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Miao R, Ding B, Zhang Y, et al. Proteomic profiling change during the early development of silicosis disease. J Thorac Dis. 2016;8(3):329-41doi: 10.21037/jtd.2016.02.46.
Miao, R., Ding, B., Zhang, Y., Xia, Q., Li, Y., & Zhu, B. (2016). Proteomic profiling change during the early development of silicosis disease. Journal of thoracic disease, 8(3), 329-41. https://doi.org/10.21037/jtd.2016.02.46
Miao, Rongming, et al. "Proteomic profiling change during the early development of silicosis disease." Journal of thoracic disease vol. 8,3 (2016): 329-41. doi: https://doi.org/10.21037/jtd.2016.02.46
Miao R, Ding B, Zhang Y, Xia Q, Li Y, Zhu B. Proteomic profiling change during the early development of silicosis disease. J Thorac Dis. 2016 Mar;8(3):329-41. doi: 10.21037/jtd.2016.02.46. PMID: 27076927; PMCID: PMC4805820.
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J Thorac Dis. 2016 Mar;8(3):329-41. doi: 10.21037/jtd.2016.02.46.

Proteomic profiling change during the early development of silicosis disease.

Journal of thoracic disease

Rongming Miao, Bangmei Ding, Yingyi Zhang, Qian Xia, Yong Li, Baoli Zhu

Affiliations

  1. 1 The 8th People's Hospital of Wuxi, Wuxi 210024, China ; 2 Jiangsu Provincial Center for Disease Prevention and Control, Nanjing 210009, China.

PMID: 27076927 PMCID: PMC4805820 DOI: 10.21037/jtd.2016.02.46

Abstract

BACKGROUND: Silicosis is one of several severe occupational diseases for which effective diagnostic tools during early development are currently unavailable. In this study we focused on proteomic profiling during the early stages of silicosis to investigate the pathophysiology and identify the proteins involved.

METHODS: Two-dimensional (2D) gel electrophoresis and MALDI-TOF-MS were used to assess the proteomic differences between healthy individuals (HI), dust-exposed workers without silicosis (DEW) and silicosis patients (SP). Proteins abundances that differed by a factor of two-fold or greater were subjected to more detailed analysis, and enzyme linked to immunosorbent assay (ELISA) was employed to correlate with protein expression data.

RESULTS: Compared with HI, 42 proteins were more abundant and 8 were less abundant in DEW, and these were also differentially accumulated in SP. Closer inspection revealed that serine protease granzyme A, alpha-1-B-glycoprotein (A1BG) and the T4 surface glycoprotein precursor (TSGP) were among the up-regulated proteins in DEW and SP. Significant changes in serine proteases, glycoproteins and proto-oncogenes may be associated with the response to cytotoxicity and infectious pathogens by activation of T cells, positive regulation of extracellular matrix structural constituents and immune response, and fibroblast proliferation. Up-regulation of cytokines included TNFs, interferon beta precursor, interleukin 6, atypical chemokine receptor 2, TNFR13BV, and mutant IL-17F may be involved in the increased and persistent immune response and fibrosis that occurred during silicosis development.

CONCLUSIONS: Granzymes, glycoproteins, cytokines and immune factors were dramatically involved in the immune response, metabolism, signal regulation and fibrosis during the early development of silicosis. Proteomic profiling has expanded our understanding of the pathogenesis of silicosis, and identified a number of targets that may be potential biomarkers for early diagnosis of this debilitating disease.

Keywords: Cytokines; fibrosis; immune response; proteomic profiling; silicosis

References

  1. J Med Invest. 1999 Aug;46(3-4):151-8 - PubMed
  2. Proc Natl Acad Sci U S A. 1998 Dec 8;95(25):14863-8 - PubMed
  3. Am J Respir Cell Mol Biol. 1994 Nov;11(5):522-30 - PubMed
  4. Am J Respir Cell Mol Biol. 1997 Oct;17(4):501-7 - PubMed
  5. Curr Opin Immunol. 2003 Oct;15(5):553-9 - PubMed
  6. Mol Biol Cell. 2012 Mar;23(6):1010-23 - PubMed
  7. Bioinformatics. 2004 Jun 12;20(9):1453-4 - PubMed
  8. J Biomed Biotechnol. 2012;2012:492608 - PubMed
  9. Nucleic Acids Res. 2008 Jun;36(10):3420-35 - PubMed
  10. Exp Mol Pathol. 2003 Aug;75(1):68-73 - PubMed
  11. Science. 1992 Jan 17;255(5042):306-12 - PubMed
  12. J Biol Chem. 1986 Feb 15;261(5):1998-2002 - PubMed
  13. Genes Immun. 2009 Sep;10(6):566-78 - PubMed
  14. Am J Respir Cell Mol Biol. 1993 Nov;9(5):475-83 - PubMed
  15. Arch Pathol Lab Med. 1988 Jul;112(7):673-720 - PubMed
  16. Bioinformatics. 2005 Sep 15;21(18):3674-6 - PubMed
  17. Oncol Lett. 2014 Aug;8(2):939-947 - PubMed
  18. Mol Cell Biochem. 2002 May-Jun;234-235(1-2):177-84 - PubMed
  19. Blood. 2014 Aug 21;124(8):1266-76 - PubMed
  20. J Clin Pathol. 2004 Dec;57(12):1292-8 - PubMed
  21. J Rheumatol. 2013 Mar;40(3):219-27 - PubMed
  22. Cell. 1988 Aug 12;54(4):541-52 - PubMed
  23. Am J Respir Crit Care Med. 1999 Oct;160(4):1274-82 - PubMed
  24. Proteomics. 2012 Apr;12(8):1244-52 - PubMed
  25. Am Rev Respir Dis. 1987 Dec;136(6):1429-34 - PubMed
  26. Eur Respir J. 1994 Mar;7(3):515-8 - PubMed
  27. Electrophoresis. 1999 Dec;20(18):3551-67 - PubMed
  28. Eur J Immunol. 2009 Feb;39(2):342-51 - PubMed
  29. Gene. 2001 Sep 19;275(2):217-21 - PubMed
  30. Int J Exp Pathol. 1995 Aug;76(4):287-98 - PubMed
  31. Histol Histopathol. 1991 Jul;6(3):395-402 - PubMed
  32. J Immunol. 2004 Jul 15;173(2):807-17 - PubMed
  33. Free Radic Biol Med. 2003 Jun 15;34(12):1507-16 - PubMed
  34. J Histochem Cytochem. 1994 Aug;42(8):1061-70 - PubMed
  35. Am J Respir Cell Mol Biol. 1994 Oct;11(4):426-31 - PubMed
  36. Am J Respir Crit Care Med. 1998 May;157(5 Pt 1):1666-80 - PubMed
  37. Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3299-303 - PubMed
  38. Toxicol Lett. 1995 Dec;82-83:483-9 - PubMed
  39. Proc Natl Acad Sci U S A. 1995 Aug 29;92(18):8458-62 - PubMed

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