Chemical chaperones in metabolic fitness beyond protein folding

Ester Zito; Alain Lescure; Nica Borgese

doi:10.1016/j.tem.2024.04.006

Chemical chaperones in metabolic fitness beyond protein folding

Trends Endocrinol Metab. 2024 Apr 24:S1043-2760(24)00089-4. doi: 10.1016/j.tem.2024.04.006. Online ahead of print.

Authors

Ester Zito¹, Alain Lescure², Nica Borgese³

Affiliations

¹ Istituto di Ricerche Farmacologiche Mario Negri IRCCS, Milan, Italy; Department of Biomolecular Sciences, University of Urbino Carlo Bo, Urbino, Italy. Electronic address: ester.zito@marionegri.it.
² University of Strasbourg, CNRS, Architecture and Reactivity of RNA, Strasbourg, France.
³ Consiglio Nazionale delle Ricerche Neuroscience Institute, 20854 Vedano al Lambro, Italy.

PMID: 38664151
DOI: 10.1016/j.tem.2024.04.006

Abstract

Chemical chaperones are small molecules that improve protein folding, alleviating aberrant pathological phenotypes due to protein misfolding. Recent reports suggest that, in parallel with their role in relieving endoplasmic reticulum (ER) stress, chemical chaperones rescue mitochondrial function and insulin signaling. These effects may underlie their pharmacological action on metabolically demanding tissues.

Keywords: PBA; TUDCA; chemical chaperone; congenital myopathies; insulin signaling; metabolic disease; misfolding disease.