The state of health services partnering with consumers: evidence from an online survey of Australian health services.

BACKGROUND: Involving consumers in producing health services is mandated in many countries. Evidence indicates consumer partnerships lead to improved service design, quality and innovation. Involving participants from minority groups is crucial because poor understanding of distinctive needs affects individuals' service experiences and outcomes. Few studies consider service compliance with consumer partnering requirements or inclusion of minority group participants. METHODS: An online survey structured by domains of the Australian National Safety and Quality in Health Service Standards (NSQHS, 2013), was conducted. Questions covered consumer partnering in service planning, management and evaluation plus patient care design and inclusion of consumers from minority groups. Approximately 1200 Australian hospital and day surgery services were identified and 447 individual email addresses were identified for staff leading consumer partnerships. Quantitative data were analysed using SPSS. Qualitative responses, managed in NVivo, were analysed thematically. Frequencies were produced to indicate common activities and range of activities within question domains. RESULTS: Comprehensive responses were received from 115 services (25.7%), including metropolitan and non-metropolitan, private and public service settings. Most respondents (95.6%) "partnered with consumers to develop or provide feedback on patient information". Regarding inclusion of participants from minority groups, respondents were least likely to specifically include those from socially disadvantaged backgrounds (23.6%). Public health services were more likely than private services to engage with consumers. CONCLUSIONS: The survey is the first to include responses about consumer partnering from across Australia. While many respondents partner with consumers, it is clear that more easily-organised activity such as involvement in existing committees or commenting on patient information occurs more commonly than involvement in strategy or governance. This raises questions over whether strategic-level involvement is too difficult or unrealistic; or whether services simply lack tools. Minority views may be missed where there is a lack of specific action to include diversity. Future work might address why services choose the activities we found and probe emerging opportunities, such as using social media or online engagement.

A scoping review of the association between rural medical education and rural practice location.

BACKGROUND: Inequitable distribution of the medical workforce is an international problem that undermines universal access to healthcare. Governments in many countries have invested in rural-focused medical education programs to increase the supply of rural doctors. METHODS: Using a structured five-step approach, a scoping review was conducted to map the existing evidence on the relationship between professional entry-level, pre-vocational medical education delivered in rural settings and rural workforce outcomes. Key search terms were developed, with database searches yielding 37 relevant articles. During data charting, a set of types of studies emerged, and we developed a typology to assist with article sorting and information structuring. RESULTS: Medical students attending a rural campus or spending time in a rural area are more likely to practise in non-metropolitan areas upon graduation than students studying at a city campus. In many cases, these positive findings could be confounded by students having a rural origin or being predisposed to want rural work. There is some evidence to suggest that the longer a person spends time as a medical student in a rural area, the more likely they are to work rurally following graduation. Overall, the articles located had limitations related to small sample size, inconsistent definition of rurality and lack of attention to controlling for variables that might influence rural practice decision, for example, rural background. Comparative data were lacking, and most studies were conducted by staff from the medical schools that were the focus of the research. There was no consideration given in any study found to the cost-effectiveness of entry-level medical education delivered in rural settings versus other ways of producing rural practitioners. CONCLUSIONS: Given limitations, available evidence suggests that medical education in a rural location does increase the number of medical graduates that will work in a rural place. There are indications of a gradient effect where increased rural practice exposure during medical education leads to more rurally located graduates; however, robust studies are needed to verify this finding. Given the significant funding being directed to universities to increase graduates that will work rurally, appropriate future research is recommended.

Silencer of death domains (SODD) inhibits skeletal muscle and kidney enriched inositol 5-phosphatase (SKIP) and regulates phosphoinositide 3-kinase (PI3K)/Akt signaling to the actin cytoskeleton.

Phosphoinositide 3-kinase (PI3K) regulates cell polarity and migration by generating phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P(3)) at the leading edge of migrating cells. The serine-threonine protein kinase Akt binds to PI(3,4,5)P(3), resulting in its activation. Active Akt promotes spatially regulated actin cytoskeletal remodeling and thereby directed cell migration. The inositol polyphosphate 5-phosphatases (5-ptases) degrade PI(3,4,5)P(3) to form PI(3,4)P(2), which leads to diminished Akt activation. Several 5-ptases, including SKIP and SHIP2, inhibit actin cytoskeletal reorganization by opposing PI3K/Akt signaling. In this current study, we identify a molecular co-chaperone termed silencer of death domains (SODD/BAG4) that forms a complex with several 5-ptase family members, including SKIP, SHIP1, and SHIP2. The interaction between SODD and SKIP exerts an inhibitory effect on SKIP PI(3,4,5)P(3) 5-ptase catalytic activity and consequently enhances the recruitment of PI(3,4,5)P(3)-effectors to the plasma membrane. In contrast, SODD(-/-) mouse embryonic fibroblasts exhibit reduced Akt-Ser(473) and -Thr(308) phosphorylation following EGF stimulation, associated with increased SKIP PI(3,4,5)P(3)-5-ptase activity. SODD(-/-) mouse embryonic fibroblasts exhibit decreased EGF-stimulated F-actin stress fibers, lamellipodia, and focal adhesion complexity, a phenotype that is rescued by the expression of constitutively active Akt1. Furthermore, reduced cell migration was observed in SODD(-/-) macrophages, which express the three 5-ptases shown to interact with SODD (SKIP, SHIP1, and SHIP2). Therefore, this study identifies SODD as a novel regulator of PI3K/Akt signaling to the actin cytoskeleton.

