Increased temporal cortex ER stress proteins in depressed subjects who died by suicide

Neuropsychopharmacology. 2000 Mar;22(3):327-32. doi: 10.1016/S0893-133X(99)00091-3.

Abstract

Regulation of ER stress proteins, such as the 78-kilodalton glucose regulated protein (GRP78) by chronic treatment with mood stabilizing drugs suggests that this family of proteins may be involved in the pathophysiology of mood disorders. Indeed, increased levels of GRP78, GRP94, and calreticulin, a third member of the ER stress protein family, were found in temporal cortex of subjects with major depressive disorder who died by suicide compared with controls and subjects who died by other means. No such differences were found in subjects with other psychiatric disorders such as bipolar disorder or schizophrenia. These data suggest a potential role for ER stress proteins in severe depression that merits further study.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Calcium-Binding Proteins / analysis
  • Calcium-Binding Proteins / metabolism*
  • Calreticulin
  • Carrier Proteins / analysis
  • Carrier Proteins / metabolism*
  • Depressive Disorder / metabolism*
  • Depressive Disorder / pathology
  • Endoplasmic Reticulum Chaperone BiP
  • Female
  • HSP70 Heat-Shock Proteins / analysis
  • HSP70 Heat-Shock Proteins / metabolism*
  • Heat-Shock Proteins*
  • Humans
  • Male
  • Membrane Proteins / analysis
  • Membrane Proteins / metabolism*
  • Middle Aged
  • Molecular Chaperones / analysis
  • Molecular Chaperones / metabolism*
  • Ribonucleoproteins / analysis
  • Ribonucleoproteins / metabolism*
  • Suicide*
  • Temporal Lobe / metabolism*
  • Temporal Lobe / pathology

Substances

  • Calcium-Binding Proteins
  • Calreticulin
  • Carrier Proteins
  • Endoplasmic Reticulum Chaperone BiP
  • HSP70 Heat-Shock Proteins
  • HSPA5 protein, human
  • Heat-Shock Proteins
  • Membrane Proteins
  • Molecular Chaperones
  • Ribonucleoproteins
  • glucose-regulated proteins