Martínez de Toda Cabeza, IreneRattan, Suresh I. S.Fuente del Rey, Mónica de laArranz Salas, Lorena2023-06-162023-06-162021-08-31Electronic: 2076-392110.3390/antiox10091397https://hdl.handle.net/20.500.14352/4771Oxidized, damaged and misfolded proteins accumulate during aging and contribute to impaired cell function and tissue homeodynamics. Damaged proteins are degraded by cellular clearance mechanisms like the 20S proteasome. Aging relates to low 20S proteasome function, whereas long-lived species show high levels. However, contradictory results exist depending on the tissue or cell type and it is unknown how the 20S proteasome functions in exceptionally old mice. The aim of this study was to investigate two proteasome activities (caspase-like and chymotrypsin-like) in several tissues (lung, heart, axillary lymph nodes, liver, kidney) and cells (peritoneal leukocytes) from adult (28 ± 4 weeks, n = 12), old (76 ± 4 weeks, n = 9) and exceptionally old (128 ± 4 weeks, n = 9) BALB/c female mice. The results show different age-related changes depending on the tissue and the activity considered, so there is no universal decline in proteasome function with age in female mice. Interestingly, exceptionally old mice displayed better maintained proteasome activities, suggesting that preserved 20S proteasome is associated with successful aging.engAtribución 3.0 Españajournal articlehttps://doi.org/10.3390/antiox10091397https://www.mdpi.com/2076-3921/10/9/1397open access577.112612.67591.1577.27AgingHealthy agingExceptionally old20S proteasomeCaspase-like activityChymotrypsinlike activityInmunologíaBioquímica (Biología)Fisiología animal (Biología)2412 Inmunología2302 Bioquímica2401.13 Fisiología Animal