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Muscles Proteome Analysis; Irisin Administration Mimics Some Molecular Effects of Exercise in Quadriceps Muscle Publisher Pubmed



Momenzadeh S1 ; Zamani S5 ; Pourteymourfardtabrizi Z2, 3 ; Barreiro C6, 7 ; Jami MS2, 3, 4
Authors
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Authors Affiliations
  1. 1. Department of Medical Biotechnology, School of Advanced Technologies, Shahrekord University of Medical Sciences, Shahrekord, Iran
  2. 2. Cellular and Molecular Research Center, Basic Health Sciences Institute, Shahrekord University of Medical Sciences, Shahrekord, Iran
  3. 3. QIANBIOTEC, Research and Development Center for Biotechnology, Isfahan, Iran
  4. 4. Department of Neurology, David Geffen School of Medicine, University of California Los Angeles (UCLA), Los Angeles, CA, United States
  5. 5. Department of Anatomical Sciences and Molecular Biology, School of Medicine, Isfahan University of Medical Sciences, Isfahan, Iran
  6. 6. INBIOTEC (Instituto de Biotecnologia de Leon), Avda. Real 1 - Parque Cientifico de Leon 24006, Leon, Spain
  7. 7. Departamento de Biologia Molecular, Universidad de Leon, Campus de Ponferrada, Avda. Astorga s/n, Ponferrada, 24401, Spain

Source: Biochimie Published:2021


Abstract

Because of health-promoting effects, the adaptation of skeletal muscles to exercise is considered a therapeutic strategy for metabolic complications and musculoskeletal disabilities. Myokines display many beneficial effects of different exercise modalities. Among them, irisin is known as a systemic effector that positively influences several organs. There are a few studies about the effects of irisin on skeletal muscles, and irisin prosperities need to be well-defined for being an exercise mimetic. To aim this purpose, we assessed the proteome profile of mouse skeletal muscle after eight weeks of irisin injection comparing to resistance and endurance exercise treated groups. In the current study, two-dimensional gel electrophoresis was used to evaluate the protein content of the quadriceps muscle. The results were analyzed with Image Master 2D Platinum V6 software. Differentially expressed proteins were characterized by mass spectrometry (MALDI TOF/TOF) and interpreted using protein data banks and co-expression network. Irisin increases cellular ATP content by driving its overproduction through glycolysis and oxidative phosphorylation similar to two exercise protocols and as a specific property, decreases ATP consumption through creatine kinase downregulation. It also improves the microstructural properties of quadriceps muscle by increasing fiber proteins and might induce cellular proliferation and differentiation. Network analysis of differentially expressed proteins also revealed the co-expression of Irisin precursor with structural and metabolic-related proteins. The protein alterations after irisin administration display the potential of this myokine to mimic some molecular effects of exercise, suggesting it a promising candidate to improve muscle metabolism and structure. © 2021 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM)