Down-regulation of 14-3-3 Zeta Inhibits TGF-β1-Induced Actomyosin Contraction in Human Trabecular Meshwork Cells Through RhoA Signaling Pathway

Invest Ophthalmol Vis Sci. 2016 Feb;57(2):719-30. doi: 10.1167/iovs.15-17438.

Abstract

Purpose: The aim of this study was to describe the expression and distribution of 14-3-3 zeta in trabecular meshwork (TM) cells and its regulatory role in the actomyosin system.

Methods: The expression of 14-3-3 zeta was detected using Western blot analysis, RT-PCR, and immunofluorescence staining. TGF-β1 was used to induce cell contraction. Changes in the levels of 14-3-3 zeta, total RhoA, and the phosphorylation of myosin light chain (MLC) and cofilin were determined using Western blot analysis. The effects of 14-3-3 zeta knockdown on the actin cytoskeleton and focal adhesion were determined using immunofluorescence. The mRNA levels of fibronectin and collagen I and III were examined using quantitative RT-PCR. The contraction of TM cells was detected using collagen gel contraction (CGC) assays. The activation of the RhoA pathway was analyzed using a specific kit.

Results: The 14-3-3 zeta protein was highly expressed in TM cells. Down-regulation of 14-3-3 zeta resulted in the following: a decrease in the phosphorylation of both MLC and cofilin, a decrease in the formation of stress fibers and focal adhesion, alteration of the mRNA composition of the extracellular matrix (ECM), and the inhibition of TGF-β1-induced cell contraction. In addition, silencing of 14-3-3 zeta directly decreased total RhoA levels in TM cells.

Conclusions: Collectively, our data suggest that 14-3-3 zeta plays a crucial role in regulating cytoskeletal structures, ECM homeostasis, and TGF-β1-induced contraction in TM cells by acting through the RhoA signaling pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 14-3-3 Proteins / biosynthesis*
  • 14-3-3 Proteins / genetics
  • 14-3-3 Proteins / metabolism
  • Actin Cytoskeleton / metabolism
  • Actins / metabolism
  • Actomyosin / metabolism*
  • Aqueous Humor / metabolism
  • Cell Adhesion / physiology
  • Cells, Cultured
  • Cofilin 1 / metabolism
  • Collagen / metabolism
  • Cytoskeleton / metabolism
  • Down-Regulation
  • Extracellular Matrix / metabolism
  • Fibronectins / metabolism
  • Focal Adhesions / metabolism
  • Gene Knockdown Techniques
  • Humans
  • Myosin Light Chains / metabolism
  • Phosphorylation
  • Signal Transduction
  • Trabecular Meshwork / cytology
  • Trabecular Meshwork / metabolism*
  • Transforming Growth Factor beta1 / antagonists & inhibitors
  • Transforming Growth Factor beta1 / metabolism
  • Transforming Growth Factor beta1 / pharmacology*
  • rhoA GTP-Binding Protein / metabolism

Substances

  • 14-3-3 Proteins
  • Actins
  • CFL1 protein, human
  • Cofilin 1
  • Fibronectins
  • Myosin Light Chains
  • Transforming Growth Factor beta1
  • YWHAZ protein, human
  • Collagen
  • Actomyosin
  • rhoA GTP-Binding Protein