The patterns and predictors of disease disclosure by patients with cancer

Previous qualitative research has identified that disclosing a diagnosis to loved ones, is one of the hardest aspects of having cancer (Hilton et al, 2009). Although there is an extensive literature on disclosure of general information about the self, less is known about the extent to which people go on to talk about their diagnosis and the helpfulness of such disclosure within the specific context of cancer. Therefore the current study aimed to quantify disclosure patterns by measuring the degree of disclosure as well as the perceived helpfulness of disclosure. It also sought to determine the factors associated with disclosure and helpfulness of disclosure. The study was a cross-sectional postal questionnaire survey of 120 patients who had recently received a diagnosis of either lung, colorectal or skin cancer. Results indicated that the majority of patients disclosed to a variety of social targets, and most found it helpful to disclose. ‗Dispositional openness‘ and ‗perceived social support‘ were found to predict the extent of disclosure, as well as the helpfulness of disclosure. The results suggest that individual differences and situational factors may impact on disclosure and that medical professionals may play an important role in the disclosure process. With reference to the limitations, directions for future research are discussed, as well as the implications for clinical practice

The involvement of nurses and midwives in screening and brief interventions for hazardous and harmful use of alcohol and other psychoactive substances

This report provides details of a review of the literature on the involvement of nurses and midwives in screening and brief interventions for hazardous and harmful use of alcohol and other psychoactive substances

Long coiled-coil proteins and membrane traffic

AbstractProtein transport between organelles is mediated by vesicles which must accurately dock and fuse with appropriate compartments. Over the past several years a large number of long coiled-coil proteins have been identified on the Golgi and on endosomes, mostly as auto-antigens in autoimmune disorders. Based on their restricted intracellular distributions and their predicted rod-like structure, these proteins have been proposed to play a role in tethering vesicles to target organelles prior to fusion. However, such proteins may also play a structural role, for example as components of a Golgi matrix, or as scaffolds for the assembly of other factors important for fusion. This review will examine what is known about the function of these large coiled-coil proteins in membrane traffic

The golgin coiled-coil proteins capture different types of transport carriers via distinct N-terminal motifs

Abstract Background The internal organization of cells depends on mechanisms to ensure that transport carriers, such as vesicles, fuse only with the correct destination organelle. Several types of proteins have been proposed to confer specificity to this process, and we have recently shown that a set of coiled-coil proteins on the Golgi, called golgins, are able to capture specific classes of carriers when relocated to an ectopic location. Results Mapping of six different golgins reveals that, in each case, a short 20–50 residue region is necessary and sufficient to capture specific carriers. In all six of GMAP-210, golgin-84, TMF, golgin-97, golgin-245, and GCC88, this region is located at the extreme N-terminus of the protein. The vesicle-capturing regions of GMAP-210, golgin-84, and TMF capture intra-Golgi vesicles and share some sequence features, suggesting that they act in a related, if distinct, manner. In the case of GMAP-210, this shared feature is in addition to a previously characterized “amphipathic lipid-packing sensor” motif that can capture highly curved membranes, with the two motifs being apparently involved in capturing distinct types of vesicles. Of the three GRIP domain golgins that capture endosome-to-Golgi carriers, golgin-97 and golgin-245 share a closely related capture motif, whereas that in GCC88 is distinct, suggesting that it works by a different mechanism and raising the possibility that the three golgins capture different classes of endosome-derived carriers that share many cargos but have distinct features for recognition at the Golgi. Conclusions For six different golgins, the capture of carriers is mediated by a short region at the N-terminus of the protein. There appear to be at least four different types of motif, consistent with specific golgins capturing specific classes of carrier and implying the existence of distinct receptors present on each of these different carrier classes

The golgin coiled-coil proteins capture different types of transport carriers via distinct N-terminal motifs.

BACKGROUND: The internal organization of cells depends on mechanisms to ensure that transport carriers, such as vesicles, fuse only with the correct destination organelle. Several types of proteins have been proposed to confer specificity to this process, and we have recently shown that a set of coiled-coil proteins on the Golgi, called golgins, are able to capture specific classes of carriers when relocated to an ectopic location. RESULTS: Mapping of six different golgins reveals that, in each case, a short 20-50 residue region is necessary and sufficient to capture specific carriers. In all six of GMAP-210, golgin-84, TMF, golgin-97, golgin-245, and GCC88, this region is located at the extreme N-terminus of the protein. The vesicle-capturing regions of GMAP-210, golgin-84, and TMF capture intra-Golgi vesicles and share some sequence features, suggesting that they act in a related, if distinct, manner. In the case of GMAP-210, this shared feature is in addition to a previously characterized "amphipathic lipid-packing sensor" motif that can capture highly curved membranes, with the two motifs being apparently involved in capturing distinct types of vesicles. Of the three GRIP domain golgins that capture endosome-to-Golgi carriers, golgin-97 and golgin-245 share a closely related capture motif, whereas that in GCC88 is distinct, suggesting that it works by a different mechanism and raising the possibility that the three golgins capture different classes of endosome-derived carriers that share many cargos but have distinct features for recognition at the Golgi. CONCLUSIONS: For six different golgins, the capture of carriers is mediated by a short region at the N-terminus of the protein. There appear to be at least four different types of motif, consistent with specific golgins capturing specific classes of carrier and implying the existence of distinct receptors present on each of these different carrier classes