Liposome-assisted activity of superoxide dismutase under oxidative stress

Hideto Nagami, Noriko Yoshimoto, Hiroshi Umakoshi, Toshinori Shimanouchi, Ryoichi Kuboi

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

A biological membrane is the front line of defense for cells against various environmental stresses such as heat and reactive oxygen species (ROS) and is expected to play an important role in the antioxidant system with antioxidant enzymes, similarly to its chaperone-like function in cooperation with heat shock proteins. The oxidative stress response of superoxide dismutase (SOD), which is known to catalyze the dismutation of O2 - to H2O2, was investigated in the presence of artificial membranes, liposomes, in order to obtain fundamental information on the biological ROS scavenging system. SOD lost its activity in the presence of H2O2 and was found to have two loops including one which contains an α-helix which presents the substrate O2 - to the activity center of SOD (Cu(II)). From circular dichroism analysis of SOD in the presence of H2O2, the contents of the α-helix in SOD were found to decrease in correspondence with the inactivation and conformational change of SOD, suggesting that the conformation of the α-helix loops affects SOD activity. In the presence of liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), SOD was not inactivated in the presence of H2O2 although the contents of its α-helix structure were decreased. The oxidized SOD was found to interact with the liposome surface under oxidative stress using dielectric dispersion analysis. Based on these results, a possible mechanism of SOD protection against ROS on liposomes was presented.

Original languageEnglish
Pages (from-to)423-428
Number of pages6
JournalJournal of Bioscience and Bioengineering
Volume99
Issue number4
DOIs
Publication statusPublished - Apr 2005
Externally publishedYes

Fingerprint

Oxidative stress
Liposomes
Superoxide Dismutase
Oxidative Stress
Reactive Oxygen Species
Antioxidants
Oxygen
Artificial Membranes
Biological membranes
Scavenging
Dichroism
Circular Dichroism
Heat-Shock Proteins
Conformations
Permittivity
Enzymes
Hot Temperature
Proteins
Membranes

Keywords

  • Liposome
  • Membrane stress biotechnology
  • Oxidative stress
  • Superoxide dismutase

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering

Cite this

Liposome-assisted activity of superoxide dismutase under oxidative stress. / Nagami, Hideto; Yoshimoto, Noriko; Umakoshi, Hiroshi; Shimanouchi, Toshinori; Kuboi, Ryoichi.

In: Journal of Bioscience and Bioengineering, Vol. 99, No. 4, 04.2005, p. 423-428.

Research output: Contribution to journalArticle

Nagami, Hideto ; Yoshimoto, Noriko ; Umakoshi, Hiroshi ; Shimanouchi, Toshinori ; Kuboi, Ryoichi. / Liposome-assisted activity of superoxide dismutase under oxidative stress. In: Journal of Bioscience and Bioengineering. 2005 ; Vol. 99, No. 4. pp. 423-428.
@article{47e7427a467c47baaa4571e3043ab1c3,
title = "Liposome-assisted activity of superoxide dismutase under oxidative stress",
abstract = "A biological membrane is the front line of defense for cells against various environmental stresses such as heat and reactive oxygen species (ROS) and is expected to play an important role in the antioxidant system with antioxidant enzymes, similarly to its chaperone-like function in cooperation with heat shock proteins. The oxidative stress response of superoxide dismutase (SOD), which is known to catalyze the dismutation of O2 - to H2O2, was investigated in the presence of artificial membranes, liposomes, in order to obtain fundamental information on the biological ROS scavenging system. SOD lost its activity in the presence of H2O2 and was found to have two loops including one which contains an α-helix which presents the substrate O2 - to the activity center of SOD (Cu(II)). From circular dichroism analysis of SOD in the presence of H2O2, the contents of the α-helix in SOD were found to decrease in correspondence with the inactivation and conformational change of SOD, suggesting that the conformation of the α-helix loops affects SOD activity. In the presence of liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), SOD was not inactivated in the presence of H2O2 although the contents of its α-helix structure were decreased. The oxidized SOD was found to interact with the liposome surface under oxidative stress using dielectric dispersion analysis. Based on these results, a possible mechanism of SOD protection against ROS on liposomes was presented.",
keywords = "Liposome, Membrane stress biotechnology, Oxidative stress, Superoxide dismutase",
author = "Hideto Nagami and Noriko Yoshimoto and Hiroshi Umakoshi and Toshinori Shimanouchi and Ryoichi Kuboi",
year = "2005",
month = "4",
doi = "10.1263/jbb.99.423",
language = "English",
volume = "99",
pages = "423--428",
journal = "Journal of Bioscience and Bioengineering",
issn = "1389-1723",
publisher = "The Society for Biotechnology, Japan",
number = "4",

