Publications by authors named "Chitose Nakao"

Stathmin/oncoprotein 18, a protein that regulates microtubule dynamics, is highly expressed in a number of tumors including leukemia, lymphoma, neuroblastoma, breast, ovarian, and prostate cancers. High stathmin levels have been associated with the development of resistance to the widely used anti-cancer drug taxol ((®)Taxol, paclitaxel). The mechanisms of stathmin-mediated taxol resistance are not well-understood at the molecular level.

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The pathophysiology of diabetes includes oxidative stress and impaired heat shock protein (HSP) expression. We studied the effects of alpha-lipoic acid (LA) supplementation for 8 weeks and acute exercise on HSP60 expression and the oxidative stress marker 4-hydroxynonenal adducts (4-HNE) in streptozotocin-induced diabetic (SID) and nondiabetic control rats. Diabetes was associated with decreased HSP60 in the heart and increased levels of HSP60 and 4-HNE in the liver.

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Mannich bases interact with cellular thiols and inactivate thioredoxin reductase. In this study, the effects of cytotoxic mono-Mannich bases 2, 3 and cyclic Mannich base C1 on the expression of cytoprotective heat shock proteins (HSC70 and GRP75) and on levels of thioredoxin (TRX) and glutaredoxin (GRX) were investigated in Jurkat cells. Cells were exposed to the compounds for 24 h in cell culture medium with 1% FBS.

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Acute exercise induces oxidative stress and heat shock protein (HSP) expression. Information on the protection of stress proteins against oxidant insult and muscle damage during moderate exercise is scanty. We aimed to show how a single bout of moderate exercise affects the markers of oxidative stress and heat shock factor-1 (HSF1; the transcriptional regulator of HSP synthesis), and HSP70, HSP90 and glucose-regulated protein (GRP75) expression in horses.

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Strenuous exercise induces oxidative stress and modification of intracellular proteins. Exercise training, however, upregulates endogenous antioxidant defenses and heat shock protein (HSP) expression. In diabetes, perturbations in the endogenous antioxidant and HSP protection have been reported.

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RB3 is a neuron-specific homologue of the SCG10/stathmin family proteins, possessing a unique N-terminal membrane-associated domain and the stathmin-like domain at the C terminus, which promotes microtubule (MT) catastrophe and/or tubulin sequestering. We examined herein the contribution of the N-terminal subdomain of RB3 to the regulation of MT dynamics. To begin with, we determined the effects of full-length (RB3-f) and short truncated (RB3-s) forms of RB3 on the polymerization of MT in vitro.

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Human extracellular superoxide dismutase (EC-SOD) was purified to homogeneity from lung tissue and the nature of the binding of heparin to EC-SOD was investigated. The enzyme was purified using three column chromatographic steps, and 127 microg of purified EC-SOD was obtained. A specific anti-human EC-SOD antibody was obtained by immunization with the purified enzyme.

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