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Updated: Jan 19, 2026
Molecular Chaperones and Protein Folding
Immunomorphological Pattern of Molecular Chaperones in Normal and Pathological Thyroid Tissues and Circulating
Celeste Caruso Bavisotto1,2,3, Calogero Cipolla4, Giuseppa Graceffa5
1Department of Biomedicine, Neuroscience and Advanced Diagnostics (BIND), Institute of Human Anatomy and Histology, University of Palermo, 90127 Palermo, Italy. celestebavisotto@gmail.com.
Abstract:
The thyroid is a major component of the endocrine system and its pathology can cause serious diseases, e.g., papillary carcinoma (PC). However, the carcinogenic mechanisms are poorly understood and clinical useful biomarkers are scarce. Therefore, we determined if there are quantitative patterns of molecular chaperones in the tumor tissue and circulating exosomes that may be useful in diagnosis and provide clues on their participation in carcinogenesis. Hsp27, Hsp60, Hsp70, and Hsp90 were quantified by immunohistochemistry in PC, benign goiter (BG), and normal peritumoral tissue (PT). The same chaperones were assessed in plasma exosomes from PC and BG patients before and after ablative surgery, using Western blotting. Hsp27, Hsp60, and Hsp90 were increased in PC in comparison with PT and BG but no differences were found for Hsp70. Similarly, exosomal levels of Hsp27, Hsp60, and Hsp90 were higher in PC than in BG, and those in PC were higher before ablative surgery than after it. Hsp27, Hsp60, and Hsp90 show distinctive quantitative patterns in thyroid tissue and circulating exosomes in PC as compared with BG, suggesting some implication in the carcinogenesis of these chaperones and indicating their potential as biomarkers for clinical applications.
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