Additional file 1: of Alteration of actin dependent signaling pathways associated with membrane microdomains in hyperlipidemia

Mass spectrometry method. (DOCX 21 kb

Additional file 5: Table S2. of Alteration of actin dependent signaling pathways associated with membrane microdomains in hyperlipidemia

(XLSX 11 kb

Additional file 4: Figure S2. of Alteration of actin dependent signaling pathways associated with membrane microdomains in hyperlipidemia

Gene ontology details of detergent resistant membrane microdomains proteins. Data distribution based on: Cellular Component (a), Biological Process (b) and Molecular Function (c). Data expressed as mean values ± SD, following the analysis of the biological replicates. (DOCX 654 kb

Additional file 2: Table S1. of Alteration of actin dependent signaling pathways associated with membrane microdomains in hyperlipidemia

Mass spectrometry data of differentially abundant proteins extracted from Protein Center databases. (XLSX 66 kb

Endoplasmic Reticulum Chaperones Are Potential Active Factors in Thyroid Tumorigenesis

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