Analysis of the classical, alternative, and mannose binding lectin pathway of the complement system in the pathogenesis of oligoarticular juvenile idiopathic arthritis

Brunner, Juergen; Prelog, Martina; Riedl, Magdalena; Giner, Thomas; Hofer, Johannes; Würzner, Reinhard; Zimmerhackl, Lothar Bernd

doi:10.1007/s00296-011-1973-0

Cited by 8 publications

(9 citation statements)

References 9 publications

(13 reference statements)

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“…The remnant C for each pathway was determined using Wieslab Complement System Screenkits (Euro-diagnostica, Malmo, Sweden) essentially as described previously [7], [15], [16]. The kits are supplied pre-coated with specific activators for the CP, LP and AP.…”

Section: Methodsmentioning

confidence: 99%

Complement Activation by Merozoite Antigens of Plasmodium falciparum

2014

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BackgroundComplement (C) is a crucial part of the innate immune system and becomes over activated during malaria, resulting in depletion of C components, especially those for lectin pathway (LP), thereby compromising the host's innate defense. In this study, involvement of P. falciparum antigens in C activation was investigated.MethodsA highly synchronous culture of the Dd2 clone of P. falciparum was established in a serum free medium. Supernatants harvested from rings, trophozoites and schizonts at various parasite densities were tested for ability to activate C by quantifying amount of C3b deposited on erythrocytes (E). Uninfected sham culture was used as control. Remnants of each C pathway were determined using Wieslab complement System Screenkit (Euro-diagnostica, Sweden). To identify MBL binding antigens of LP, culture supernatants were added to MBL sepharose columns and trapped antigens eluted with increasing concentrations of EDTA (10 mM, 50 mM and 100 mM) and then desalted before being tested for ability to activate C. The EDTA eluate with highest activity was run on a polyacrylamide gel and silver stained proteins analyzed by mass spectroscopy.ResultsAntigens released by P. falciparum growing in culture activated C leading to C3b deposition on E. Maximal activation at 7% parasitemia was associated with schizont stage (36.7%) compared to 22% for rings, 21% for trophozoites and 3% for sham culture. All the three pathways of C were activated, with highest activation being for the alternative pathway (only 6% of C activation potential remained), 65% for classiical and 43% for the LP. Seven MBL binding merozoite proteins were identified by mass spectrometry in the 50 mM EDTA eluate.ConclusionsMBL binding merozoite adhesins with ability to activate C pathway were identified. The survival advantage for such pronounced C activation is unclear, but opsonisation could facilitate recognition and invasion of E.

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Section: Methodsmentioning

confidence: 99%

Complement Activation by Merozoite Antigens of Plasmodium falciparum

2014

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“…It has been suggested that overactivity or deficiency of some complement factors may facilitate JIA progression 9 , 10 , 11 , 12 . Those specific for lectin pathway activation have not been studied extensively.…”

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confidence: 99%

“…8 It has been suggested that overactivity or deficiency of some complement factors may facilitate JIA progression. [9][10][11][12] Those specific for lectin pathway activation have not been studied extensively. Mannose-binding lectin (MBL), ficolins and MBL-associated serine proteases (MASPs) have been detected in SF from patients suffering from rheumatoid arthritis and osteoarthritis.…”

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confidence: 99%

Lectin pathway factors in patients suffering from juvenile idiopathic arthritis

et al. 2017

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Both complement activation and certain infections (including those with Yersinia sp.) may contribute to the pathogenesis of juvenile idiopathic arthritis (JIA). We investigated factors specific for the lectin pathway of complement: mannose-binding lectin (MBL), ficolins and MBL-associated serine protease-2 (MASP-2), in 144 patients and 98 controls. One hundred and six patients had oligoarticular disease and 38 had polyarticular disease. In 51 patients (out of 133 tested), Yersinia-reactive antibodies were found (JIA Ye group). MBL deficiency was significantly more frequent in the JIA Ye group than in patients without Yersinia-reactive antibodies or in controls. Median serum ficolin-2 level was significantly lower (and proportion of values deemed ficolin-2 insufficient greater) in JIA patients irrespective of their Yersinia antibody status. The minority (C) allele at -64 of the FCN2 gene was less frequent among JIA patients than among control subjects. No differences were found in the frequency of FCN3 gene +1637delC or MASP2 +359 A>G mutations nor for median values of serum ficolin-1, ficolin-3 or MASP-2. However, high levels of serum ficolin-3 were under-represented in patients, in contrast to MBL. MBL, ficolin-1, ficolin-2, ficolin-3 and MASP-2 were also readily detectable in synovial fluid samples but at a considerably lower level than in serum. Our findings suggest a possible role for the lectin pathway in the pathogenesis of JIA, perhaps secondary to a role in host defence, and indicate that investigations on the specificity of lectin pathway recognition molecules towards specific infectious agents in JIA might be fruitful.

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“…The enzyme immunoassay (EIA) method is proposed to estimate the whole three complement activation pathways (Brunner et al, 2012;Seelen et al, 2005;Thiel, Møller-Kristensen, Jensen, & Jensenius, 2002). The principle is shown in Fig.…”

Section: Enzyme Immunoassaymentioning

confidence: 99%

Review on complement analysis method and the roles of glycosaminoglycans in the complement system

Ijaz

et al. 2015

Carbohydrate Polymers

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Analysis of the classical, alternative, and mannose binding lectin pathway of the complement system in the pathogenesis of oligoarticular juvenile idiopathic arthritis

Cited by 8 publications

References 9 publications

Complement Activation by Merozoite Antigens of Plasmodium falciparum

Complement Activation by Merozoite Antigens of Plasmodium falciparum

Lectin pathway factors in patients suffering from juvenile idiopathic arthritis

Review on complement analysis method and the roles of glycosaminoglycans in the complement system

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