Liver-specific deletion of protein tyrosine phosphatase (PTP) 1B improves obesity- and pharmacologically induced endoplasmic reticulum stress

Biochem J. 2011 Sep 1;438(2):369-78. doi: 10.1042/BJ20110373.

Abstract

Obesity is associated with induction of the ER (endoplasmic reticulum)-stress response signalling and insulin resistance. PTP1B (protein tyrosine phosphatase 1B) is a major regulator of adiposity and insulin sensitivity. The aim of the present study was to investigate the role of L-PTP1B (liver-specific PTP1B) in chronically HFD (high-fat diet) and pharmacologically induced (tunicamycin and thapsigargin) ER-stress response signalling in vitro and in vivo. We assessed the effects of ER-stress response induction on hepatic PTP1B expression, and consequences of hepatic-PTP1B deficiency, in cells and mouse liver, on components of ER-stress response signalling. We found that PTP1B protein and mRNA expression levels were up-regulated in response to acute and/or chronic ER stress, in vitro and in vivo. Silencing PTP1B in hepatic cell lines or mouse liver (L-PTP1B(-/-)) protected against induction of pharmacologically induced and/or obesity-induced ER stress. The HFD-induced increase in CHOP (CCAAT/enhancer-binding protein homologous protein) and BIP (binding immunoglobulin protein) mRNA levels were partially inhibited, whereas ATF4 (activated transcription factor 4), GADD34 (growth-arrest and DNA-damage-inducible protein 34), GRP94 (glucose-regulated protein 94), ERDJ4 (ER-localized DnaJ homologue) mRNAs and ATF6 protein cleavage were completely suppressed in L-PTP1B(-/-) mice relative to control littermates. L-PTP1B(-/-) mice also had increased nuclear translocation of spliced XBP-1 (X box-binding protein-1) via increased p85α binding. We demonstrate that the ER-stress response and L-PTP1B expression are interlinked in obesity- and pharmacologically induced ER stress and this may be one of the mechanisms behind improved insulin sensitivity and lower lipid accumulation in L-PTP1B(-/-) mice.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Activating Transcription Factor 6 / metabolism
  • Animals
  • Cell Nucleus / drug effects
  • Cell Nucleus / metabolism
  • Class Ia Phosphatidylinositol 3-Kinase / metabolism
  • DNA-Binding Proteins / metabolism
  • Endoplasmic Reticulum / drug effects
  • Endoplasmic Reticulum / pathology*
  • Endoribonucleases / metabolism
  • Eukaryotic Initiation Factor-2 / metabolism
  • Gene Deletion*
  • Gene Knockdown Techniques
  • Glucose / metabolism
  • Hep G2 Cells
  • Homeostasis / drug effects
  • Humans
  • Lipid Metabolism / drug effects
  • Liver / drug effects
  • Liver / enzymology*
  • Liver / pathology
  • Mice
  • Obesity / enzymology*
  • Obesity / pathology
  • Organ Specificity / drug effects
  • Organ Specificity / genetics
  • Protein Serine-Threonine Kinases / metabolism
  • Protein Transport / drug effects
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1 / deficiency*
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1 / genetics
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1 / metabolism
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Regulatory Factor X Transcription Factors
  • Signal Transduction / drug effects
  • Stress, Physiological* / drug effects
  • Thapsigargin / pharmacology
  • Transcription Factors / metabolism
  • Tunicamycin / pharmacology
  • X-Box Binding Protein 1

Substances

  • Activating Transcription Factor 6
  • DNA-Binding Proteins
  • Eukaryotic Initiation Factor-2
  • RNA, Messenger
  • Regulatory Factor X Transcription Factors
  • Transcription Factors
  • X-Box Binding Protein 1
  • XBP1 protein, human
  • Xbp1 protein, mouse
  • Tunicamycin
  • Thapsigargin
  • Class Ia Phosphatidylinositol 3-Kinase
  • Ern1 protein, mouse
  • Protein Serine-Threonine Kinases
  • Endoribonucleases
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1
  • Glucose