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A short report: PAMM, a novel antioxidant protein, induced by oxidative stress.

Xu Y, Morse LR, da Silva RA, Wang D, Battaglino RA - Redox Biol (2015)

Bottom Line: These results indicate that M-CSF-induced PAMM expression is mediated by Akt phosphorylation.Our data also suggest that estrogen-induced PAMM expression is mediated by phosphorylation of Akt.These findings point to PAMM as a potential candidate for Akt-mediated protection against oxidative stress.

View Article: PubMed Central - PubMed

Affiliation: Department of Mineralized Tissue Biology, The Forsyth Institute, 245 First Street, Cambridge, MA 02142, USA; School of Pharmaceutical Science, Kunming Medical University, 1168 West Chunrong Road, Kunming 650500, China. Electronic address: yxu@forsyth.org.

No MeSH data available.


Related in: MedlinePlus

M-CSF stimulation of PAMM expression requires Akt phosphorylation. Human CD14+ PBMCs were stimulated with M-CSF (+) and Wortmannin (W) or Rapamycin (R) for 4 days. M-CSF induced PAMM expression and phosphorylation of Akt (Ser 473). Wortmannin and Rapamycin, on the other hand, blocked M-CSF-induced Akt phosphorylation and PAMM expression. (−): Untreated control cells. (+): Cells stimulated with 150 ng/mL M-CSF. W: Cells stimulated with M-CSF and 100 nM Wortmannin. R: Cells stimulated with M-CSF and 100 nM Rapamycin.
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f0015: M-CSF stimulation of PAMM expression requires Akt phosphorylation. Human CD14+ PBMCs were stimulated with M-CSF (+) and Wortmannin (W) or Rapamycin (R) for 4 days. M-CSF induced PAMM expression and phosphorylation of Akt (Ser 473). Wortmannin and Rapamycin, on the other hand, blocked M-CSF-induced Akt phosphorylation and PAMM expression. (−): Untreated control cells. (+): Cells stimulated with 150 ng/mL M-CSF. W: Cells stimulated with M-CSF and 100 nM Wortmannin. R: Cells stimulated with M-CSF and 100 nM Rapamycin.

Mentions: We have previously shown that M-CSF induces PAMM expression in cultured CD14+ peripheral blood mononuclear cells (PBMCs) [12]. We next determined if M-CSF stimulation of PAMM expression required Akt phosphorylation, which requires PI3Kinase activity. We stimulated human CD14+ PBMCs with M-CSF and determined PAMM abundance and phosphorylated Akt in the presence of Wortmannin or Rapamycin. Wortmannin is a specific PI3Kinase inhibitor and Rapamycin is an inhibitor of the Akt/mTOR pathway, that acts downstream of Akt. We found that both Wortmannin and Rapamycin blocked M-CSF induced PAMM expression via inhibited phosphorylation of Akt (Fig. 3).


A short report: PAMM, a novel antioxidant protein, induced by oxidative stress.

Xu Y, Morse LR, da Silva RA, Wang D, Battaglino RA - Redox Biol (2015)

M-CSF stimulation of PAMM expression requires Akt phosphorylation. Human CD14+ PBMCs were stimulated with M-CSF (+) and Wortmannin (W) or Rapamycin (R) for 4 days. M-CSF induced PAMM expression and phosphorylation of Akt (Ser 473). Wortmannin and Rapamycin, on the other hand, blocked M-CSF-induced Akt phosphorylation and PAMM expression. (−): Untreated control cells. (+): Cells stimulated with 150 ng/mL M-CSF. W: Cells stimulated with M-CSF and 100 nM Wortmannin. R: Cells stimulated with M-CSF and 100 nM Rapamycin.
© Copyright Policy - CC BY-NC-ND
Related In: Results  -  Collection

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Show All Figures
getmorefigures.php?uid=PMC4588419&req=5

f0015: M-CSF stimulation of PAMM expression requires Akt phosphorylation. Human CD14+ PBMCs were stimulated with M-CSF (+) and Wortmannin (W) or Rapamycin (R) for 4 days. M-CSF induced PAMM expression and phosphorylation of Akt (Ser 473). Wortmannin and Rapamycin, on the other hand, blocked M-CSF-induced Akt phosphorylation and PAMM expression. (−): Untreated control cells. (+): Cells stimulated with 150 ng/mL M-CSF. W: Cells stimulated with M-CSF and 100 nM Wortmannin. R: Cells stimulated with M-CSF and 100 nM Rapamycin.
Mentions: We have previously shown that M-CSF induces PAMM expression in cultured CD14+ peripheral blood mononuclear cells (PBMCs) [12]. We next determined if M-CSF stimulation of PAMM expression required Akt phosphorylation, which requires PI3Kinase activity. We stimulated human CD14+ PBMCs with M-CSF and determined PAMM abundance and phosphorylated Akt in the presence of Wortmannin or Rapamycin. Wortmannin is a specific PI3Kinase inhibitor and Rapamycin is an inhibitor of the Akt/mTOR pathway, that acts downstream of Akt. We found that both Wortmannin and Rapamycin blocked M-CSF induced PAMM expression via inhibited phosphorylation of Akt (Fig. 3).

Bottom Line: These results indicate that M-CSF-induced PAMM expression is mediated by Akt phosphorylation.Our data also suggest that estrogen-induced PAMM expression is mediated by phosphorylation of Akt.These findings point to PAMM as a potential candidate for Akt-mediated protection against oxidative stress.

View Article: PubMed Central - PubMed

Affiliation: Department of Mineralized Tissue Biology, The Forsyth Institute, 245 First Street, Cambridge, MA 02142, USA; School of Pharmaceutical Science, Kunming Medical University, 1168 West Chunrong Road, Kunming 650500, China. Electronic address: yxu@forsyth.org.

No MeSH data available.


Related in: MedlinePlus