Ability to grow in vitro and character of transformation of synovial fluid cells from patients with rheumatoid arthritis

1975 ◽  
Vol 80 (5) ◽  
pp. 1380-1383
Author(s):  
L. A. Trunova ◽  
N. V. Ignatovich
2003 ◽  
Vol 48 (7) ◽  
pp. 1873-1880 ◽  
Author(s):  
Michel Neidhart ◽  
Christian A. Seemayer ◽  
Klaus M. Hummel ◽  
Beat A. Michel ◽  
Renate E. Gay ◽  
...  

2004 ◽  
Vol 24 (2) ◽  
pp. 71-76 ◽  
Author(s):  
Samuel Solomon ◽  
Madhan Masilamani ◽  
Subhasis Mohanty ◽  
J�rg E. Schwab ◽  
Eva-Maria Boneberg ◽  
...  

2013 ◽  
Vol 40 (6) ◽  
pp. 903-909 ◽  
Author(s):  
Jolanta Parada-Turska ◽  
Wojciech Zgrajka ◽  
Maria Majdan

Objective.Previously we demonstrated that kynurenic acid (KYNA), an endogenous metabolite of kynurenine, is present in the synovial fluid of patients with rheumatoid arthritis (RA). KYNA inhibits proliferation of synoviocytesin vitro. The goal of our study was to compare KYNA concentrations in synovial fluid and blood of patients with RA, inflammatory spondyloarthropathies (SpA), and osteoarthritis (OA).Methods.Serum and synovial fluid samples were obtained from 189 patients with RA, 56 patients with SpA, and 32 patients with OA. KYNA was separated using a high-performance liquid chromatography system and measured fluorometrically.Results.KYNA concentration in synovial fluid obtained from patients with RA and SpA was significantly lower than that in patients with OA (p < 0.05). The concentration of KYNA in serum of patients with RA, SpA, and OA did not differ among all groups studied. The positive correlation between KYNA content in synovial fluid and serum was found in patients with RA (p < 0.05). Univariate linear regression analysis demonstrated that fibrinogen was significantly associated with KYNA in synovial fluid (p < 0.05), and red blood cell counts, morning stiffness, and pain scores were significantly associated with KYNA level in serum (all p < 0.05). Multivariate regression analysis revealed correlation between the following independent variables: hemoglobin level, hematocrit, red blood cell count in conjunction with age and KYNA content in synovial fluid. A lack of correlation was observed between KYNA content in synovial fluid of patients with RA and other clinical and laboratory measures of disease activity.Conclusion.Our data show a local deficit of KYNA in inflammatory states.


1984 ◽  
Vol 43 (2) ◽  
pp. 222-227 ◽  
Author(s):  
B Bonvoisin ◽  
G Cordier ◽  
J P Revillard ◽  
E Lejeune ◽  
M Bouvier

Blood ◽  
1993 ◽  
Vol 81 (3) ◽  
pp. 726-733 ◽  
Author(s):  
EM Conway ◽  
B Nowakowski

Abstract Thrombomodulin (TM) is a transmembrane glycoprotein that interacts with thrombin, thereby serving as a cofactor in the activation of protein C, a major physiologically relevant natural anticoagulant. Although initially described as a vascular endothelial cell receptor, TM has also been reported to be synthesized by several cells, including megakaryocytes, platelets, monocytes, neutrophils (PMN), mesothelial cells, and synovial lining cells. A prominent feature of rheumatoid arthritis (RA) is infiltration of PMN into the joint space. To determine whether TM might play a role in the inflammatory process, we examined synovial fluid for the presence of TM in 10 patients with RA and five patients with osteoarthritis (OA). We determined that the mean synovial fluid and plasma TM levels in the OA group were 23.5 ng/mL and 24.2 ng/mL, respectively, whereas those with RA had a significantly elevated mean synovial fluid TM level of 136.2 ng/mL as compared with the plasma TM concentration of 43.9 ng/mL (P < .05). Synovial fluid TM levels did not correlate with PMN counts (r = .261). Purified TM from synovial fluid was identical in molecular weight to plasma-derived TM and was biologically functional with respect to protein C cofactor activity. Using direct immunofluorescence, we determined that adherent cultured synovial fluid cells that are not monocytoid in origin express surface and cytoplasmic TM, thereby providing an alternative source of the protein. Biologic activity of the cell-surface TM was confirmed by acceleration of thrombin-dependent protein C activation. Northern analysis of RNA extracted from the cultured cells indicated that TM messenger RNA was present, suggesting local synthesis. Our results indicate that in RA-associated synovial effusions, biologically active TM is increased, the source of which may be from plasma, PMN, and/or synovial lining cells. TM may play a regulatory role either in fibrin deposition in the inflamed joint and/or in the progression of the inflammatory process.


2005 ◽  
Vol 26 (5) ◽  
pp. 422-426 ◽  
Author(s):  
Jolanta Parada-Turska ◽  
Wojciech Rzeski ◽  
Wojciech Zgrajka ◽  
Maria Majdan ◽  
Martyna Kandefer-Szerszeń ◽  
...  

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