Proteomic analysis reveals aberrant expression of CALR and HSPA5 in thyroid tissues of Graves' disease

Clin Biochem. 2017 Jan;50(1-2):40-45. doi: 10.1016/j.clinbiochem.2016.08.014. Epub 2016 Aug 24.

Abstract

Objectives: To explore the proteomic changes in thyroid tissue from GD patients and find new biomarkers for the prevention, diagnosis as well as the treatment of GD.

Design and methods: Group1 included five thyroid specimens of GD cases and 5 normal thyroid tissue samples which were removed surgically and collected. The proteins were extracted from these thyroid tissues and then the differentially expressed protein spots were identified by MALDI-TOF-MS. The interested proteins were further validated in more specimens (group2: 11 pathological thyroid specimens and 7 normal thyroid tissue samples).

Results: A total of 34 differentially expressed proteins were observed, and the majority of these proteins were involved in endoplasmic reticulum stress (ER-stress), oxidative stress, energy metabolism, cytoskeleton and movement. The overexpression of calreticulin(CALR) and heat shock 70kDa protein 5(HSPA5) was further validated.

Conclusion: Alltogether, abundant new candidate molecules, especially proteins related to ER-stress, were found to be involved in the pathogenesis of GD.

Keywords: Calreticulin(CALR); Endoplasmic reticulum (ER) stress; Graves' disease(GD); Heat shock 70kDa protein 5(HSPA5); Proteomics.

MeSH terms

  • Adult
  • Calreticulin / metabolism*
  • Endoplasmic Reticulum Chaperone BiP
  • Female
  • Graves Disease / metabolism*
  • Heat-Shock Proteins / metabolism*
  • Humans
  • Male
  • Middle Aged
  • Proteomics*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Thyroid Gland / metabolism*
  • Thyroid Gland / pathology
  • Young Adult

Substances

  • Calreticulin
  • Endoplasmic Reticulum Chaperone BiP
  • HSPA5 protein, human
  • Heat-Shock Proteins