Astragaloside IV attenuates high glucose-induced EMT by inhibiting the TGF-β/Smad pathway in renal proximal tubular epithelial cells.

Bioscience Reports
Ya-Ning WangYun-Fang Zhang

Abstract

In the present study, we examined the molecular mechanism of astragaloside IV (AS-IV) in high glucose (HG)-induced epithelial-to-mesenchymal transition (EMT) in renal proximal tubular epithelial cells (PTCs). NRK-52E cell viability and apoptosis were determined by the cell counting kit-8 (CCK-8) assay and flow cytometric analysis, respectively. Expressions of E-cadherin, N-cadherin, vimentin, and occludin were measured by Western blot, and those of E-cadherin and N-cadherin were additionally measured by immunofluorescence analysis. Transforming growth factor-β1 (TGF-β1) and α-smooth muscle actin (α-SMA) expressions were detected by quantitative real-time polymerase chain reaction (qRT-PCR) and Western blot. The expressions of Smad2, Smad3, phosphorylated-Smad2 (p-Smad2), and p-Smad3 were measured using Western blot. We found that AS-IV could recover NRK-52E cell viability and inhibit HG-induced cell apoptosis. TGF-β1, α-SMA, Smad2, Smad3, p-Smad2, and p-Smad3 expressions were decreased in the AS-IV-treated groups compared with the HG group. Moreover, the expressions of E-cadherin and occludin were remarkably up-regulated and those of N-cadherin and vimentin were down-regulated in the AS-IV-treated groups compared with the HG gr...Continue Reading

References

Apr 25, 2000·The EMBO Journal·J Massagué, D Wotton
Feb 16, 2002·Methods : a Companion to Methods in Enzymology·K J Livak, T D Schmittgen
Apr 24, 2003·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Jin H LiHui Y Lan
May 28, 2003·Biochemical and Biophysical Research Communications·Masaki FujimotoSeijiro Mori
Dec 16, 2004·American Journal of Physiology. Renal Physiology·Ho Jae HanMary Taub
Dec 31, 2008·Cell Research·Ying E Zhang
Jun 3, 2009·The Journal of Clinical Investigation·Hervé AcloqueM Angela Nieto
Nov 6, 2009·American Journal of Nephrology·Claire E Hills, Paul E Squires
Jan 22, 2010·American Journal of Physiology. Renal Physiology·Li ZhouHui Yao Lan
Jan 26, 2011·Annual Review of Pathology·Yashpal S KanwarSheldon Chen
Nov 5, 2011·American Journal of Kidney Diseases : the Official Journal of the National Kidney Foundation·David K PackhamHiddo J Lambers Heerspink
Jan 4, 2012·Clinical and Experimental Pharmacology & Physiology·Hui Yao Lan
Dec 12, 2012·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Yan-Xu ChangXiu-Mei Gao
Jan 18, 2013·Apoptosis : an International Journal on Programmed Cell Death·Dingkun GuiNiansong Wang
Nov 20, 2016·Cold Spring Harbor Perspectives in Biology·Ying E Zhang
May 19, 2018·Biomedicine & Pharmacotherapy = Biomédecine & Pharmacothérapie·Tiantian CaiXiaohui Zeng
Dec 13, 2018·American Journal of Physiology. Renal Physiology·Wei ZhangQingjuan Liu
Jan 8, 2019·Biochimica Et Biophysica Acta. Molecular Cell Research·Xiaoli YangXiang He

❮ Previous
Next ❯

Methods Mentioned

BETA
protein assay
electrophoresis
flow cytometry
GTPase

Software Mentioned

Pro Plus
SPSS
Image

Related Concepts

Related Feeds

Apoptosis

Apoptosis is a specific process that leads to programmed cell death through the activation of an evolutionary conserved intracellular pathway leading to pathognomic cellular changes distinct from cellular necrosis

Cadherins and Catenins

Cadherins (named for "calcium-dependent adhesion") are a type of cell adhesion molecule (CAM) that is important in the formation of adherens junctions to bind cells with each other. Catenins are a family of proteins found in complexes with cadherin cell adhesion molecules of animal cells: alpha-catenin can bind to β-catenin and can also bind actin. β-catenin binds the cytoplasmic domain of some cadherins. Discover the latest research on cadherins and catenins here.