Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0039483 (giant cell arteritis)
 3,204 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Sera from patients with giant cell arteritis and/or polymyalgia rheumatica have been found to contain increased levels of circulating immune complexes (IC). Results with the polyethyleneglycol precipitation complement consumption (PEG-CC) assay have been correlated with disease activity. 44% of samples from an active untreated group (21 patients) had increased levels of ICs compared with 23% from an inactive treated group (49 patients). Further analysis of circulating ICs was performed by 125I-Clq binding, the PEG-C4 test, and 125I-conglutinin binding assays. Although we did not find a high correlation between IC levels and disease activity, isolation and analysis of the ICs may lead to further understanding of this disorder.
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PMID:Circulating immune complexes in polymyalgia rheumatica and giant cell arteritis. 725 27

We report on the use of PDMS multichannels for affinity studies of DNA aptamer-human Immunoglobulin E (IgE) interactions by surface plasmon resonance imaging (SPRi). The sensing surface was prepared with thiol-terminated aptamers through a self-assembling process in the PDMS channels defined on a gold substrate. Cysteamine was codeposited with the thiol aptamers to promote proper spatial arrangement of the aptamers and thus maintain their optimal binding efficiencies. Four aptamers with different nucleic acid sequences were studied to test their interaction affinity toward IgE, and the results confirmed that aptamer I (5'-SH-GGG GCA CGT TTA TCC GTC CCT CCT AGT GGC GTG CCC C-3') has the strongest binding affinity. Control experiments were conducted with a PEG-functionalized surface and IgG was used to replace IgE in order to verify the selective binding of aptamer I to the IgE molecules. A linear concentration-dependent relationship between IgE and aptamer I was obtained, and a 2-nM detection limit was achieved. SPRi data were further analyzed by global fitting, and the dissociation constant of aptamer I-IgE complex was found to be 2.7 x 10(-7) M, which agrees relatively well with the values reported in the literature. Aptamer affinity screening by SPR imaging demonstrates marked advantages over competing methods because it does not require labeling, can be used in real-time, and is potentially high-throughput. The ability to provide both qualitative and quantitative results on a multichannel chip further establishes SPRi as a powerful tool for the study of biological interactions in a multiplexed format.
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PMID:Surface plasmon resonance imaging for affinity analysis of aptamer-protein interactions with PDMS microfluidic chips. 1767 82