SHIP-2 forms a tetrameric complex with filamin, actin, and GPIb-IX-V: localization of SHIP-2 to the activated platelet actin cytoskeleton.

The platelet receptor for the von Willebrand factor (VWF) glycoprotein Ib-IX-V (GPIb-IX-V) complex mediates platelet adhesion at sites of vascular injury. The cytoplasmic tail of the GPIbalpha subunit interacts with the actin-binding protein, filamin, anchoring the receptor in the cytoskeleton. In motile cells, the second messenger phosphatidylinositol 3,4,5 trisphosphate (PtdIns(3,4,5)P3) induces submembraneous actin remodeling. The inositol polyphosphate 5-phosphatase, Src homology 2 domain-containing inositol polyphosphate 5-phosphatase-2 (SHIP-2), hydrolyzes PtdIns(3,4,5)P3 forming phosphatidylinositol 3,4 bisphosphate (PtdIns(3,4)P2) and regulates membrane ruffling via complex formation with filamin. In this study we investigate the intracellular location and association of SHIP-2 with filamin, actin, and the GPIb-IX-V complex in platelets. Immunoprecipitation of SHIP-2 from the Triton-soluble fraction of unstimulated platelets demonstrated association between SHIP-2, filamin, actin, and GPIb-IX-V. SHIP-2 associated with filamin or GPIb-IX-V was active and demonstrated PtdIns(3,4,5)P3 5-phosphatase activity. Following thrombin or VWF-induced platelet activation, detection of the SHIP-2, filamin, and receptor complex decreased in the Triton-soluble fraction, although in control studies the level of SHIP-2, filamin, or GPIb-IX-V immunoprecipitated by their respective antibodies did not change following platelet activation. In activated platelets spreading on a VWF matrix, SHIP-2 localized intensely with actin at the central actin ring and colocalized with actin and filamin at filopodia and lamellipodia. In spread platelets, GPIb-IX-V localized to the center of the platelet and showed little colocalization with filamin at the plasma membrane. These studies demonstrate a functionally active complex between SHIP-2, filamin, actin, and GPIb-IX-V that may orchestrate the localized hydrolysis of PtdIns(3,4,5)P3 and thereby regulate cortical and submembraneous actin.

Identification of a novel domain in two mammalian inositol-polyphosphate 5-phosphatases that mediates membrane ruffle localization. The inositol 5-phosphatase skip localizes to the endoplasmic reticulum and translocates to membrane ruffles following epidermal growth factor stimulation.

SKIP (skeletal muscle and kidney enriched inositol phosphatase) is a recently identified phosphatidylinositol 3,4,5-trisphosphate- and phosphatidylinositol 4,5-bisphosphate-specific 5-phosphatase. In this study, we investigated the intracellular localization of SKIP. Indirect immunofluorescence and subcellular fractionation showed that, in serum-starved cells, both endogenous and recombinant SKIP colocalized with markers of the endoplasmic reticulum (ER). Following epidermal growth factor (EGF) stimulation, SKIP transiently translocated to plasma membrane ruffles and colocalized with submembranous actin. Data base searching demonstrated a novel 128-amino acid domain in the C terminus of SKIP, designated SKICH for SKIP carboxyl homology, which is also found in the 107-kDa 5-phosphatase PIPP and in members of the TRAF6-binding protein family. Recombinant SKIP lacking the SKICH domain localized to the ER, but did not translocate to membrane ruffles following EGF stimulation. The SKIP SKICH domain showed perinuclear localization and mediated EGF-stimulated plasma membrane ruffle localization. The SKICH domain of the 5-phosphatase PIPP also mediated plasma membrane ruffle localization. Mutational analysis identified the core sequence within the SKICH domain that mediated constitutive membrane association and C-terminal sequences unique to SKIP that contributed to ER localization. Collectively, these studies demonstrate a novel membrane-targeting domain that serves to recruit SKIP and PIPP to membrane ruffles.

The myotubularin family: novel phosphoinositide regulators.

Phosphatidylinositol 3-phosphate [PtdIns(3)P] acts as a second messenger via the recruitment of diverse signalling proteins to various cellular compartments. Recent advances have highlighted the association of human diseases with mutations in phosphatases that regulate PtdIns(3)P levels. Myotubularin, the gene mutated in myotubular myopathy, functions as a lipid phosphatase with specificity for PtdIns(3)P. It is now apparent that there is an increasing family of proteins that are defined by their significant homology with myotubularin. The myotubularin-related gene family includes proteins that exhibit a lipid phosphatase catalytic motif, those that contain mutations of the critical catalytic residues, and at least one protein that functions as an adapter subunit for PtdIns(3)P-3-phosphatase activity. The present challenge is to understand how deregulation of phosphoinositide metabolism causes human disease.