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Biomarkers of systemic inflammation in farmers with musculoskeletal disorders; a plasma proteomic study.

Ghafouri B, Carlsson A, Holmberg S, Thelin A, Tagesson C - BMC Musculoskelet Disord (2016)

Bottom Line: The levels of leucine-rich alpha-2-glycoprotein, haptoglobin, complement factor B, serotransferrin, one isoform of kininogen, one isoform of alpha-1-antitrypsin, and two isoforms of hemopexin were higher in farmers with MSD than in referents.On the other hand, the levels of alpha-2-HS-glycoprotein, alpha-1B-glycoprotein, vitamin D- binding protein, apolipoprotein A1, antithrombin, one isoform of kininogen, and one isoform of alpha-1-antitrypsin were lower in farmers than in referents.Farmers with MSD had altered plasma levels of protein biomarkers compared to the referents, indicating that farmers with MSD may be subject to a more systemic inflammation.

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, Linköping, SE-581 85, Sweden. bijar.ghafouri@liu.se.

ABSTRACT

Background: Farmers have an increased risk for musculoskeletal disorders (MSD) such as osteoarthritis of the hip, low back pain, and neck and upper limb complaints. The underlying mechanisms are not fully understood. Work-related exposures and inflammatory responses might be involved. Our objective was to identify plasma proteins that differentiated farmers with MSD from rural referents.

Methods: Plasma samples from 13 farmers with MSD and rural referents were included in the investigation. Gel based proteomics was used for protein analysis and proteins that differed significantly between the groups were identified by mass spectrometry.

Results: In total, 15 proteins differed significantly between the groups. The levels of leucine-rich alpha-2-glycoprotein, haptoglobin, complement factor B, serotransferrin, one isoform of kininogen, one isoform of alpha-1-antitrypsin, and two isoforms of hemopexin were higher in farmers with MSD than in referents. On the other hand, the levels of alpha-2-HS-glycoprotein, alpha-1B-glycoprotein, vitamin D- binding protein, apolipoprotein A1, antithrombin, one isoform of kininogen, and one isoform of alpha-1-antitrypsin were lower in farmers than in referents. Many of the identified proteins are known to be involved in inflammation.

Conclusions: Farmers with MSD had altered plasma levels of protein biomarkers compared to the referents, indicating that farmers with MSD may be subject to a more systemic inflammation. It is possible that the identified differences of proteins may give clues to the biochemical changes occurring during the development and progression of MSD in farmers, and that one or several of these protein biomarkers might eventually be used to identify and prevent work-related MSD.

No MeSH data available.


Related in: MedlinePlus

Comparison between plasma protein separation in pI range of 3–10 (a) and 4–7 (b). The marked areas are some example of the improved resolution using IPGs 4–7
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Fig1: Comparison between plasma protein separation in pI range of 3–10 (a) and 4–7 (b). The marked areas are some example of the improved resolution using IPGs 4–7

Mentions: To determine proper 2DE conditions for the analysis to be made, plasma proteins were separated in the pI ranges 3–10 and 4–7 (first dimension) followed by SDS-PAGE (second dimension). As illustrated in Fig. 1, most of the spots detected in pI range 3–10 were also detected in the pI range 4–7 (about 90 %). The marked areas in Fig. 1 illustrate the good resolving power when using IPGs in pI range 4–7 compared to 3–10. A few proteins (Fig. 1a, dashed squares9 with pI outside the 4–7 range were lost. Due to the good separation in the pI range 4–7 we decided to analyze all samples using IPGs 4–7. Mapping of the plasma proteome in the pI range 4–7 was performed by mass spectrometry. Seventy five spots could be identified (Table 2, Fig. 2). According to the accession number these identified protein spots represent 20 different proteins. Several of the identified proteins were expressed as different isoforms due to post- translational modifications such as glycosylation and phosphorylation.Fig. 1


Biomarkers of systemic inflammation in farmers with musculoskeletal disorders; a plasma proteomic study.

