ScienceDaily (Aug. 2, 2010) — A team of scientists at the University of California, Davis and the University of Auckland has discovered that neuroglobin may protect against Alzheimer’s disease by preventing brain neurons from dying in response to natural stress. Neuroglobin protects cells from stroke damage, amyloid toxicity and injury due to lack of oxygen. Neuroglobin occurs in various regions of the brain and at particularly high levels in neurons. Recent studies have hinted that neuroglobin protects cells by maintaining the function of mitochondria and regulating the concentration of important chemicals in the cell. However, the exact mechanisms by which neuroglobin protects cells from dying a natural death has, until now, remained unclear. Click here for more on the research that resulted in these insights.
University of California Irvine biologists Robert Steele and Hans Bode, along with nine other UCI scientists and an international team of researchers, have describes the genome sequence of Hydra, an organism that continues to advance research on regeneration, stem cells and patterning.
The team discovered Hydra to have about the same number of genes as humans, sharing many of the same ones. Surprisingly, they also found genes linked with Huntington’s disease and with the beta-amyloid plaque formation seen in Alzheimer’s disease — two areas in which UCI has traditionally strong research programs — suggesting the possible use of Hydra as a research model for these two diseases. Report of their discoveries was reported March 14 in NATURE.
A novel intracellular signaling pathway mediated FE65 and APP
Tadashi Nakaya, Ph.D.
Head of Laboratory, Hokkaido University
Graduate School of Pharmaceutical Sciences
10:00 am – 11:00 am, Monday, September 15, 2008
15th Floor Conference room, WRB
Recommended Review Article:
McLoughlin, D.M.; & Miller, C.C.J. 2008. The FE65 proteins and Alzheimer’s disease. Journal of Neuroscience Research. 86(4):744-754. (please order copies from the Markus Library)
Nakaya, T.; Kawai, T.; & Suzuki, T. 2008. Regulation of FE65 Nuclear Translocation and Function by Amyloid β-Protein Precursor in Osmotically Stressed Cells. The Journal of Biological Chemistry. 283(27):19119-19131.
Müller, T.; et al. 2008. The amyloid precursor protein intracellular domain (AICD) as modulator of gene expression, apoptosis, and cytoskeletal dynamics—Relevance for Alzheimer’s disease. Progress in Neurology. 85(4):393-406.
Nakaya, T.; & Suzuki, T. 2006. Role of APP phosphorylation in FE65-dependent gene transactivation mediated by AICD. Genes to Cells. 11(6):633-645.