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The knowledge translation movement in health has led to the production of vast amounts of knowledge tools aimed at broadening clinicians' evidence base and improving the quality and efficacy of their practices. However important, these tools, largely oriented towards biomedical and technological aspects of care, are of limited potential for addressing the complex interactions between patients' socio-economic contexts and their health. Yet health professionals frequently lack the sensitivity, knowledge and ability to incorporate approaches to poverty within their practices; this is partly due to their limited understanding of the lived experience of poverty and of the complexity of barriers underprivileged people face to achieve and maintain health. In a context of persisting social inequalities in oral health, the Montreal-based Listening to Others multi-stakeholder partnership has been engaged in developing health professional education on poverty since 2006. In this article, we describe and reflect on how service users representing the Québec antipoverty coalition, academics from University of Montreal and McGill University, representatives of Québec dental regulatory bodies and artists collaborated to produce an educational film on poverty. Project partners' specific contributions to the film script are highlighted, emphasizing their potential to enrich the health professional educator's practice knowledge base. In doing so, this article provides an explicit and concrete example of how participatory processes can support co-learning and knowledge co-production through engagement with the arts. The overall aim is to demonstrate how participatory research can enhance knowledge translation by producing educational tools that promote critical reflection and address complexity.

To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.ydbio.2008.02.053 Byline: Gaetan Pascreau (a), Jean-Guy Delcros (a), Nathalie Morin (b), Claude Prigent (a), Yannick Arlot-Bonnemains (a) Keywords: Aurora-A; Kinase; Autophosphorylation; Xenopus; Oocyte; Maturation Abstract: Xenopus laevis Aurora-A is phosphorylated in vivo onto three amino acids: Ser53, Thr295 and Ser349. The activation of the kinase depends on its autophosphorylation on Thr295 within the T-loop. The phosphorylation of Ser53 by still unknown kinase(s) prevents its degradation. The present work focused on the regulation of Aurora-A function via Ser349 phosphorylation. Mutagenesis of Ser349 to alanine (S349A) had few impact in vitro on the capability of the kinase to autophosphorylate as well as on its activity. These data in addition to in gel kinase assays and site-specific proteolytic digestion experiments prove that Ser349 is clearly neither a primary autophosphorylation site, nor an autophosphorylation site depending on the priming phosphorylation of Thr295. Using specific antibodies, we also show that the phosphorylation of Aurora-A Ser349 is a physiological event during Xenopus oocyte maturation triggered by progesterone. A peak of phosphorylation paralleled the decrease of Aurora activity observed between meiosis I and II. In response to progesterone, X. laevis stage VI oocytes microinjected with the Aurora-A S349A mutant proceeded normally to germinal vesicle breakdown (GVBD), but degenerated rapidly soon after. Since phosphorylation of Ser349 is responsible for a decrease in kinase activity, our results suggest that a down-regulation of Aurora-A activity involving Ser349 phosphorylation is required in the process of maturation. Author Affiliation: (a) CNRS UMR6061 'Genetique et Developpement', Groupe Cycle Cellulaire, IFR-140 GFAS, Faculte de Medecine, Universite Rennes 1, 2 Av du Pr Leon Bernard, 35043 Rennes Cedex, France (b) CNRS FRE 2593, Centre de Recherches en Biochimie Macromoleculaire, 34293 Montpellier, France Article History: Received 29 May 2007; Revised 3 February 2008; Accepted 27 February 2008

Third National Health and Nutrition Examination Survey (NHANES III) collected data from 13,227 people, aged 20 to 79 years, to get information on sociodemographic characteristics, cigarette smoking, perceived dental treatment needs and clinical health. The results indicate that current cigarette smokers in the United States are more likely to have greater perceived dental needs compared with non-smokers. The results motivate people to seek dental care and enhance efforts directed toward tobacco-use cessation programs.

The p21-activated kinase (PAK) proteins regulate many cellular events including cell cycle progression, cell death and survival, and cytoskeleton rearrangements. We previously identified X-PAK5 that binds the actin and microtubule networks, and could potentially regulate their coordinated dynamics during cell motility. In this study, we investigated the functional importance of this kinase during gastrulation in Xenopus. X-PAK5 is mainly expressed in regions of the embryo that undergo extensive cell movements during gastrula such as the animal hemisphere and the marginal zone. Expression of a kinase-dead mutant inhibits convergent extension movements in whole embryos and in activin-treated animal cap by modifying behavior of cells. This phenotype is rescued in embryo by adding back X-PAK5 catalytic activity. The active kinase decreases cell adhesiveness when expressed in animal hemisphere and inhibits the calcium-dependent reassociation of cells, while dead X-PAK5 kinase localizes to cell-cell junctions and increases cell adhesion. In addition, endogenous X-PAK5 colocalizes with adherens junction proteins and its activity is regulated by extracellular calcium. Taken together, our results suggest that X-PAK5 regulates convergent extension movements in vivo by modulating the calcium-mediated cell-cell adhesion. Keywords: X-PAK5; Xenopus embryogenesis; Cell adhesion; Convergent extension

Described is a method for channel erosion control and habitat rehabilitation featuring intermittent placement of structures made of large woody debris. This method is expressly tailored to address severe problems typical of incised channels with little sediment coarser than sand. In these types of environments, buoyancy forces are typically more important factors in woody debris stability than fluid drag. Buoyant forces are counteracted by the weight of the structure, earth anchors, and sediment deposits. Design concepts were tested in a demonstration project constructed along 2 km of channel draining a 37-[km.sup.2] watershed. Large woody debris structures reduced velocities in the region adjacent to the bank toe and induced sediment deposition and retention. Construction costs per unit channel length were 23-58% of costs for recent stone bank stabilization projects within the same region. During the second year following construction, 31% of the structures failed during high flows, probably due to inadequate anchoring. CE Database subject headings: Stream channels; Bank stabilization; Ecosystems; Restoration; Channel erosion; Debris; Wood.

Abstract Background Cytokinesis is the final step of cell division taking place at the end of mitosis during which the cytoplasmic content and replicated chromosomes of a cell are equally partitioned between the two daughter cells. This process is achieved by the formation and the ingression of an actomyosin contractile ring under the control of equatorial microtubules. The mechanisms of contractile ring formation are not fully understood but involve recruitment of preexisting actin filaments and de novo actin polymerisation. Results In this study, we evaluated the role of the actin nucleation factor, Arp2/3 complex, during cytokinesis. We found that the Arp2/3 complex is recruited late to the cleavage furrow suggesting a potential involvement of Arp2/3 complex during this process. Furthermore, wiskostatin a potent inhibitor of N-WASP activity towards the Arp2/3 complex blocked cytokinesis without affecting mitosis. Nonetheless, this inhibition could not be reproduced using alternative approaches targeting the N-WASP/Arp2/3 complex pathway. Conclusion We conclude that the wiskostatin induced defective cytokinesis does not occur through the inhibition of the N-WASP/Arp2/3 pathway. Wiskostatin is likely to either directly target other proteins required for cytokinesis progression or alternately wiskostatin bound to N-WASP could affect the activity of other factors involved in cytokinesis.