ABSTRACT
The WHO has called for action to integrate physical activity promotion into healthcare settings, yet there is a lack of consensus on the competencies required by health professionals to deliver effective movement behaviour change support. The objective of this study was to establish key competencies relevant for all health professionals to support individuals to change their movement behaviours. Consensus was obtained using a three-phase Delphi process. Participants with expertise in physical activity and sedentary behaviour were asked to report what knowledge, skills and attributes they believed health professionals should possess in relation to movement behaviour change. Proposed competencies were developed and rated for importance. Participants were asked to indicate agreement for inclusion, with consensus defined as group level agreement of at least 80%. Participants from 11 countries, working in academic (55%), clinical (30%) or combined academic/clinical (13%) roles reached consensus on 11 competencies across 3 rounds (n=40, n=36 and n=34, respectively). Some competencies considered specific to certain disciplines did not qualify for inclusion. Participants agreed that health professionals should recognise, take ownership of, and practise interprofessional collaboration in supporting movement behaviour change; support positive culture around these behaviours; communicate using person-centred approaches that consider determinants, barriers and facilitators of movement behaviours; explain the health impacts of these behaviours; and recognise how their own behaviour influences movement behaviour change support. This consensus defines 11 competencies for health professionals, which may serve as a catalyst for building a culture of advocacy for movement behaviour change across health disciplines.
Subject(s)
Exercise , Health Personnel , Humans , Delphi Technique , Sedentary Behavior , ConsensusABSTRACT
Alzheimer's disease (AD) is a multigenic neurodegenerative disorder characterized by distinct neuropathological hallmarks including deposits of the beta-amyloid (A beta) peptide. A beta is a 39- to 43-amino acid peptide derived from the proteolytic processing of the amyloid precursor protein (APP). While increasing evidence suggests that altered APP processing and A beta metabolism is a common feature of AD, the relationship between the levels of A beta and various APP products and the onset of AD remains unclear. We have undertaken a screen to characterize genetic factors that modify APP processing, A beta metabolism and A beta deposition in a genomic-based yeast artificial chromosome (YAC) transgenic mouse model of AD. A mutant human APP YAC transgene was transferred to three inbred mouse strains. Despite similar levels of holo-APP expression in the congenic strains, the levels of APP C-terminal fragments as well as brain and plasma A beta in young animals varied by genetic background. Furthermore, we demonstrate that age-dependent A beta deposition in the APP YAC transgenic model is dramatically altered depending on the congenic strain examined. These studies demonstrate that APP processing, A beta metabolism and A beta deposition are regulated by genetic background and that analysis of these phenotypes in mice should provide new insights into the factors that regulate AD pathogenesis.
Subject(s)
Amyloid beta-Peptides/metabolism , Amyloid beta-Protein Precursor/genetics , Protein Processing, Post-Translational , Alzheimer Disease/metabolism , Alzheimer Disease/pathology , Amyloid beta-Peptides/genetics , Amyloid beta-Protein Precursor/metabolism , Animals , Antibodies, Monoclonal/metabolism , Blotting, Western , Brain/metabolism , Brain/pathology , Chromosomes, Artificial, Bacterial , Enzyme-Linked Immunosorbent Assay , Gene Expression Regulation , Genetic Variation , Immunohistochemistry , Mass Spectrometry , Mice , Mice, Transgenic , Precipitin Tests , Species Specificity , TransgenesABSTRACT
Mutations in the amyloid precursor protein (APP) gene are associated with altered production and deposition of amyloid beta (Abeta) peptide in the Alzheimer's disease (AD) brain. The pathways that regulate APP processing, Abeta production and Abeta deposition in different tissues and brain regions remain unclear. To address this, we examined levels of various APP processing products as well as Abeta deposition in a genomic-based (R1.40) and a cDNA-based (Tg2576) transgenic mouse model of AD. In tissues, only brain generated detectable levels of the penultimate precursor to Abeta, APP C-terminal fragment-beta. In brain regions, holoAPP levels remained constant, but ratios of APP C-terminal fragments and levels of Abeta differed significantly. Surprisingly, cortex had the lowest steady-state levels of Abeta compared to other brain regions. Comparison of Abeta deposition in Tg2576 and R1.40 animals revealed that R1.40 exhibited more abundant deposition in cortex while Tg2576 exhibited extensive deposition in the hippocampus. Our results suggest that AD transgenic models are not equal; their unique characteristics must be considered when studying AD pathogenesis and therapies.
