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Serum- and glucocorticoid-regulated protein kinase 3 overexpression promotes tumor development and aggression in breast cancer cells.

Sun X, Liu X, Liu BO, Li S, Zhang D, Guo H - Oncol Lett (2016)

Bottom Line: SGK3 levels were significantly higher in breast cancer samples compared with adjacent noncancerous and normal tissues.Cell growth curves revealed increased proliferation and decreased apoptosis in SGK3-overexpressing cells.Phosphorylation of GSK-3β, which is downstream in the phosphoinositide 3-kinase signaling pathway, was activated by SGK3 overexpression. β-catenin phosphorylation did not differ between the SGK3-overexpressing and non-SGK3-overexpressing cells.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry, Qiqihar Medical University, Qiqihar, Heilongjiang 161006, P.R. China.

ABSTRACT

Serum- and glucocorticoid-regulated protein kinase 3 (SGK3) is critical for tumor survival, proliferation and invasion. In the present study we evaluated SGK3 expression in breast tissues and investigated alterations in SGK3 levels in tumor multiplication, progression and apoptosis. Tissue microarray analyses were performed to examine SGK3 expression in breast cancer samples, as well as in adjacent noncancerous and normal tissues. The pEGFP-N1-SGK3 plasmid was transfected into MDA-MB-231 cells to generate SGK3-overexpressing cells. Cell growth assays, colony formation assays, cell cycle analyses, horizontal and vertical migration tests, reverse transcription-polymerase chain reaction and western blot assays were employed to investigate the biological behavior of SGK3-overexpressing cells. SGK3 levels were significantly higher in breast cancer samples compared with adjacent noncancerous and normal tissues. Cell growth curves revealed increased proliferation and decreased apoptosis in SGK3-overexpressing cells. SGK3-overexpressing cells also demonstrated enhanced invasion and migration abilities. SGK3-overexpressing cells had high levels of an apoptosis-related gene (bcl-xl) and invasion-related genes (mmp2 and mmp9), and decreased levels of an anti-apoptosis gene (bad). Phosphorylation of GSK-3β, which is downstream in the phosphoinositide 3-kinase signaling pathway, was activated by SGK3 overexpression. β-catenin phosphorylation did not differ between the SGK3-overexpressing and non-SGK3-overexpressing cells. SGK3 overexpression induces GSK-3β phosphorylation, enhancing apoptosis- and invasion-related genes and proteins and thereby leading to tumor development and aggression in breast cancer cells.

No MeSH data available.


Related in: MedlinePlus

(A) Effect of serum- and glucocorticoid-regulated protein kinase 3 (SGK3) overexpression on GSK3β phosphorylation; #∇P<0.01. (B) Effect of SGK3 overexpression on β-catenin phosphorylation. # and * indicate comparison between groups SGK3 and 231; ∇ and ♦ indicate comparison between groups SGK3 and N1.
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f5-ol-0-0-4638: (A) Effect of serum- and glucocorticoid-regulated protein kinase 3 (SGK3) overexpression on GSK3β phosphorylation; #∇P<0.01. (B) Effect of SGK3 overexpression on β-catenin phosphorylation. # and * indicate comparison between groups SGK3 and 231; ∇ and ♦ indicate comparison between groups SGK3 and N1.

Mentions: We next examined the expression of phospho-GSK3β and phospho-β-catenin (Fig. 5A and B). The grayscale value of phospho-GSK3β demonstrated that expression was higher in the SGK3 group cells (P<0.01), whereas no differences were detected between N1 and 231 group cells (P>0.05). In contrast, western blot analyses revealed that SGK3-overexpressing cells did not differ in phospho-β-catenin levels compared with the other two groups (P>0.05). Thus, SGK3 overexpression did not contribute to β-catenin phosphorylation.


Serum- and glucocorticoid-regulated protein kinase 3 overexpression promotes tumor development and aggression in breast cancer cells.

Sun X, Liu X, Liu BO, Li S, Zhang D, Guo H - Oncol Lett (2016)

(A) Effect of serum- and glucocorticoid-regulated protein kinase 3 (SGK3) overexpression on GSK3β phosphorylation; #∇P<0.01. (B) Effect of SGK3 overexpression on β-catenin phosphorylation. # and * indicate comparison between groups SGK3 and 231; ∇ and ♦ indicate comparison between groups SGK3 and N1.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4940681&req=5

f5-ol-0-0-4638: (A) Effect of serum- and glucocorticoid-regulated protein kinase 3 (SGK3) overexpression on GSK3β phosphorylation; #∇P<0.01. (B) Effect of SGK3 overexpression on β-catenin phosphorylation. # and * indicate comparison between groups SGK3 and 231; ∇ and ♦ indicate comparison between groups SGK3 and N1.
Mentions: We next examined the expression of phospho-GSK3β and phospho-β-catenin (Fig. 5A and B). The grayscale value of phospho-GSK3β demonstrated that expression was higher in the SGK3 group cells (P<0.01), whereas no differences were detected between N1 and 231 group cells (P>0.05). In contrast, western blot analyses revealed that SGK3-overexpressing cells did not differ in phospho-β-catenin levels compared with the other two groups (P>0.05). Thus, SGK3 overexpression did not contribute to β-catenin phosphorylation.

Bottom Line: SGK3 levels were significantly higher in breast cancer samples compared with adjacent noncancerous and normal tissues.Cell growth curves revealed increased proliferation and decreased apoptosis in SGK3-overexpressing cells.Phosphorylation of GSK-3β, which is downstream in the phosphoinositide 3-kinase signaling pathway, was activated by SGK3 overexpression. β-catenin phosphorylation did not differ between the SGK3-overexpressing and non-SGK3-overexpressing cells.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry, Qiqihar Medical University, Qiqihar, Heilongjiang 161006, P.R. China.

ABSTRACT

Serum- and glucocorticoid-regulated protein kinase 3 (SGK3) is critical for tumor survival, proliferation and invasion. In the present study we evaluated SGK3 expression in breast tissues and investigated alterations in SGK3 levels in tumor multiplication, progression and apoptosis. Tissue microarray analyses were performed to examine SGK3 expression in breast cancer samples, as well as in adjacent noncancerous and normal tissues. The pEGFP-N1-SGK3 plasmid was transfected into MDA-MB-231 cells to generate SGK3-overexpressing cells. Cell growth assays, colony formation assays, cell cycle analyses, horizontal and vertical migration tests, reverse transcription-polymerase chain reaction and western blot assays were employed to investigate the biological behavior of SGK3-overexpressing cells. SGK3 levels were significantly higher in breast cancer samples compared with adjacent noncancerous and normal tissues. Cell growth curves revealed increased proliferation and decreased apoptosis in SGK3-overexpressing cells. SGK3-overexpressing cells also demonstrated enhanced invasion and migration abilities. SGK3-overexpressing cells had high levels of an apoptosis-related gene (bcl-xl) and invasion-related genes (mmp2 and mmp9), and decreased levels of an anti-apoptosis gene (bad). Phosphorylation of GSK-3β, which is downstream in the phosphoinositide 3-kinase signaling pathway, was activated by SGK3 overexpression. β-catenin phosphorylation did not differ between the SGK3-overexpressing and non-SGK3-overexpressing cells. SGK3 overexpression induces GSK-3β phosphorylation, enhancing apoptosis- and invasion-related genes and proteins and thereby leading to tumor development and aggression in breast cancer cells.

No MeSH data available.


Related in: MedlinePlus