›› 2018, Vol. 38 ›› Issue (9): 1013-.doi: 10.3969/j.issn.1674-8115.2018.09.003

• Original article (Basic research) • Previous Articles     Next Articles

Rho-associated coiled coil protein kinase 1 involved in amyloid β-protein-induced damage in primary neurons of rats

HU Yong-Bo1,2, REN Ru-Jing1, WANG Gang1   

  1. 1. Department of Neurology, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China; 2. Department of Pharmacology and Chemical Biology, Shanghai Jiao Tong University College of Basic Medical Sciences, Shanghai 200025, China
  • Online:2018-09-28 Published:2018-10-15
  • Supported by:
    National Natural Science Foundation of China, 81671043; Shanghai Pujiang Program, 15PJ1405400; the "Dawn" Program of Shanghai Education Commission, 16SG15; Shanghai Municipal Education Commission— Gaofeng Clinical Medicine Support, 20172001

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Abstract: Objective · To investigate the role of Rho-associated coiled coil protein kinase 1 (ROCK1) in amyloid β-protein (Aβ) induced damage of rat hippocampal neurons. Methods · The rat primary neurons were treated with Aβ40 oligopeptides to establish a neurotoxicity model. Western blotting was used to detect the protein of ROCK1. Its activity was detectedthe kit. Confocal laser scanning was used to observe the calcium signal in neurons, and apoptosis of neurons was detectedTUNEL assay. Y-27632, an inhibitor of ROCK1, was added into the culture medium into observe its effect on Aβ40. Results · Aβ40 (10 μmol/L) could significantly induce calcium overload, increase ROCK1 and activity, and promote apoptosis in primary neurons. Furthermore, ROCK1 inhibitor could decrease all the effect inducedAβ40. Conclusion · ROCK1 is involved in both Aβinduced neuronal calcium overload and neurotoxicity, and ROCK1 inhibitor can antagonize the toxic effects of Aβ.

Key words: Alzheimers disease, Rho-associated coiled coil protein kinase 1 (ROCK1), amyloid β-protein (Aβ), calcium overload

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