This review provides a brief overview of mammalian circadian biology before summarizing experimental data demonstrating several mechanisms by which this may occur, including: reducing activation of SCN cells receiving retinal
input, transient disorganization of SCN outputs, and reduced sensitivity to SCN signals in hypothalamic sites responsible for integrating homeostatic and circadian information. Further investigation of these mechanisms will be key to elucidating pharmacological or behavioural interventions that check details suppress the negative psychological and health effects of light-driven circadian rhythms in humans, specifically those with work schedules that do not conform to the solar day. (C) 2011 Elsevier Ltd. All rights reserved.”
“Gephyrin is a multifunctional protein responsible for molybdenum cofactor synthesis and the clustering of glycine and GABA(A) receptors at inhibitory synapses. Based on the structure of its two conserved domains, click here G and E,
gephyrin is thought to form a hexagonal lattice serving as a scaffold for accessory proteins at postsynaptic sites. However, important aspects of gephyrin gene expression, protein structure and regulation, as well as the role of gephyrin in synapse formation and plasticity, remain poorly understood. Here we review the current state of knowledge about gephyrin, highlighting new research avenues based on a different structural model and a revised nomenclature for gephyrin splice variants. Unraveling the biology of gephyrin will further our understanding of glycinergic and GABAergic synapses in health and disease.”
“Osteoarthritis (OA) is characterized by cartilage degradation. The chondrocyte is the only cell type present in mature cartilage, and it is important in the control of cartilage
integrity. The aim of this study was to analyze, by a proteomic approach, Cytidine deaminase the changes that are characteristic of OA chondrocytes, and to identify new CIA-related proteins. Chondrocytes were isolated from the cartilage of ten CIA patients undergoing joint replacement and ten donors with no history of joint disease. Whole-cell proteins were resolved by 2-DE and stained with SYPRO Ruby. Protein expression patterns of 2-DE gels from OA and normal chondrocyte proteins were analyzed with PDQuest 7.3.1 software. OA-related proteins were identified by MALDI-TOF or MALDI-TOF/ TOF MS. The results were validated for ANXA1, GSTO1, GRP78, and HSP90 beta in cells by Western blotting and in tissue cartilage by immunohistochemistry Results showed an average of 700 protein spots that were present in the 2-DE gels. Compared to normal chondrocytes, 19 protein spots were found to be significantly increased in OA cells (ratio OA:N >= 2.0, p < 0.05), whereas nine were decreased in CIA chondrocytes (ratio OA:N <= 0.5, p < 0.05).