A stress-inducible rat liver endoplasmic reticulum protein, ERp29

Eur J Biochem. 1998 Jan 15;251(1-2):304-13. doi: 10.1046/j.1432-1327.1998.2510304.x.


We have isolated, cDNA cloned and characterised a 29-kDa protein (ERp29), containing a C-terminal endoplasmic reticulum(ER)-retrieval signal, from the rat liver ER. ERp29 was induced to high levels in the rat hepatoma cells under metabolic stress conditions known to cause an aberrant accumulation of proteins in the ER [(e.g. culture in presence of the Ca2+ ionophore A23187, inhibitors of Ca2+-ATPase (thapsigargin), intracellular protein transport (brefeldin A), or protein N-glycosylation (tunicamycin)]. Experimental evidence of its localisation in the luminal compartment of the ER was obtained by topology studies including immunofluorescence microscopy, in vitro translation and proteinase protection assay. ERp29 constitutes about 0.1% of the rat hepatic microsomal proteins and is constitutively expressed in all rat tissues examined, as evident from northern blot analysis. In rat hepatoma cells ERp29 was found to be associated with the abundant molecular chaperone/stress protein BiP/GRP78 and this interaction was significantly enhanced after treatment with tunicamycin and A23187. Taken together, these results suggest that ERp29 is a member of the stress-response machinery of the ER.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Carrier Proteins / metabolism
  • Cloning, Molecular
  • DNA, Complementary
  • Endoplasmic Reticulum / chemistry*
  • Endoplasmic Reticulum / metabolism
  • Endoplasmic Reticulum Chaperone BiP
  • Heat-Shock Proteins / genetics*
  • Heat-Shock Proteins / isolation & purification
  • Heat-Shock Proteins / metabolism*
  • Liver / chemistry*
  • Male
  • Molecular Chaperones / metabolism
  • Molecular Sequence Data
  • Precipitin Tests
  • Rats
  • Rats, Sprague-Dawley
  • Stress, Physiological*
  • Tissue Distribution


  • Carrier Proteins
  • DNA, Complementary
  • Endoplasmic Reticulum Chaperone BiP
  • Erp29 protein, rat
  • Heat-Shock Proteins
  • Molecular Chaperones

Associated data

  • GENBANK/U36482