an additional release of Ca(2+) via InsP3 receptors (InsP3Rs). This raises the question whether InsP3Rs are appropriately located for this effect and whether sources of InsP3 and Ca(2+) are available for their activation. We have defined the structural basis for InsP3R activity at the nucleus, using immunolabeling for confocal microscopy and freeze-drying/shadowing, T tubule "staining" and thin sectioning for electron microscopy. By these means we establish the presence of InsP3R at the outer nuclear envelope and show a close spatial relationship between the nuclear envelope, T tubules (a likely source of InsP3) and dyads (the known source of Ca(2+)). The frequency, distribution and distance from the nucleus of T tubules and dyads appropriately establish local perinuclear Ca(2+) microdomains in cardiac myocytes.