Detection of antibodies against glucose 6-phosphate isomerase in synovial fluid of rheumatoid arthritis using surface plasmon resonance (BIAcore)

Kim, Ji Yeon; Lee, Mi Hong; Jung, Kyung In; Na, Hye Young; Suk, Hoon; Ko, Eunyoung; Kim, Tae Jin

doi:10.1038/emm.2003.42

Cited by 30 publications

(13 citation statements)

References 23 publications

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“…However, sera that recognized p56 did not react with recombinant p53 and antibodies specific to p53 did not stain partially purified p56 (not shown). Analysis of tryptic peptides revealed a homology of p56 with neuroleukin or glucose-6-phosphate isomerase, the enzyme which was reported to be an autoantigen in autoimmune diseases [30,31]. Further studies are designed to identify p56 definitively.…”

Section: Discussionmentioning

confidence: 99%

Serum Antibodies to Retinal Antigens in Lung Cancer and Sarcoidosis

et al. 2004

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Objective: Autoantibodies to various neuronal proteins frequently accompany lung cancer and their appearance may precede cancer symptoms. In this study we examined which retinal antigens (RAs) are recognized by sera of patients with lung cancer and whether the occurrence of serum antibodies to particular RAs is characteristic for cancer in comparison with a noncancer lung disease. Methods: Sera of 72 patients with non-small-cell lung cancer (NSCLC), 29 with small-cell lung cancer (SCLC), 27 with sarcoidosis (S), and sera of 32 healthy donors were examined in immunoblotting using retinal extracts and purified RAs as antigens. Results: 69.0% of SCLC, 45.8% of NSCLC, and 44.4% of S sera displayed anti-RAs reactivity. Significantly less (p < 0.05; χ² test) percent of healthy control sera reacted with RAs. Lung cancer sera recognized mainly 46-, 56-, and 36-kD and to a smaller extent also 96-, 72-, 43-, and 26-kD proteins. Most of them were recognized with about 2-fold lower frequencies by S and control sera. Only lung cancer sera contained very high-titer antibodies to 46- and 26-kD RAs, identified as α-enolase and recoverin, respectively. Conclusion: Antibodies to RAs occur more frequently and in higher titers in lung cancer (especially SCLC) than in sarcoidosis or control sera. Although antibodies to retinal α-enolase, recoverin and other RAs are present mainly or exclusively in lung cancer sera, none of them seems to be a specific marker of a particular disease.

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Section: Discussionmentioning

confidence: 99%

Serum Antibodies to Retinal Antigens in Lung Cancer and Sarcoidosis

et al. 2004

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“…Kinetic interactions of TSK114, infliximab, and adalimumab with TNF-α were measured at 25 o C using a Biacore 2000 SPR biosensor (Biacore AB, Uppsala, Sewden) as described previously (Kim et al, 2003(Kim et al, , 2006. After immobilization of the antibodies onto the carboxymethylated dextran surface of a CM5 sensor chip at a level of about 2,500-3,000 response units, 60 µl of serially diluted human TNF-α in a buffer containing 10 mM HEPES (pH 7.4), 150 mM NaCl, 3 mM EDTA, and 0.005% polysorbate was injected into the flow cell at a rate of 30 µl/min (Gil et al, 2002).…”

Section: Surface Plasmon Resonance (Spr)mentioning

confidence: 99%

Characterization of a novel anti-human TNF-α murine monoclonal antibody with high binding affinity and neutralizing activity

et al. 2008

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In order to develop an anti-human TNF-α mAb, mice were immunized with recombinant human TNF-α. A murine mAb, TSK114, which showed the highest binding activity for human TNF-α was selected and characterized. TSK114 specifically bound to human TNF-α without cross-reactivity with the homologous murine TNF-α and human TNF-β. TSK114 was found to be of IgG1 isotype with κ light chain. The nucleotide sequences of the variable regions of TSK114 heavy and light chains were determined and analyzed for the usage of gene families for the variable (V), diversity (D), and joining (J) segments. Kinetic analysis of TSK114 binding to human TNF-α by surface plasmon resonance technique revealed a binding affinity (KD) of ~5.3 pM, which is about 1,000-and 100-fold higher than those of clinically relevant infliximab (Remicade) and adalimumab (Humira) mAbs, respectively. TSK114 neutralized human TNF-α-mediated cytotoxicity in proportion to the concentration, exhibiting about 4-fold greater efficiency than those of infliximab and adalimumab in WEHI 164 cells used as an in vitro model system. These results suggest that TSK114 has the potential to be developed into a therapeutic TNF-α-neutralizing antibody with picomolar affinity.

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“…[10][11][12][13][14] To quantify anti-GPI Ab concentrations as mg/ml of IgG, a human IgG anti-GPI Ab standard was prepared by affinity purification of sera from patients with RA with high titre anti-GPI Abs. Analysis of the purified human anti-GPI IgG showed that the antibody preparation bound specifically to hGPI (but minimally to a panel of control antigens, fig 1A) and had a functional affinity comparable to that of serum from 60 day old arthritic K/BxN mice ( fig 1B).…”

Section: Detection Of Anti-gpi Abs In Serum and Sfmentioning

confidence: 99%

“…8 The presence of anti-GPI Abs in sera from patients with RA has been confirmed by others, albeit in most studies at a frequency lower than we observed. [10][11][12][13][14] B lymphocyte stimulator (BLyS), a recently identified member of the tumour necrosis factor ligand superfamily, [15][16][17][18][19][20] if given in vivo to mice induces B cell expansion and polyclonal hypergammaglobulinaemia, 15 which is, at least in part, a consequence of inhibition of B cell apoptosis and enhanced B cell survival. [21][22][23][24] Constitutive overexpression of BLyS in blystransgenic mice leads to raised serum titres of multiple autoantibodies, including anti-dsDNA and rheumatoid factor (RF) autoantibodies.…”

mentioning

confidence: 99%