(-)-Epigallocatechin-3-gallate stimulates myogenic differentiation through TAZ activation

Biochem Biophys Res Commun. 2017 Apr 29;486(2):378-384. doi: 10.1016/j.bbrc.2017.03.049. Epub 2017 Mar 14.

Abstract

Muscle loss is a typical process of aging. Green tea consumption is known to slow down the progress of aging. Their underlying mechanisms, however, remain largely unknown. In this study, we investigated the effect of (-)-epigallocatechin-3-gallate (EGCG), a polyphenolic compound of green tea, on myogenic differentiation and found that EGCG significantly increases myogenic differentiation. After EGCG treatment, the expression of myogenic marker genes, such as myosin heavy chain, are increased through activation of TAZ, a transcriptional coactivator with a PDZ-binding motif. TAZ-knockdown does not stimulate EGCG-induced myogenic differentiation. EGCG facilitates the interaction between TAZ and MyoD, which stimulates MyoD-mediated gene transcription. EGCG induces nuclear localization of TAZ through the dephosphorylation of TAZ at its Ser89 residue, which relieves 14-3-3 binding in the cytosol. Interestingly, inactivation of Lats kinase is observed after EGCG treatment, which is responsible for the production of dephosphorylated TAZ. Together, these results suggest that EGCG induces myogenic differentiation through TAZ, suggesting that TAZ plays an important role in EGCG induced muscle regeneration.

Keywords: Catechins; Myogenesis; Satellite cells; TAZ.

MeSH terms

  • 14-3-3 Proteins / genetics
  • 14-3-3 Proteins / metabolism
  • Animals
  • Catechin / analogs & derivatives*
  • Catechin / pharmacology
  • Cell Differentiation / drug effects*
  • Cell Line
  • Gene Expression Regulation
  • HEK293 Cells
  • Humans
  • Mice
  • Mice, Inbred C57BL
  • MyoD Protein / genetics
  • MyoD Protein / metabolism
  • Myoblasts / cytology
  • Myoblasts / drug effects*
  • Myoblasts / metabolism
  • Myogenin / genetics
  • Myogenin / metabolism
  • Myosin Heavy Chains / genetics
  • Myosin Heavy Chains / metabolism
  • Primary Cell Culture
  • Protein-Serine-Threonine Kinases / antagonists & inhibitors
  • Protein-Serine-Threonine Kinases / genetics
  • Protein-Serine-Threonine Kinases / metabolism
  • Satellite Cells, Skeletal Muscle / cytology
  • Satellite Cells, Skeletal Muscle / drug effects*
  • Satellite Cells, Skeletal Muscle / metabolism
  • Signal Transduction
  • Tea / chemistry
  • Transcription Factors / agonists*
  • Transcription Factors / genetics
  • Transcription Factors / metabolism

Substances

  • 14-3-3 Proteins
  • MyoD Protein
  • MyoD1 myogenic differentiation protein
  • Myog protein, mouse
  • Myogenin
  • Tea
  • Transcription Factors
  • Catechin
  • epigallocatechin gallate
  • Taz protein, mouse
  • TAFAZZIN protein, human
  • Lats1 protein, mouse
  • Protein-Serine-Threonine Kinases
  • Myosin Heavy Chains