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Protein alterations in women with chronic widespread pain--An explorative proteomic study of the trapezius muscle.

Olausson P, Gerdle B, Ghafouri N, Sjöström D, Blixt E, Ghafouri B - Sci Rep (2015)

Bottom Line: Here, we use proteomics to study protein changes in trapezius muscle from 18 female patients diagnosed with CWP compared to 19 healthy female subjects.Other proteins are associated with muscle damage, muscle recovery, stress and inflammation.Taken together, this study gives further support that peripheral factors may be of importance in maintaining CWP.

View Article: PubMed Central - PubMed

Affiliation: Division of Community Medicine, Department of Medical and Health Sciences, Faculty of Health Sciences, Linköping University and Pain and Rehabilitation Center, Anaesthetics, Operations and Specialty Surgery Center, Region Östergötland.

ABSTRACT
Chronic widespread pain (CWP) has a high prevalence in the population and is associated with prominent negative individual and societal consequences. There is no clear consensus concerning the etiology behind CWP although alterations in the central processing of nociception maintained by peripheral nociceptive input has been suggested. Here, we use proteomics to study protein changes in trapezius muscle from 18 female patients diagnosed with CWP compared to 19 healthy female subjects. The 2-dimensional gel electrophoresis (2-DE) in combination with multivariate statistical analyses revealed 17 proteins to be differently expressed between the two groups. Proteins were identified by mass spectrometry. Many of the proteins are important enzymes in metabolic pathways like the glycolysis and gluconeogenesis. Other proteins are associated with muscle damage, muscle recovery, stress and inflammation. The altered expressed levels of these proteins suggest abnormalities and metabolic changes in the myalgic trapezius muscle in CWP. Taken together, this study gives further support that peripheral factors may be of importance in maintaining CWP.

No MeSH data available.


Related in: MedlinePlus

A basic structure of a myocyte.Actin and myosin are the major proteins in the contractile apparatus; the sarcomere. Desmin are predominantly found around the Z-disc linking the myofibrils together. Alpha-crystallin B chain binds to other cytoskeletal and myofibrillar proteins thus having a stabilizing effect. Adapted with permission from The Journal of Clinical Investigation77.
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f2: A basic structure of a myocyte.Actin and myosin are the major proteins in the contractile apparatus; the sarcomere. Desmin are predominantly found around the Z-disc linking the myofibrils together. Alpha-crystallin B chain binds to other cytoskeletal and myofibrillar proteins thus having a stabilizing effect. Adapted with permission from The Journal of Clinical Investigation77.

Mentions: Heat shock protein beta-1 and alpha-crystallin B chain belongs to the small heat shock protein (HSP20) family. Alpha-crystallin B chain has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions626364. The up-regulation and accumulation of the heat shock proteins including alpha-crystallin B chain may result in myofibrils more resilient to both oxidative and mechanical stresses6566 and to protect the cytoskeleton of the myofibrils67 (Fig. 2). It has also been suggested that by binding to cytoskeletal and myofibrillar proteins, alpha-crystallin B chain function as stabilizers of disrupted myofibrillar structures indicating a role in muscle recovery67. Heat shock protein beta-1 is found in various tissues including striated muscle and is involved in stress resistance and actin organization6869. The lowered abundance of heat shock protein beta-1 in our study may reflect an insufficient capacity or strain upon the processes of promoting muscle recovery.


Protein alterations in women with chronic widespread pain--An explorative proteomic study of the trapezius muscle.

Olausson P, Gerdle B, Ghafouri N, Sjöström D, Blixt E, Ghafouri B - Sci Rep (2015)

A basic structure of a myocyte.Actin and myosin are the major proteins in the contractile apparatus; the sarcomere. Desmin are predominantly found around the Z-disc linking the myofibrils together. Alpha-crystallin B chain binds to other cytoskeletal and myofibrillar proteins thus having a stabilizing effect. Adapted with permission from The Journal of Clinical Investigation77.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4493691&req=5

f2: A basic structure of a myocyte.Actin and myosin are the major proteins in the contractile apparatus; the sarcomere. Desmin are predominantly found around the Z-disc linking the myofibrils together. Alpha-crystallin B chain binds to other cytoskeletal and myofibrillar proteins thus having a stabilizing effect. Adapted with permission from The Journal of Clinical Investigation77.
Mentions: Heat shock protein beta-1 and alpha-crystallin B chain belongs to the small heat shock protein (HSP20) family. Alpha-crystallin B chain has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions626364. The up-regulation and accumulation of the heat shock proteins including alpha-crystallin B chain may result in myofibrils more resilient to both oxidative and mechanical stresses6566 and to protect the cytoskeleton of the myofibrils67 (Fig. 2). It has also been suggested that by binding to cytoskeletal and myofibrillar proteins, alpha-crystallin B chain function as stabilizers of disrupted myofibrillar structures indicating a role in muscle recovery67. Heat shock protein beta-1 is found in various tissues including striated muscle and is involved in stress resistance and actin organization6869. The lowered abundance of heat shock protein beta-1 in our study may reflect an insufficient capacity or strain upon the processes of promoting muscle recovery.

Bottom Line: Here, we use proteomics to study protein changes in trapezius muscle from 18 female patients diagnosed with CWP compared to 19 healthy female subjects.Other proteins are associated with muscle damage, muscle recovery, stress and inflammation.Taken together, this study gives further support that peripheral factors may be of importance in maintaining CWP.

View Article: PubMed Central - PubMed

Affiliation: Division of Community Medicine, Department of Medical and Health Sciences, Faculty of Health Sciences, Linköping University and Pain and Rehabilitation Center, Anaesthetics, Operations and Specialty Surgery Center, Region Östergötland.

ABSTRACT
Chronic widespread pain (CWP) has a high prevalence in the population and is associated with prominent negative individual and societal consequences. There is no clear consensus concerning the etiology behind CWP although alterations in the central processing of nociception maintained by peripheral nociceptive input has been suggested. Here, we use proteomics to study protein changes in trapezius muscle from 18 female patients diagnosed with CWP compared to 19 healthy female subjects. The 2-dimensional gel electrophoresis (2-DE) in combination with multivariate statistical analyses revealed 17 proteins to be differently expressed between the two groups. Proteins were identified by mass spectrometry. Many of the proteins are important enzymes in metabolic pathways like the glycolysis and gluconeogenesis. Other proteins are associated with muscle damage, muscle recovery, stress and inflammation. The altered expressed levels of these proteins suggest abnormalities and metabolic changes in the myalgic trapezius muscle in CWP. Taken together, this study gives further support that peripheral factors may be of importance in maintaining CWP.

No MeSH data available.


Related in: MedlinePlus