Effects of a resistance-training programme on endoplasmic reticulum unfolded protein response and mitochondrial functions in PBMCs from elderly subjects

• Published in: European journal of sport science Vol. 19; no. 7; pp. 931 - 940
• Main Authors: Estébanez, Brisamar, Moreira, Osvaldo C., Almar, Mar, de Paz, José A., Gonzalez-Gallego, Javier, Cuevas, María J.
• Format: Journal Article
• Language: English
• Published: England Routledge 09.08.2019
• Subjects: Aging; endoplasmic reticulum stress; mitophagy; physical activity; strength; unfolded protein response; Aging; unfolded protein response; mitophagy; strength; endoplasmic reticulum stress; physical activity
• ISSN: 1746-1391; 1536-7290
• DOI: 10.1080/17461391.2018.1561950

Aging has been related with a decline in the ability to handle protein folding, which leads to endoplasmic reticulum stress and alterations in unfolded protein response (UPR). Importantly, physical activity could activate the UPR and attenuate or prevent age-induced endoplasmic reticulum (ER) dysfunction. The current study evaluated the effects of a resistance exercise on UPR and mitochondrial functions in peripheral blood mononuclear cells (PBMCs) from elderly subjects. Thirty healthy women and men (age, 72.8, s x −  = 2.2 years) were randomized to a training group, which performed an 8-week resistance training programme, or a control group, which followed their daily routines. The phosphorylation of PERK and IRE1, as well as ATF4, and XBP1 protein expression, significantly increased following the training, while expression of BiP, AFT6 and CHOP remain without changes. Additionally, the intervention also induced an increase in PGC-1α and Mfn1 protein levels, while no changes were found in Drp1 expression. Finally, the resistance protocol was not able to activate PINK1/Parkin and Bnip3/Nix pathways. The results obtained seem to indicate that 8-week resistance exercise activates the UPR, stimulates mitochondrial biogenesis, maintains mitochondrial dynamics and prevents mitophagy activation by unfolded proteins in PBMCs from elderly subjects.