Research Paper Volume 13, Issue 9 pp 12308—12333
Shikimic acid protects skin cells from UV-induced senescence through activation of the NAD+-dependent deacetylase SIRT1
- 1 Chromatin Biology Laboratory, Josep Carreras Leukaemia Research Institute (IJC), Barcelona 08916, Badalona, Spain
- 2 Chromatin Biology Laboratory, Cancer Epigenetics and Biology Program (PEBC), Bellvitge Biomedical Research Institute (IDIBELL), Barcelona 08908, Spain
- 3 Mesostetic Pharma Group, Barcelona 08840, Viladecans, Spain
- 4 MIRAS Beamline, ALBA-CELLS Synchrotron, Barcelona 08290, Cerdanyola del Vallès, Spain
- 5 Ionizing Radiation Research Group, Physics Department, Universitat Autònoma de Barcelona (UAB), Barcelona 08193, Cerdanyola del Vallès, Spain
Received: September 18, 2020 Accepted: March 31, 2021 Published: April 26, 2021
https://doi.org/10.18632/aging.203010How to Cite
Abstract
UV radiation is one of the main contributors to skin photoaging by promoting the accumulation of cellular senescence, which in turn induces a proinflammatory and tissue-degrading state that favors skin aging. The members of the sirtuin family of NAD+-dependent enzymes play an anti-senescence role and their activation suggests a promising approach for preventing UV-induced senescence in the treatment of skin aging. A two-step screening designed to identify compounds able to protect cells from UV-induced senescence through sirtuin activation identified shikimic acid (SA), a metabolic intermediate in many organisms, as a bona-fide candidate. The protective effects of SA against senescence were dependent on specific activation of SIRT1 as the effect was abrogated by the SIRT1 inhibitor EX-527. Upon UV irradiation SA induced S-phase accumulation and a decrease in p16INK4A expression but did not protect against DNA damage or increased polyploidies. In contrast, SA reverted misfolded protein accumulation upon senescence, an effect that was abrogated by EX-527. Consistently, SA induced an increase in the levels of the chaperone BiP, resulting in a downregulation of unfolded protein response (UPR) signaling and UPR-dependent autophagy, avoiding their abnormal hyperactivation during senescence. SA did not directly activate SIRT1 in vitro, suggesting that SIRT1 is a downstream effector of SA signaling specifically in the response to cellular senescence. Our study not only uncovers a shikimic acid/SIRT1 signaling pathway that prevents cellular senescence, but also reinforces the role of sirtuins as key regulators of cell proteostasis.