BackgroundHealthy movement behaviours of Canadian children and youth have been found to be suboptimal; this is associated with declines in physical fitness, increases in obesity, and elevated chronic disease risk. Physical literacy is an evolving construct representing foundational domains upon which physically active lifestyles are based. Many sectors and organizations in Canada are embracing physical literacy in their programs, practices, policies, and research; however, the use of inconsistent definitions and conceptualizations of physical literacy had been identified by stakeholders as hindering promotion and advancement efforts.MethodsWith leadership from ParticipACTION, organizations from the physical activity, public health, sport, physical education, and recreation sectors collaborated to create a physical literacy consensus definition and position statement for use by all Canadian organizations and individuals. The process involved an environmental scan, survey of related evidence, stakeholder consultations, and creation of a Steering Committee. From this background work a consensus statement was drafted, shared with stakeholders, revised, and ratified.ResultsCanada’s Physical Literacy Consensus Statement was launched in June 2015 at the International Physical Literacy Conference in Vancouver, British Columbia. To further promote the Consensus Statement, the Sport for Life Society developed and simultaneously released the “Vancouver Declaration”, which contained additional guidance on physical literacy. Both the Consensus Statement and the Declaration endorsed the International Physical Literacy Association’s definition of physical literacy, namely “the motivation, confidence, physical competence, knowledge and understanding to value and take responsibility for engagement in physical activities for life”.ConclusionsSector partners hope that the Consensus Statement, with its standardized definition, brings greater harmony, synergy, and consistency to physical literacy efforts in Canada and internationally. Going forward, the impact of this initiative on the sector, and the more distal goal of increasing habitual physical activity levels, should be assessed.Electronic supplementary materialThe online version of this article (10.1186/s12889-018-5903-x) contains supplementary material, which is available to authorized users.

Expression of the phosphoenolpyruvate carboxykinase (PEPCK) gene is induced by 3-aminobenzamide, an inhibitor of poly(ADP-ribose) polymerase. Synthesis of PEPCK mRNA is repressed by insulin, but remains detectable in H4IIE hepatoma cells exposed simultaneously to both 3-aminobenzamide and insulin. This capability of 3-aminobenzamide to block the inhibitory actions of insulin suggests that ADPribosylation is required for the regulation of PEPCK gene expression by insulin. Furthermore, neither changes in chromatin condensation nor cell growth status were linked to these events. The inability of 3,4-dihydro-5-methylisoquinolinone (PD128763), a selective inhibitor of poly(ADP-ribose) polymerase, to impede insulin-dependent repression of PEPCK gene expression, however, indicated that 3-aminobenzamide does not operate by inhibiting poly(ADP-ribosyl)ation. The potential involvement of mono(ADP-ribosyl)ation, a process that is also inhibited by 3-aminobenzamide, in the regulation of PEPCK gene activity was then evaluated. Analysis of poly(ADP-ribose) polymerase activity and poly-(ADP-ribosyl)ation confirmed that there were no significant changes in response to insulin, while microsomal mono(ADP-ribosyl)transferase activity was elevated approximately fourfold. An increase in protein hydroxylamine-sensitive mono(ADP-ribosyl)ation was observed following insulin treatment. The sensitivity of the mono(ADP-ribosyl)transferase activity to 3-aminobenzamide but not PD128763 makes it plausible that mono(ADP-ribosyl)ation rather than poly(ADP-ribosyl)ation contributes to the regulation of PEPCK gene expression.Keywords : phosphoenolpyruvate carboxykinase; ADP-ribosylation; 3-aminobenzamide; insulin.Expression of the hepatic phosphoenolpyruvate carboxyki-ments found at position Ϫ1150 and position Ϫ450 [5]. While it has been demonstrated that insulin operates through an insulinnase (PEPCK) gene is transcriptionally regulated by insulin and other humoral agents in response to changes in glucose utiliza-responsive element (IRE) site present at position Ϫ410 [6], neither the proteins that bind to this site nor details of the signalling tion [1, 2]. In the fasting state and under conditions of stress, blood glucose levels are elevated by an increase in PEPCK system that conveys signals from the insulin receptor have been identified. mRNA synthesis through the actions of glucagon and glucocorticoids. In contrast, high blood glucose levels stimulate the reThe repression of PEPCK gene expression by insulin in the lease of insulin, which represses gene activity. Molecular dissec-presence of positive mediators such as glucagon indicates that tion has demonstrated that each humoral agent operates through insulin is a dominant factor [7]. Since glucagon-dependent a distinct regulatory element present in the PEPCK gene pro-CREB phosphorylation is not prevented by insulin, transcripmoter [3]. Glucagon, for instance, functions through the cAMP-tional inactivation likely involves an IRE-binding protein (IRdependent phosphorylation of the cAMP-resp...

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