Substrate stiffness promotes latent TGF-β1 activation in hepatocellular carcinoma

Biochem Biophys Res Commun. 2017 Jan 29;483(1):553-558. doi: 10.1016/j.bbrc.2016.12.107. Epub 2016 Dec 24.

Abstract

Hepatocellular carcinoma (HCC) was usually coupled with increased stiffness of the extracellular matrix (ECM) and elevated level of transforming growth factor-β1 (TGF-β1). However, the mechanism by which substrate rigidity modulated TGF-β1 signaling transduction remained unknown. This paper investigated the molecular mechanism of how matrix stiffness regulating TGF-β1 signaling in HCC cells. By means of stiffness tunable collagen I-coated polyacrylamide (PA) gels, we found that the expressions of β1 integrin, p-FAK Y397 and p-Smad2 upregulated on stiffer gels as well as the content of TGF-β1 in culture media of HCC cells, which were inhibited by RGD blocking peptides, Y-27632 (ROCK inhibitor) or Blebbistatin (myosin II inhibitor). Cellular traction force was also significantly higher when plated on stiffer substrates but dramatically decreased after treatment with Y-27632 or Blebbistatin. Furthermore, the upregulation of p-Smad2 in the HCC cells on stiffer PA gels induced by exogenetic latent TGF-β1 was downregulated in the presence of RGD peptides. The nuclear translocation of Smad2 induced by latent TGF-β1 was inhibited by Y-27632 or Blebbistatin. Our results suggested that the extracellular matrix stiffness regulated latent TGF-β1 activation by cytoskeletal tension in HCC cells, showing that matrix stiffness was a key regulator involving the TGF-β1 activity in HCC cells. The current study presented a mechanism of how hepatocirrhosis developed into liver cancer.

Keywords: Hepatocellular carcinoma; Substrate stiffness; Traction forces; Transforming growth factor β1; β1 integrin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amides / chemistry
  • Carcinoma, Hepatocellular / metabolism*
  • Cell Line, Tumor
  • Cytoskeleton / metabolism
  • Extracellular Matrix / metabolism*
  • Focal Adhesion Protein-Tyrosine Kinases / metabolism
  • Gene Expression Regulation, Neoplastic*
  • Hep G2 Cells
  • Heterocyclic Compounds, 4 or More Rings / chemistry
  • Humans
  • Integrin beta1 / metabolism
  • Liver Neoplasms / metabolism*
  • Oligopeptides / chemistry
  • Protein Binding
  • Pyridines / chemistry
  • Signal Transduction
  • Smad2 Protein / metabolism*
  • Transforming Growth Factor beta1 / metabolism*
  • Up-Regulation
  • rho GTP-Binding Proteins / metabolism

Substances

  • Amides
  • Heterocyclic Compounds, 4 or More Rings
  • Integrin beta1
  • Oligopeptides
  • Pyridines
  • SMAD2 protein, human
  • Smad2 Protein
  • Transforming Growth Factor beta1
  • Y 27632
  • blebbistatin
  • arginyl-glycyl-aspartic acid
  • Focal Adhesion Protein-Tyrosine Kinases
  • rho GTP-Binding Proteins