Endoplasmic reticulum protein 29 (ERp29): An emerging role in cancer

Int J Biochem Cell Biol. 2011 Jan;43(1):33-6. doi: 10.1016/j.biocel.2010.09.019. Epub 2010 Nov 3.

Abstract

The endoplasmic reticulum protein 29 (ERp29) is a molecule that facilitates processing and transport of proteins in the early secretory pathway. Structural and functional analyses have suggested a biological role as a putative chaperone in the endoplasmic reticulum. The N-terminal domain of ERp29 resembles the thioredoxin domain of protein disulfide isomerase, but lacks its redox-active function due to the absence of an active motif consisting of double cysteines. In the context of carcinogenesis, the role of ERp29 in cancer progression has not been fully elucidated. However, recent studies indicate that high expression of ERp29 inversely correlates to tumor progression. In addition, over-expression of ERp29 significantly inhibits proliferation and suppresses tumorigenesis by modulating ER stress signaling and the mesenchymal-epithelial transition in breast cancer cells. In this review, we summarize the biological properties of ERp29 and its novel function as a tumor suppressor.

Publication types

  • Review

MeSH terms

  • Animals
  • Breast Neoplasms / etiology*
  • Breast Neoplasms / genetics*
  • Breast Neoplasms / metabolism*
  • Breast Neoplasms / pathology
  • Cell Transformation, Neoplastic / genetics
  • Cell Transformation, Neoplastic / metabolism
  • Endoplasmic Reticulum* / metabolism
  • Epithelial-Mesenchymal Transition
  • Female
  • Gene Expression Regulation, Neoplastic
  • Heat-Shock Proteins* / genetics
  • Heat-Shock Proteins* / metabolism
  • Humans
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / metabolism
  • Male
  • Mice
  • Molecular Chaperones* / genetics
  • Molecular Chaperones* / metabolism
  • Oxidation-Reduction
  • Protein Disulfide Reductase (Glutathione)*
  • Protein Disulfide-Isomerases / genetics
  • Protein Disulfide-Isomerases / metabolism
  • Rats
  • Thioredoxins / genetics
  • Thioredoxins / metabolism
  • Tumor Cells, Cultured

Substances

  • Erp29 protein, rat
  • Heat-Shock Proteins
  • Intracellular Signaling Peptides and Proteins
  • Molecular Chaperones
  • Thioredoxins
  • Protein Disulfide Reductase (Glutathione)
  • TXNDC12 protein, human
  • Protein Disulfide-Isomerases