Jangampalli Adi Pradeepkiran , Sudhir Kshirsagar , Rainier Vladlen Alvir , Philip Irwin Motakatla , P. Hemachandra Reddy
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引用次数: 0
Abstract
Tau hyperphosphorylation was the initial recognized pathogenic tau protein post-translational modification in Alzheimer's disease. In our present research, treatment of diethyl (3,4-dihydroxy phenethylamine) (quinolin-4-yl) methylphosphonate (DDQ) HT22 cells with mTau transfected HT22 cells decreased the phosphorylation of tau at Ser202, Thr205, p-ERK, and increased LC3B, and TOM20 as detected by Western blots. Moreover, DDQ p-tau and p-ERK inhibition of phosphorylation also contributed to significant mitochondrial protection in the presence of mTau. Taken together, for the first time, we found that DDQ is involved in phosphorylation inhibition to restore the mitophagy, which may relate to the Sirt3 activation of the ERK-CREB mediated pathway.
期刊介绍:
BBA Molecular Basis of Disease addresses the biochemistry and molecular genetics of disease processes and models of human disease. This journal covers aspects of aging, cancer, metabolic-, neurological-, and immunological-based disease. Manuscripts focused on using animal models to elucidate biochemical and mechanistic insight in each of these conditions, are particularly encouraged. Manuscripts should emphasize the underlying mechanisms of disease pathways and provide novel contributions to the understanding and/or treatment of these disorders. Highly descriptive and method development submissions may be declined without full review. The submission of uninvited reviews to BBA - Molecular Basis of Disease is strongly discouraged, and any such uninvited review should be accompanied by a coverletter outlining the compelling reasons why the review should be considered.