Protein carbonyls and protein thiols in rheumatoid arthritis


  • Pullaiah P. Department of Biochemistry, SV Institute of Medical Sciences, Tirupati, Andhra Pradesh, India
  • Suchitra M. M. Department of Biochemistry, SV Institute of Medical Sciences, Tirupati, Andhra Pradesh, India
  • Siddhartha Kumar B. Department of Medicine, SV Institute of Medical Sciences, Tirupati, Andhra Pradesh, India



Antioxidant, Oxidative stress, Protein carbonyl content, Protein thiols, Protein oxidation


Background: Oxidative stress (OS) has an important role in the pathogenesis and progression of rheumatoid arthritis (RA). OS causes protein modification, thereby impairing the biological functions of the protein. This study was conducted to assess the oxidatively modified protein as protein carbonyl content and the antioxidant status as protein thiols, and to study the association between protein carbonyls and protein thiols in RA.

Methods: Newly diagnosed RA patients who were not taking any disease modifying anti-rheumatic drugs were included into the study group (n=45) along with age and sex matched healthy controls (n=45). Serum protein carbonyl content and protein thiols were estimated.

Results: Elevated protein carbonyl content and decreased protein thiol levels (p<0.001) were observed in RA. A significant negative correlation was observed between protein carbonyl content and protein thiol levels (p<0.001).

Conclusions: Oxidative stress in RA is evidenced by enhanced protein oxidation and decreased antioxidant protein thiol levels. Decreased protein thiols may also reflect protein modifications leading to compromise in the antioxidant properties. This oxidant and antioxidant imbalance needs to be addressed by therapeutic interventions to prevent disease progression.


Mcinnes IB, Schett G. The pathogenesis of rheumatoid arthritis. New England J medicine. 2011;365(23):2205-19.

Haris ED. Pathogenesis of rheumatoid arthritis. In: Kelley WN, editor. Textbook of Rheumatology. Philadelphia W. B. Saunders; 1989:905-42.

Ozturk HS, Cimen MYB, Cimen OB, Kacmaz M, Drek J. Oxidant/antioxidant status of plasma samples from patients with rheumatoid arthritis. Rheumatol Int. 1999;19:35-7.

Mahajan A, Tandon VR. Antioxidants and rheumatoid arthritis. J Indian Rheumatol Assoc. 2004;12:139-42.

Grune T, Reinheckel T, Joshi M, Davies KJA. Proteolysis in cultured liver epithelial cells during oxidative stress-role of the multicatalytic proteinase complex, proteasome. J Biol Chem. 1995;270:2344-51.

Grune T, Reinheckel T, Davies KJA. Degradation of oxi dized proteins in K562 human hematopoietic cells by proteasome. J Biol Chem. 1996;271:15504-9.

Andrew MP and Kelvin JAD. Degradation of damaged proteins-the main function of the 20s proteasome. Prog Mol Biol Transl Sci. 2012;109:227-48.

Helen RGN, Irundika HKD, Rachel SW, Andrew D. Redox regulation of protein damage in plasma. Redox Biology. 2014;2:430-5.

Serteser M, Evcik D, Koken T, Kahraman A. Changes in protein sulfhydryls, protein carbonyls and lipid peroxidation levels in sera of patients with rheumatoid arthritis: correlation with disease activity. Rheumatism. 2006;21(1):18-22.

Frank CA, Steven ME, Daniel AB, Dennis JMS, James FF, Norman SC, et al. The American Rheumatism Association 1987 Revised criteria for the classification of rheumatoid arthritis. Arthritis and Rheumatism. 1998;31(3):315-24.

Levine RL, Garland D, Oliver CN, Anici A, Lenz AG, Ahn B, et al. Determination of Carbonyl content in oxidatively modified proteins. Methods in Enzymology. 1990;186:464-78.

Motchnik AP, Frei B, Ames NB. Measurement of antioxidants in human blood plasma: protein thiols. In: Packer L, editor. Methods in Enzymology. California, Academic Press. 1994:273-4.

Mazzetti I, Grigolo B, Pulsatelli L, Dolzani P, Silvestri T, Rosetti L, et al. Differential roles of nitric oxide and oxygen radicals in chondrocytes affected by osteoarthritis and rheumatoid arthritis. Clin Sci. 2001;101:593-9.

Amara A, Constans J, Chaugier C, Sebban A, Dubourg L, Peuchant E, et al. Autoantibodies to malondialdehyde-modified epitope in connective tissue diseases and vasculitis. Clin Exp Immunol. 1995;101:233-8.

Alturfan AA, Uslu E, Alturfan EE, Hatemi G, Fresko I, Kokoglu E. Increased Serum Sialic Acid Levels in Primary Osteoarthritis and Inactive Rheumatoid Arthritis. Tohoku J Experimental Medicine. 2007;213(3): 41-8.

Mantle D, Falkous G, Walker D. Quantification of protease activities in synovial fluid from rheumatoid and osteoarthritis cases: comparison with antioxidant and free radical damage markers. Clin Chem Acta. 1999;284:45-58.

Renke J, Popadiuk S, Korzon M, Bugajczyk B, Wozniak M. Protein carbonyl groups contents as a useful clinical marker of antioxidant barrier impairment in plasma of children with juvenile chronic arthritis. Free Radic Biol Med. 2000;29:101-4.

Tetik S, Ahmad S, Alturfan AA, Disbudak M, Sahin YS, et al. Determination of oxidant stress in plasma of rheumatoid arthritis and primary osteoarthritis patients. Ind J Biochem Biophysics. 2010;47:353-8.

Lemarechal H, Allanore Y, Chenevier GC, Kahan A, Ekindjian OG, Borderie D. Serum protein oxidation in patients with rheumatoid arthritis and effects of infliximab therapy. Clin Chem Acta. 2006;372:147-53.

Kalaivanam KN, Santhosh KN, Bheemasen R, Ramadas D. Evolution of protein carbonyl content as a marker of AMI. J Biotechnol Biochem. 2016;2(5):21-3.

Olena R, Philip E. Biochemical methods for monitoring protein thiol redox states in biological systems. Redox Biology. 2014;2:803-13.

Droge W, Breitkreutz R. Glutathione and immune function. Proc Nutr Soc. 2000;59:595-600.




How to Cite

P., P., M. M., S., & B., S. K. (2018). Protein carbonyls and protein thiols in rheumatoid arthritis. International Journal of Research in Medical Sciences, 6(5), 1738–1741.



Original Research Articles