Ghafouri B, Carlsson A, Holmberg S, Thelin A, Tagesson C - BMC Musculoskelet Disord (2016)

Comparison between plasma protein separation in pI range of 3–10 (a) and 4–7 (b). The marked areas are some example of the improved resolution using IPGs 4–7
© Copyright Policy - OpenAccess
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4862124&req=5

Fig1: Comparison between plasma protein separation in pI range of 3–10 (a) and 4–7 (b). The marked areas are some example of the improved resolution using IPGs 4–7
Mentions: To determine proper 2DE conditions for the analysis to be made, plasma proteins were separated in the pI ranges 3–10 and 4–7 (first dimension) followed by SDS-PAGE (second dimension). As illustrated in Fig. 1, most of the spots detected in pI range 3–10 were also detected in the pI range 4–7 (about 90 %). The marked areas in Fig. 1 illustrate the good resolving power when using IPGs in pI range 4–7 compared to 3–10. A few proteins (Fig. 1a, dashed squares9 with pI outside the 4–7 range were lost. Due to the good separation in the pI range 4–7 we decided to analyze all samples using IPGs 4–7. Mapping of the plasma proteome in the pI range 4–7 was performed by mass spectrometry. Seventy five spots could be identified (Table 2, Fig. 2). According to the accession number these identified protein spots represent 20 different proteins. Several of the identified proteins were expressed as different isoforms due to post- translational modifications such as glycosylation and phosphorylation.Fig. 1

Bottom Line: The levels of leucine-rich alpha-2-glycoprotein, haptoglobin, complement factor B, serotransferrin, one isoform of kininogen, one isoform of alpha-1-antitrypsin, and two isoforms of hemopexin were higher in farmers with MSD than in referents.On the other hand, the levels of alpha-2-HS-glycoprotein, alpha-1B-glycoprotein, vitamin D- binding protein, apolipoprotein A1, antithrombin, one isoform of kininogen, and one isoform of alpha-1-antitrypsin were lower in farmers than in referents.Farmers with MSD had altered plasma levels of protein biomarkers compared to the referents, indicating that farmers with MSD may be subject to a more systemic inflammation.

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, Linköping, SE-581 85, Sweden. bijar.ghafouri@liu.se.

ABSTRACT

Background: Farmers have an increased risk for musculoskeletal disorders (MSD) such as osteoarthritis of the hip, low back pain, and neck and upper limb complaints. The underlying mechanisms are not fully understood. Work-related exposures and inflammatory responses might be involved. Our objective was to identify plasma proteins that differentiated farmers with MSD from rural referents.

Methods: Plasma samples from 13 farmers with MSD and rural referents were included in the investigation. Gel based proteomics was used for protein analysis and proteins that differed significantly between the groups were identified by mass spectrometry.

Results: In total, 15 proteins differed significantly between the groups. The levels of leucine-rich alpha-2-glycoprotein, haptoglobin, complement factor B, serotransferrin, one isoform of kininogen, one isoform of alpha-1-antitrypsin, and two isoforms of hemopexin were higher in farmers with MSD than in referents. On the other hand, the levels of alpha-2-HS-glycoprotein, alpha-1B-glycoprotein, vitamin D- binding protein, apolipoprotein A1, antithrombin, one isoform of kininogen, and one isoform of alpha-1-antitrypsin were lower in farmers than in referents. Many of the identified proteins are known to be involved in inflammation.

Conclusions: Farmers with MSD had altered plasma levels of protein biomarkers compared to the referents, indicating that farmers with MSD may be subject to a more systemic inflammation. It is possible that the identified differences of proteins may give clues to the biochemical changes occurring during the development and progression of MSD in farmers, and that one or several of these protein biomarkers might eventually be used to identify and prevent work-related MSD.

No MeSH data available.


Related in: MedlinePlus