Please use this identifier to cite or link to this item:
Title: Role of CaMKII and sarcolipin in muscle adaptations to strength training with different levels of fatigue in the set
Authors: Martinez-Canton, Miriam
Gallego Sellés, Angel 
Gelabert-Rebato, Miriam 
Martín Rincón, Marcos 
Pareja-Blanco, Fernando
Rodriguez-Rosell, David
Morales Álamo, David 
Sanchís Moysi, Joaquín 
Dorado García, Cecilia 
González-Badillo, Juan José
Calbet, Jose A.L. 
UNESCO Clasification: 241106 Fisiología del ejercicio
Keywords: Exercise
Myosin Heavy Chain
Skeletal Muscle, et al
Issue Date: 2021
Project: Viabilidad y Sostenibilidad Del Adelgazamiento Mediante Tratamiento Intensificado en Pacientes Con Sobrepeso U Obesidad: Mecanismos Neuroendocrinos y Moleculares 
Desarrollo y Caracterización Molecular de Un Nuevo Modelo de Precondicionamiento Remoto 
Estudio Longitudinal de Los Efectos de Una Modificación Intensiva Del Estilo de Vida en la Composición Corporal E Indicadores Bioquímicos y Moleculares de Salud en Pacientes Con Sobrepeso y Obesidad: Aplicación Para la Evaluación Fisiológica de Rutas y Sistemas de Monitorización Del Esfuerzo 
Journal: Scandinavian Journal of Medicine and Science in Sports 
Abstract: Strength training promotes a IIX-to-IIA shift in myosin heavy chain (MHC) composition, likely due to changes in sarcoplasmic [Ca2+] which are sensed by CaMKII. Sarcoplasmic [Ca2+] 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-Thr287-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-Thr287-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.
ISSN: 0905-7188
DOI: 10.1111/sms.13828
Source: Scandinavian Journal of Medicine and Science in Sports [ISSN 0905-7188], v. 31(1), p. 91-103, (Enero 2021)
Appears in Collections:Artículos
Show full item record


checked on Nov 20, 2022

Page view(s)

checked on Oct 15, 2022

Google ScholarTM




Export metadata

Items in accedaCRIS are protected by copyright, with all rights reserved, unless otherwise indicated.