}

TY - JOUR

T1 - Liposome-assisted activity of superoxide dismutase under oxidative stress

AU - Nagami, Hideto

AU - Yoshimoto, Noriko

AU - Umakoshi, Hiroshi

AU - Shimanouchi, Toshinori

AU - Kuboi, Ryoichi

PY - 2005/4

Y1 - 2005/4

N2 - A biological membrane is the front line of defense for cells against various environmental stresses such as heat and reactive oxygen species (ROS) and is expected to play an important role in the antioxidant system with antioxidant enzymes, similarly to its chaperone-like function in cooperation with heat shock proteins. The oxidative stress response of superoxide dismutase (SOD), which is known to catalyze the dismutation of O2 - to H2O2, was investigated in the presence of artificial membranes, liposomes, in order to obtain fundamental information on the biological ROS scavenging system. SOD lost its activity in the presence of H2O2 and was found to have two loops including one which contains an α-helix which presents the substrate O2 - to the activity center of SOD (Cu(II)). From circular dichroism analysis of SOD in the presence of H2O2, the contents of the α-helix in SOD were found to decrease in correspondence with the inactivation and conformational change of SOD, suggesting that the conformation of the α-helix loops affects SOD activity. In the presence of liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), SOD was not inactivated in the presence of H2O2 although the contents of its α-helix structure were decreased. The oxidized SOD was found to interact with the liposome surface under oxidative stress using dielectric dispersion analysis. Based on these results, a possible mechanism of SOD protection against ROS on liposomes was presented.

AB - A biological membrane is the front line of defense for cells against various environmental stresses such as heat and reactive oxygen species (ROS) and is expected to play an important role in the antioxidant system with antioxidant enzymes, similarly to its chaperone-like function in cooperation with heat shock proteins. The oxidative stress response of superoxide dismutase (SOD), which is known to catalyze the dismutation of O2 - to H2O2, was investigated in the presence of artificial membranes, liposomes, in order to obtain fundamental information on the biological ROS scavenging system. SOD lost its activity in the presence of H2O2 and was found to have two loops including one which contains an α-helix which presents the substrate O2 - to the activity center of SOD (Cu(II)). From circular dichroism analysis of SOD in the presence of H2O2, the contents of the α-helix in SOD were found to decrease in correspondence with the inactivation and conformational change of SOD, suggesting that the conformation of the α-helix loops affects SOD activity. In the presence of liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), SOD was not inactivated in the presence of H2O2 although the contents of its α-helix structure were decreased. The oxidized SOD was found to interact with the liposome surface under oxidative stress using dielectric dispersion analysis. Based on these results, a possible mechanism of SOD protection against ROS on liposomes was presented.

KW - Liposome

KW - Membrane stress biotechnology

KW - Oxidative stress

KW - Superoxide dismutase

UR - http://www.scopus.com/inward/record.url?scp=19644382137&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=19644382137&partnerID=8YFLogxK

U2 - 10.1263/jbb.99.423

DO - 10.1263/jbb.99.423

M3 - Article

C2 - 16233812

AN - SCOPUS:19644382137

VL - 99

SP - 423

EP - 428

JO - Journal of Bioscience and Bioengineering

JF - Journal of Bioscience and Bioengineering

SN - 1389-1723

IS - 4

ER -