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Quantitative proteomics analysis of sporadic parathyroid adenoma tissue samples

  • Arya, A. K.1
  • Bhadada, S. K.1
  • Singh, P.1
  • Dahiya, D.2
  • Kaur, G.1
  • Sharma, S.3
  • Saikia, U. N.4
  • Behera, A.2
  • Rao, S. D.5
  • Bhasin, M.6
  • 1 Postgraduate Institute of Medical Education and Research (PGIMER), Department of Endocrinology, Room No. 2, 4th Floor Block-F, Nehru Hospital, PGIMER, Chandigarh, 160012, India , Chandigarh (India)
  • 2 PGIMER, Department of General Surgery, Chandigarh, India , Chandigarh (India)
  • 3 PGIMER, Department of Biochemistry, Chandigarh, India , Chandigarh (India)
  • 4 PGIMER, Department of Histopathology, Chandigarh, India , Chandigarh (India)
  • 5 Henry Ford Hospital, Bone and Mineral Research Laboratory, Detroit, USA , Detroit (United States)
  • 6 Harvard Medical School, Department of Medicine, Beth Israel Deaconess Medical Center, Boston, MA, USA , Boston (United States)
Published Article
Journal of Endocrinological Investigation
Publication Date
Oct 03, 2018
DOI: 10.1007/s40618-018-0958-1
Springer Nature


ObjectiveMolecular pathogenesis of parathyroid tumors is incompletely understood. Identification of novel molecules and understanding their role in parathyroid tumorigenesis by proteomics approach would be informative with potential clinical implications.MethodAdenomatous (n = 5) and normal (n = 2) parathyroid tissue lysates were analyzed for protein profile by LC–MS/MS method and the proteins were classified using bioinformatics tools such as PANTHER and toppfun functional enrichment tool. Identified proteins were further validated by western blotting and qRT-PCR (n = 20).ResultComparative proteomics analysis revealed that a total of 206 proteins (74 upregulated and 132 downregulated) were differentially expressed (≥ twofold change) in adenomas. Bioinformatics analysis revealed that 48 proteins were associated with plasma membrane, 49 with macromolecular complex, 39 were cytoplasm, 38 were organelle related, 21 were cell junction and 10 were extracellular proteins. These proteins belonged to a diverse protein family such as enzymes, transcription factors, cell signalling, cell adhesion, cytoskeleton proteins, receptors, and calcium-binding proteins. The major biological processes predicted for the proteins were a cellular, metabolic and developmental process, cellular localization, and biological regulation. The differentially expressed proteins were found to be associated with MAPK, phospholipase C (PLC) and phosphatidylinositol (PI) signalling pathways, and with chromatin organization. Western blot and qRT-PCR analysis of three proteins (DNAJC2, ACO2, and PRDX2) validated the LC–MS/MS findings.ConclusionThis exploratory study demonstrates the feasibility of proteomics approach in finding the dysregulated proteins in benign parathyroid adenomas, and our preliminary results suggest that MAPK, PLC and PI signalling pathways and chromatin organization are involved in parathyroid tumorigenesis.

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