Proteomic profiling of thyroid tissue in patients with obesity and benign diffuse goiter.
2D-DIGE
MALDI-TOF
goiter
obese
proteomics
thyroid tissue
Journal
Frontiers in endocrinology
ISSN: 1664-2392
Titre abrégé: Front Endocrinol (Lausanne)
Pays: Switzerland
ID NLM: 101555782
Informations de publication
Date de publication:
2022
2022
Historique:
received:
19
04
2022
accepted:
04
07
2022
entrez:
15
8
2022
pubmed:
16
8
2022
medline:
17
8
2022
Statut:
epublish
Résumé
Goiter is a term to describe the enlargement of the thyroid gland. The pathophysiology and molecular changes behind development of diffuse benign goiter remains unclear. The present study targeted to identify and describe the alterations in the thyroid tissue proteome from patients (obese euthyroid) with benign diffuse goiter (BDG) using proteomics approach. Thyroid tissue samples, from 7 age and sex matched, patients with BDG and 7 controls were obtained at the time of surgery. An untargeted proteomic analysis of the thyroid tissue was performed out utilizing two-dimensional difference (2D-DIGE) in gel electrophoresis followed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) for identification of the proteins. Progenesis software was used to identify changes in expression of tissue proteins and found statistically significant differences in abundance in a total of 90 proteins, 46 up and 44 down (1.5-fold change, ANOVA, p ≤ 0.05) in BDG compared to the control group. Bioinformatic analysis using Ingenuity Pathway Analysis (IPA) identified dysregulation of signalling pathways linked to ERK1/2, Glutathione peroxidase and NADPH oxidase associated to organismal injury and abnormalities, endocrine system disorders and cancer. The thyroid tissue proteome in patients with BDG revealed a significant decrease in thyroglobulin along with dysregulation of glycolysis and an increase in prooxidant peroxidase enzymes. Dysregulation of metabolic pathways related to glycolysis, redox proteins, and the proteins associated with maintaining the cytoskeletal structure of the thyrocytes was also identified.
Identifiants
pubmed: 35966064
doi: 10.3389/fendo.2022.923465
pmc: PMC9365950
doi:
Substances chimiques
Proteome
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
923465Informations de copyright
Copyright © 2022 Benabdelkamel, Rafiullah, Masood, Alsaif, Musambil and Alfadda.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be considered as a potential conflict of interest.
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