Role of CaMKII and sarcolipin in muscle adaptations to strength training with different levels of fatigue in the set. (2nd October 2020)

• Record Type: Journal Article
• Authors: Martinez‐Canton, Miriam; Gallego‐Selles, Angel; Gelabert‐Rebato, Miriam; Martin‐Rincon, Marcos; Pareja‐Blanco, Fernando; Rodriguez‐Rosell, David; Morales‐Alamo, David; Sanchis‐Moysi, Joaquin; Dorado, Cecilia; Jose Gonzalez‐Badillo, Juan; Calbet, Jose A. L.
• Is Part Of: Scandinavian journal of medicine & science in sports. Volume 31:Number 1(2021)
• Page Start: 91
• Page End: 103
• Publication Date: 2020-10-02
• Subjects: exercise -- fatigue -- human -- myosin heavy chain -- skeletal muscle -- velocity‐based training; Sports medicine -- Periodicals; Sports -- Physiological aspects -- Periodicals; Sports -- Periodicals; 617.1027
• DOI: 10.1111/sms.13828
• Languages: English
• ISSNs: 0905-7188

Abstract

Abstract: Strength training promotes a IIX‐to‐IIA shift in myosin heavy chain (MHC) composition, likely due to changes in sarcoplasmic [Ca 2+ ] which are sensed by CaMKII. Sarcoplasmic [Ca 2+ ] is in part regulated by sarcolipin (SLN), a small protein that when overexpressed in rodents stimulates mitochondrial biogenesis and a fast‐to‐slow fiber type shift. The purpose of this study was to determine whether CaMKII and SLN are involved in muscle phenotype and performance changes elicited by strength training. Twenty‐two men followed an 8‐week velocity‐based resistance training program using the full squat exercise while monitoring repetition velocity. Subjects were randomly assigned to two resistance training programs differing in the repetition velocity loss allowed in each set: 20% (VL20) vs 40% (VL40). Strength training caused muscle hypertrophy, improved 1RM and increased total CaMKII protein expression, particularly of the δD isoform. Phospho‐Thr 287 ‐CaMKII δD expression increased only in VL40 (+89%), which experienced greater muscle hypertrophy, and a reduction in MHC‐IIX percentage. SLN expression was increased in VL20 (+33%) remaining unaltered in VL40. The changes in phospho‐Thr 287 ‐CaMKII δD were positively associated with muscle hypertrophy and the number of repetitions during training, and negatively with the changes in MHC‐IIX and SLN. Most OXPHOS proteins remained unchanged, except for NDUFB8 (Complex I), which was reduced after training (−22%) in both groups. The amount of fatigue allowed in each set critically influences muscle CaMKII and SLN responses and determines muscle phenotype changes. With lower intra‐set fatigue, the IIX‐to‐IIA MHC shift is attenuated.