• Media type: E-Article
  • Title: Mitochondrial-specific autophagy linked to mitochondrial dysfunction following traumatic freeze injury in mice
  • Contributor: Nichenko, Anna S.; Southern, W. Michael; Tehrani, Kayvan Forouhesh; Qualls, Anita E.; Flemington, Alexandra B.; Mercer, Grant H.; Yin, Amelia; Mortensen, Luke J.; Yin, Hang; Call, Jarrod A.
  • Published: American Physiological Society, 2020
  • Published in: American Journal of Physiology-Cell Physiology, 318 (2020) 2, Seite C242-C252
  • Language: English
  • DOI: 10.1152/ajpcell.00123.2019
  • ISSN: 0363-6143; 1522-1563
  • Origination:
  • Footnote:
  • Description: The objective of this study was to interrogate the link between mitochondrial dysfunction and mitochondrial-specific autophagy in skeletal muscle. C57BL/6J mice were used to establish a time course of mitochondrial function and autophagy induction after fatigue ( n = 12), eccentric contraction-induced injury ( n = 20), or traumatic freeze injury (FI, n = 28); only FI resulted in a combination of mitochondrial dysfunction, i.e., decreased mitochondrial respiration, and autophagy induction. Moving forward, we tested the hypothesis that mitochondrial-specific autophagy is important for the timely recovery of mitochondrial function after FI. Following FI, there is a significant increase in several mitochondrial-specific autophagy-related protein contents including dynamin-related protein 1 (Drp1), BCL1 interacting protein (BNIP3), Pink1, and Parkin (~2-fold, P < 0.02). Also, mitochondrial-enriched fractions from FI muscles showed microtubule-associated protein light chain B1 (LC3)II colocalization suggesting autophagosome assembly around the damaged mitochondrial. Unc-51 like autophagy activating kinase (Ulk1) is considered necessary for mitochondrial-specific autophagy and herein we utilized a mouse model with Ulk1 deficiency in adult skeletal muscle ( myogenin-Cre). While Ulk1 knockouts had contractile weakness compared with littermate controls (−27%, P < 0.02), the recovery of mitochondrial function was not different, and this may be due in part to a partial rescue of Ulk1 protein content within the regenerating muscle tissue of knockouts from differentiated satellite cells in which Ulk1 was not genetically altered via myogenin-Cre. Lastly, autophagy flux was significantly less in injured versus uninjured muscles (−26%, P < 0.02) despite the increase in autophagy-related protein content. This suggests autophagy flux is not upregulated to match increases in autophagy machinery after injury and represents a potential bottleneck in the clearance of damaged mitochondria by autophagy.
  • Access State: Open Access