In women, the results did not differ statistically significantly.
Conclusions. Physical activity at age of 20-64 years was associated with better mobility in old age. It was also linked to better grip strength and walking speed in older men but not in women.”
“Parkinson’s disease (PD) is a currently incurable neurodegenerative disorder that ISRIB in vivo affects the aging population. The loss of dopaminergic neurons in the substantia nigra is one of the pathological features of PD. The precise causes of PD remain unresolved but evidence supports both environmental and genetic contributions. Current efforts for the treatment of PD are directed toward the discovery of compounds that show promise in impeding Nec-1s concentration age-dependent
neurodegeneration in PD patients. Alpha-synuclein (alpha-Syn) is a human protein that is mutated in specific populations of patients with familial PD. Overexpression of alpha-Syn in animal models of PD replicates key symptoms of PD, including neurodegeneration. Here, we use the nematode Caenorhabditis elegans as a model system, whereby alpha-Syn toxicity causes dopaminergic neurodegeneration,
to test the capacity of valproic acid (VA) to protect neurons. The results of our study showed that treatment of nematodes with moderate concentrations of VA significantly protects dopaminergic neurons against alpha-Syn toxicity. Consistent with previously established knowledge related to the mechanistic action of VA in the cell, we showed through genetic analysis that the neuroprotection conferred by VA is inhibited by cell-specific depletion of the C. elegans ortholog of the MAP extracellular signal-regulated kinase (ERK), MPK-1, in the dopaminergic neurons. These findings LY294002 suggest that VA may exert its neuroprotective effect via ERK-MAPK, or alternately could act with MAPK signaling to additively provide dopaminergic neuroprotection. (C) 2013 Elsevier Ireland Ltd. All rights reserved.”
“Group II chaperonins exist in archaea and the eukaryotic cytosol, and mediate protein folding in an ATP-dependent
manner. We have been studying the reaction mechanism of group II chaperonins using alpha chaperonin, the recombinant chaperonin alpha subunit homo-oligomer from a hyperthermophilic archaeon, Thermococcus sp. strain KS-1 (T. KS-1). Although the high stability and activity of T. KS-1 alpha chaperonin provided advantages for our study, its high thermophilicity caused the difficulty in using various analytical methods. To resolve this problem, we tried to adapt T. KS-1 alpha chaperonin to moderate temperatures by mutations. The comparison of amino acid sequences between 26 thermophilic and 17 mesophilic chaperonins showed that three amino acid replacements are likely responsible for the difference of their optimal temperatures. We introduced three single mutations and also their double combinations into T. KS-1 alpha chaperonin.