Role of social interaction on quality of life

Introduction: Society plays an important role in determining quality of life of human beings particularly in case of loneliness, physical inability and loss of income. In this background there is a great role of social interaction in improving quality of life of geriatric population. Methodology: This community-based interventional longitudinal study was done among the study population using Quality of Life Questionnaire developed by World Health Organization (WHOQOL-BREF) by conducting interviews by house to house visit. The selected study subjects according to gender and place of residence were told to conduct regular social interaction session as per their convenient time and place. After 8 weeks of social interaction sessions again the participants were asked about their quality of life by conducting interviews using WHOQOL-BREF questionnaire. Results: It was found that mean transformed scores of quality of life improved significantly in all domains after social interaction as compared to score at the beginning of the study. Further, the difference of score (before and after social interaction) was significantly higher among those who attended social interaction session for more number of days. Conclusion: Social interaction has a significant role in improving the quality of life of elderly people. [Natl J Med Res 2015; 5(4.000): 290-292

Prion-like p53 amyloids in cancer

The global transcription factor, p53, is a master regulator of gene expression in cells. Mutations in the TP53 gene promote unregulated cell growth through the inactivation of downstream effectors of the p53 pathway. In fact, mutant p53 is highly prone to misfolding and frequently resides inside the cell as large aggregates, causing loss of physiological function of the tumor-suppressor protein. Here, we review the plausible reasons for functional loss of p53, including amyloid formation leading to unhindered cancer progression. We discuss previous as well as recent findings regarding the amyloid formation of p53 in vitro and in vivo. We elaborate on prion-like properties of p53 amyloids and their possible involvement in cancer progression. Because the p53 pathway is historically most targeted for the development of anticancer therapeutics, we have also summarized some of the recent approaches and advances in reviving the antiproliferative activities of wild-type p53. In this Perspective, we provide insight into understanding p53 as a prion-like protein and propose cancer to be recognized as an amyloid or prion-like disease

Comparison of Kinetics, Toxicity, Oligomer Formation, and Membrane Binding Capacity of α‑Synuclein Familial Mutations at the A53 Site, Including the Newly Discovered A53V Mutation

The involvement of α-synuclein (α-Syn) amyloid formation in Parkinson’s disease (PD) pathogenesis is supported by the discovery of α-Syn gene (SNCA) mutations linked with familial PD, which are known to modulate the oligomerization and aggregation of α-Syn. Recently, the A53V mutation has been discovered, which leads to late-onset PD. In this study, we characterized for the first time the biophysical properties of A53V, including the aggregation propensities, toxicity of aggregated species, and membrane binding capability, along with those of all familial mutations at the A53 position. Our data suggest that the A53V mutation accelerates fibrillation of α-Syn without affecting the overall morphology or cytotoxicity of fibrils compared to those of the wild-type (WT) protein. The aggregation propensity for A53 mutants is found to decrease in the following order: A53T > A53V > WT > A53E. In addition, a time course aggregation study reveals that the A53V mutant promotes early oligomerization similar to the case for the A53T mutation. It promotes the largest amount of oligomer formation immediately after dissolution, which is cytotoxic. Although in the presence of membrane-mimicking environments, the A53V mutation showed an extent of helix induction capacity similar to that of the WT protein, it exhibited less binding to lipid vesicles. The nuclear magnetic resonance study revealed unique chemical shift perturbations caused by the A53V mutation compared to those caused by other mutations at the A53 site. This study might help to establish the disease-causing mechanism of A53V in PD pathology