Protein sulphydryl depression during adjuvant arthritis.

Abstract

. Protein sulphydryl depression during adjuvant arthritis. The changes in plasma protein sulphydryl level were measured during the course of adjuvant-induced arthritis in rats. Major depressions in the plasma sulphydryl level occurred at the onset of adjuvant disease, and the extent of the depression was related to the severity of the disease. Plasma sulphydryl levels remain unchanged when the systemic arthritis is suppressed by inclusion of a competing antigen in the adjuvant. Changes in sulphydryl content of the plasma were shown not to be due to weight loss or decrease in plasma protein level. Materials and methodsFor all experimental and control groups, 5 male Lewis strain rats (Microbiological Associates) weighing 150-250 g initially, were used. Adjuvant arthritis was induced by intradermal injection of 010 ml Freund's complete adjuvant into a foot pad of the left hind paw. The adjuvant was prepared by suspending Mycobacterium butyricum (Difco Laboratories) in paraffin oil (6-0 mg/ml).The arthritis score was used as an index of the severity of the AA and was determined by observation of the extent of swelling, lesions, and redness of each joint, including the tail, with scores of 0 to 4 being assigned to each joint. The maximum score for one animal was 20.Blood samples were collected into heparinized tubes by amputation of the tip of the tail. Plasma protein SH was determined radiochemically by addition of 0-1 ml plasma to 0-2 ml 203Hg p-chloromercuribenzene sulphonic acid (PCMBS, 1-18 mmol/l in 0 09 % NaCl), to a final volume of 1 5 ml with water followed by precipitation with 1-5 ml of 7 % trichloroacetic acid (TCA) and centrifugation.Precipitates were washed twice with 3-750% TCA, and protein bound 203Hg in the precipitates was counted in a well scintillation spectrometer. When larger sample volumes were available, serum sulphydryl levels were also measured by argentometric titration, and no significant differences were found. In those occasional samples which showed signs of haemolysis, corrections were made for heme protein SH in the plasma samples by determining (before TCA precipitation) the heme peak at 415 nm in both the plasma sample and an appropriately diluted haemolysate of cells from the same animal. The haemolysate was analysed for SH in the same manner as the

Protective effect of Withania somnifera root powder in relation to lipid peroxidation, antioxidant status, glycoproteins and bone collagen on adjuvant‐induced arthritis in rats

“…From the literature reviewed, it is apparent that RA is exposed to oxidative stress and is prone to lipid peroxidation [39]. Protein-sulfydryl level reduction may be due to the activation of inflammatory mediators [46]. Similar results have been reported by Geetha et al [40] and Ramprasad et al [41].…”

“…Protein-sulfydryl groups play an important role in the destruction of peroxides formed during phagocytosis by granulocytes. Protein-sulfydryl level reduction may be due to the activation of inflammatory mediators [46]. Vitamins C and E were significantly reduced in arthritic rats.…”

Luminol dependent chemiluminescence and thiol group oxidation provoked by neutrophils is attributable to different oxidizing species

“…Depressed thiol levels are found in serum and synovial fluid of patients with active rheumatoid disease and may be indicative of oxygen metabolite mediated structural modification of proteins at sites of disease activity (Lorber et al, 1975). Although albumin is responsible for up to 90% of total serum thiol levels (Thomas and Evans, 1975) a small proportion can be accounted for by the 0.2 moles/mole of free thiol found on IgG (Buchwald and Connell, 1974) The consequences to the biological functions of IgG of oxidation of its thiol groups by reactive oxygen metabolites, including the metastable oxidant reported here, may be of crucial importance in the pathogenesis of rheumatoid arthritis and require further investigation.…”