2026-06-29T02:10:20Zhttps://docta.ucm.es/rest/oai/requestoai:docta.ucm.es:20.500.14352/47712025-09-15T14:09:34Zcom_20.500.14352_14col_20.500.14352_15
Docta Complutense
author
Martínez de Toda Cabeza, Irene
author
Rattan, Suresh I. S.
author
Fuente del Rey, Mónica de la
author
Arranz Salas, Lorena
2023-06-16T14:20:55Z
2023-06-16T14:20:55Z
2021
2076-3921
10.3390/antiox10091397
https://hdl.handle.net/20.500.14352/4771
https://doi.org/10.3390/antiox10091397
https://www.mdpi.com/2076-3921/10/9/1397
Oxidized, 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.
eng
Atribución 3.0 España
Female mice reaching exceptionally high old age have
preserved 20S proteasome activities
journal article
URL
https://docta.ucm.es/bitstreams/273e20ad-613d-4dd4-b1fc-8e1adfdb7458/download
File
MD5
d4e8d16122b4c44d1cdd13d2250c491a
989043
application/pdf
Martínez de Toda, I. et al. 2021. Female Mice Reaching Exceptionally....pdf