Manganese superoxide dismutase promotes interaction of actin, S100A4 and Talin and enhances rat gastric tumor cell invasion

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Hiroko P. Indo, Hirofumi Matsui, Jing Chen, Haining Zhu, Clare Louise Hawkins, Michael J. Davies, Chontida Yarana, Daret K St Clair, Hideyuki J. Majima

It hasbeendemonstratedthatcancercells areunderhigh levels of oxidative stress and express high levels of Manganese superoxide dismutase (MnSOD) to protect themselves and support the anabolic metabolism needed for growth and cell motility. The aim of this study was to identify proteins that may have a correlation with invasion and redox regulation by mitochondrial reactive oxygen species (ROS). MnSOD scavenges superoxide anions generated from mitochondria and is an important regulator of cellular redox status. Oxidative posttranslational modification of cysteine residues is a key mechanism that regulates protein structure and function. We hypothesized that MnSOD regulates intracellular reduced thiol status and promotes cancer invasion. A proteomic thiol-labeling approach with 5-iodoacetamidofluores-cein was used to identify changes in intracellular reduced thiol-containing proteins. Our results demonstrate that overexpression of MnSOD maintained the major structural protein, actin, in a reduced state, and enhanced the invasion ability in gastric mucosal cancer cells, RGK1. We also found that the expression of Talin and S100A4 were increased in MnSOD-overexpressed RGK1 cells. Moreover, Talin bound not only with actin but also with S100A4, suggesting that the interaction of these proteins may, in part, contribute to the invasive ability of rat gastric cancer.

Original languageEnglish
JournalJournal of Clinical Biochemistry and Nutrition
Volume57
Issue number1
Pages (from-to)13-20
Number of pages8
ISSN0912-0009
DOIs
Publication statusPublished - 1 Jul 2015
Externally publishedYes

    Research areas

  • Actin binding protein, Cancer invasion, MnSOD, Reduced form of actin, ROS

ID: 152247521