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• W2035678698 abstract "Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FLSulfiredoxin (Srx) is an antioxidant protein that reduces over-oxidized catalytic cysteine residues of peroxiredoxins I-IV and catalyzes reduction of some S-glutathionylated proteins. We previously showed that Srx plays a role in cell migration and interacts with non-muscle myosin IIA (NM IIA; Bowers et al AACR 2010). The purpose of the present study was to extend our knowledge of the effect of Srx on cell adhesion and migration. Immunoprecipitation of Srx from non-small lung cancer (A549 cells) revealed a number of Srx-interacting proteins including NM IIA and S100A4. NM IIA plays a central role in the control of cell adhesion and migration, and S100A4 is a key regulator of NM IIA activity that is linked to cancer metastases. Adhesion assays showed that A549 cells over-expressing Srx have reduced adhesion to fibronectin-coated dishes and decreased levels of Tyr397-phosphorylated focal adhesion kinase (p-FAK). Conversely, Srx knockdown by shRNA increased A549 cell adhesion to fibronectin and p-FAK levels. Srx over-expression in A549 cells increased actin stress fiber formation and altered focal adhesion formation. Depletion of Srx in A549 cells resulted in decreased actin stress fiber formation and also altered sites of cell:extracellular matrix adhesion. In silico molecular modeling of an Srx-S100A4 homodimer complex showed close proximity (∼13A) of the single Cys99 of Srx to the Cys85 of S100A4. The calculated binding constant for the Srx-S100A4 interaction indicated reasonable affinity (KD∼ 62 nM). This affinity was not dependent upon disulfide bonding, since mutation of Srx residue Cys99 to Ser resulted in increased affinity (KD ∼22 nM). In vitro S-glutathionylation of Cys85 of S100A4 markedly increased its affinity to Srx (KD∼4 nM), but had no effect with the inactive Srx C99S mutant. Srx over-expression produced a doubling of the basal cellular level of free Ca2+ suggesting that the protein:protein interactions altered the capacity of S100A4 to bind Ca2+. Our data show that Srx may play important role in S100A4-mediated cancer cell cytoskeletal remodeling and motility and could potentially be a target for development of specific anticancer therapies.Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 102nd Annual Meeting of the American Association for Cancer Research; 2011 Apr 2-6; Orlando, FL. Philadelphia (PA): AACR; Cancer Res 2011;71(8 Suppl):Abstract nr 2077. doi:10.1158/1538-7445.AM2011-2077" @default.
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• W2035678698 title "Abstract 2077: Interactions between sulfiredoxin, S100A4 and non-muscle myosin IIA regulate cancer cell adhesion and motility" @default.
• W2035678698 doi "https://doi.org/10.1158/1538-7445.am2011-2077" @default.
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