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Objective: This study investigated body weight and nutritional behavior perceptions among Division II collegiate athletes. Participants: The sample was composed of 155 collegiate athletes who responded to a survey. Methods: Data were self-reported by athletes via questionnaire. Independent-sample t tests were used to identify significant gender differences related to body weight perceptions, nutritional practices, and ideal weight difference (IWD). An alpha level of 0.05 was used to determine statistical significance. Results: Mean ± SD female and male IWD was -6.8 ± 8.8 and 1.3 ± 12.3 lbs, respectively (p < 0.001). Significant differences in level of agreement regarding perceived body weight effects on performance and dietary practices existed between genders. Conclusions: Significant gender differences may exist regarding body weight perceptions and nutritional practices among collegiate athletes. Deliverance of gender-specific educational information about proper nutritional practices is warranted. To properly tailor interventions to specific sports, research with larger sample sizes is needed.

Mutations in methyl DNA binding protein 2 (MeCP2) cause the neurodevelopmental disorder Rett syndrome (RTT). The mechanism(s) by which the native MeCP2 protein operates in the cell are not well understood. Historically, MeCP2 has been characterized as a proximal gene silencer with 2 functional domains: a methyl DNA binding domain and a transcription repression domain. However, several lines of new data indicate that MeCP2 structure and function relationships are more complex. In this review, we first discuss recent studies that have advanced understanding of the basic structural biochemistry of MeCP2. This is followed by an analysis of cell-based experiments suggesting MeCP2 is a regulator, rather than a strict silencer, of transcription. The new data establish MeCP2 as a multifunctional nuclear protein, with potentially important roles in chromatin architecture, regulation of RNA splicing, and active transcription. We conclude by discussing clinical correlations between domain-specific mutations and RTT pathology to stress that all structural domains of MeCP2 are required to properly mediate cellular function of the intact protein. Key words: Rett syndrome, epigenomics, chromatin architecture, splice regulation, methyl DNA binding. Les mutations au sein de la proteine MeCP2 (<< methyl DNA binding protein 2 >>) sont responsables d'une maladie neurodeveloppementale, le syndrome de Rett (RTT). Les mecanismes par lesquels la proteine MeCP2 intacte agit dans la cellule ne sont pas bien compris. Historiquement, la MeCP2 a ete caracterisee comme etant un silenceur genique proximal possedant 2 domaines fonctionnels : un domaine de liaison de l'ADN methyle et un domaine de repression de la transcription. Cependant, plusieurs pistes nouvelles indiquent que les relations structure/fonction de la MeCP2 sont plus complexes. Dans cette synthese, nous discuterons d'abord des etudes recentes qui ont permis de faire avancer nos connaissances de la biochimie structurale de base de la MeCP2. Suivra une analyse d'experiences realisees sur des cellules qui suggerent que la MeCP2 est davantage un regulateur qu'un strict silenceur de la transcription. Les nouveaux resultats etablissent que la MeCP2 est une proteine nucleaire multifonctionnelle possedant des roles potentiellement importants dans l'architecture de la chromatine, la regulation de l'epissage de YARN et la transcription active. Nous concluons en discutant des correlations cliniques qui peuvent s'etablir entre les mutations specifiques a chaque domaine et la pathologie du RTT afin de mettre en evidence le fait que tous les domaines structuraux de la MeCP2 sont requis pour assurer adequatement la fonction cellulaire de la proteine intacte. Mots-cles : syndrome de Rett, epigenomique, architecture de la chromatine, regulation de l'epissage, liaison a l'ADN methyle. [Traduit par la Redaction], Introduction: a historical perspective of MeCP2 structure and function Methyl CpG binding protein (MeCP) 2 is a 53 kDa nuclear protein named for its ability to bind methylated DNA (Lewis [...]