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J Proteome Res. 2016 Sep 2;15(9):3377-87. doi: 10.1021/acs.jproteome.6b00567. Epub 2016 Aug 16.

Endoplasmic Reticulum Chaperones Are Potential Active Factors in Thyroid Tumorigenesis.

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Institute of Cellular Biology and Pathology "Nicolae Simionescu" , 8, B.P. Hasdeu Street, P.O. Box 35-14, 050568 Bucharest, Romania.
National Institute of Endocrinology "C.I. Parhon" , 34-36 Aviatorilor Boulevard, 011863 Bucharest, Romania.
University of Bucharest, Faculty of Physics , 405 Atomi┼čtilor Street, 077125 Magurele, Romania.


The study aimed to evaluate the proteomic changes in benign follicular adenoma versus malignant follicular variant of papillary thyroid carcinoma. Tumor and nontumor adjacent samples were analyzed by liquid nanochromatography mass spectrometry, and protein abundance was evaluated by label-free quantification. Western blotting and quantitative real-time polymerase chain reaction were used to validate and complement the mass spectrometry data. The results demonstrated deregulated expression of four endoplasmic reticulum chaperones (78 kDa glucose-regulated protein, endoplasmin, calnexin, protein disulfide-isomerase A4), glutathione peroxidase 3 and thyroglobulin, all of them involved in thyroid hormone synthesis pathway. The altered tissue abundance of endoplasmic reticulum chaperones in thyroid cancer was correlated with serum expression levels. The identified proteins significantly discriminate between adenoma and carcinoma in both thyroid tissue and corresponding sera. Data are available via ProteomeXchange with identifier PXD004322.


endoplasmic reticulum chaperone; mass spectrometry; thyroid cancer biomarkers

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