Affordable Access

deepdyve-link
Publisher Website

Tat-HSP70 protects neurons from oxidative damage in the NSC34 cells and ischemic damage in the ventral horn of rabbit spinal cord.

Authors
  • Kim, Woosuk1
  • Kwon, Hyun Jung2
  • Jung, Hyo Young1
  • Yoo, Dae Young3
  • Moon, Seung Myung4
  • Kim, Dae Won5
  • Hwang, In Koo6
  • 1 Department of Anatomy and Cell Biology, College of Veterinary Medicine, and Research Institute for Veterinary Science, Seoul National University, Seoul, 08826, South Korea. , (North Korea)
  • 2 Department of Biochemistry and Molecular Biology, Research Institute of Oral Sciences, College of Dentistry, Gangneung-Wonju National University, Gangneung, 25457, South Korea. , (North Korea)
  • 3 Department of Anatomy, College of Medicine, Soonchunhyang University, Cheonan, Chungcheongnam, 31151, South Korea. , (North Korea)
  • 4 Department of Neurosurgery, Dongtan Sacred Heart Hospital, College of Medicine, Hallym University, Hwaseong, 18450, South Korea; Research Institute for Complementary & Alternative Medicine, Hallym University, Chuncheon, 24253, South Korea. , (North Korea)
  • 5 Department of Biochemistry and Molecular Biology, Research Institute of Oral Sciences, College of Dentistry, Gangneung-Wonju National University, Gangneung, 25457, South Korea. Electronic address: [email protected] , (North Korea)
  • 6 Department of Anatomy and Cell Biology, College of Veterinary Medicine, and Research Institute for Veterinary Science, Seoul National University, Seoul, 08826, South Korea. Electronic address: [email protected] , (North Korea)
Type
Published Article
Journal
Neurochemistry international
Publication Date
Oct 01, 2019
Volume
129
Pages
104477–104477
Identifiers
DOI: 10.1016/j.neuint.2019.104477
PMID: 31145969
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Heat shock protein 70 (HSP70) is an ATP-dependent molecular chaperone, and it has been shown that its levels increase after exposure to various types of stress, including ischemia. In the present study, we investigated the effects of HSP70 against H2O2-induced neuronal stress in NSC34 cells and against spinal cord ischemia in rabbits. Tat-HSP70 proteins facilitated the intracellular delivery of HSP70 into the NSC34 cells and enabled them to cross the blood-brain barrier in the rabbit spinal cord. Tat-HSP70 was effectively transduced into NSC34 cells in a concentration- and time-dependent manner, while control-HSP70 protein could not be delivered intracellularly at any concentration or time after treatment. Treatment with Tat-HSP70 reduced the generation of reactive oxygen species and cell death induced by H2O2, while the control-HSP70 did not show any significant effect on the NSC34 cells exposed to H2O2. In rabbit spinal cord, the administration of Tat-HSP70 showed significant amelioration of neurological defects and neuronal death in the ventral horn of spinal cord. In addition, Tat-HSP70 treatment significantly reduced lipid peroxidation and increased Cu, Zn-superoxide dismutase activities in the spinal cord, but glutathione peroxidase and Mn-superoxide dismutase activities remained unchanged. These results suggest that Tat-HSP70, not control-HSP70, decreases cell damage by reducing oxidative stress in NSC34 cells and rabbit spinal cord, and it can be employed for the reduction of neuronal damage caused after spinal cord ischemia. Copyright © 2019 Elsevier Ltd. All rights reserved.

Report this publication

Statistics

Seen <100 times