Myosin light chain and calcium regulating protein differences in chronic musculoskeletal neck and shoulder pain

DOI: 10.5584/jiomics.v6i1.191

Authors

  • Jenny Hadrevi Department of Community Medicine and Rehabilitation, Sports Medicine unit, Umeå University, SE 901 87 Umeå, Sweden
  • Maria V Turkina Department of Clinical and Experimental Medicine, Linköping University, SE 581 83 Linköping, Sweden
  • Anders Carlsson Division of Community Medicine, Department of Medical and Health Sciences, Linköping University and Pain and Rehabilitation Center, Anesthetics, Operations and Specialty Surgery Center, Region Östergötland, SE 581 85 Linköping, Sweden
  • Bjorn Gerdle Division of Community Medicine, Department of Medical and Health Sciences, Linköping University and Pain and Rehabilitation Center, Anesthetics, Operations and Specialty Surgery Center, Region Östergötland, SE 581 85 Linköping, Sweden
  • Britt Larsson Division of Community Medicine, Department of Medical and Health Sciences, Linköping University and Pain and Rehabilitation Center, Anesthetics, Operations and Specialty Surgery Center, Region Östergötland, SE 581 85 Linköping, Sweden
  • Fredrik Hellstrom Department of Occupational and Public Health Sciences, University of Gävle, 801 76 Gävle, Sweden
  • Bijar Ghafouri Division of Community Medicine, Department of Medical and Health Sciences, Linköping University and Pain and Rehabilitation Center, Anesthetics, Operations and Specialty Surgery Center, Region Östergötland, SE 581 85 Linköping, Sweden

Abstract

Proteomic screening analysis has detected myosin light chain (MLC) as a protein implied to be involved in chronic musculoskeletal neck and shoulder pain. Several analyses of MLC proteins have stated a difference in phosphorylation being the determining factor for protein activation hence altered contrability of the muscle in i.e. senescence. In continuation of a previous publication, this study is an attempt to analyze the different MLC isoforms by mass spectrometry and immune-analyses in myalgic and healthy trapezius muscle. In the present study no differences in phosphorylation level between the corresponding individual proteins were detected using LC-MSMS and immunoblotting; instead we assigned different isoforms of regulatory MLCs. To further elucidate the contrability: calcium (Ca2+) regulatory proteins, sarco(endo)plasmic reticulum Ca2+ ATPase 1 (SERCA-1) and calsequestrine (CSQ) were analyzed by western blot. The analysis revealed a significantly increased abundance of SERCA-1 protein in the myalgic muscle and a significantly increased abundance of CSQ in healthy muscle. Myalgic muscle contraction patterns have in previous studies shown to differ from healthy muscle which may be connected to the Ca2+ availability in the muscle. Here we present the proteomic characterization of differences in Ca2+ regulating proteins and particularly regulatory MLCs in trapezius muscle of women with chronic musculoskeletal neck and shoulder pain.

Published

2016-06-30