Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0267964 (PAA)
 2,561 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Considering that nitric oxide (NO) may be involved in anti-tumoral and anti-parasite lectin effects, in this report we investigated whether lectin induces NO production. Lectins from Canavalia brasiliensis, Dioclea grandiflora, Pisum arvense (PAA), and concanavalin A induced murine peritoneal cells to produce NO in vitro. PAA induced similar levels to that obtained with lipopolysaccharide plus interferon-gamma. NO production by adherent cells was significantly lower than that of unfractionated cells, suggesting a combination of lectin stimuli directly on macrophages and via lymphocyte stimulation. Ex vivo experiments showed that cells stimulated in vivo could maintain NO production in vitro without further stimuli. NO synthesis blockage in vivo can significantly increase cell numbers in draining lymph nodes after lectin injection compared to unblocked controls, suggesting an in vivo association of lectin stimuli and NO production. Taken together these data show that lectins can induce NO production both in vitro and in vivo.
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PMID:Lectin-induced nitric oxide production. 1035 85

Highly efficient antibody immobilization is crucial for conducting high-performance immunoassays such as enzyme-linked immunosorbent assay (ELISA) in microarray and microfluidic biochips. In this study, a biotin-poly(L-lysine)-g-poly(ethylene glycol) (biotin-PLL-g-PEG) and protein A-based technique was developed to immobilize antibody on the surface of poly(methyl methacrylate) (PMMA) microchannels. First, PMMA surface was activated by oxygen plasma, followed by poly(acrylic acid) (PAA) grafting to add functional carboxyl group for subsequent binding. After the biotin-PLL-g-PEG molecules reacted with carboxyl groups through the electrostatic interactions, biotinylated protein A was immobilized on the surface through a linking molecule, neutravidin. To evaluate the applicability of this novel immobilization strategy, human interferon-gamma (IFN-gamma) was used as a model protein. Since protein A could better control the immobilization orientation, and the combination of biotin-PLL-g-PEG and PLL-g-PEG could adjust the conformation of antibodies, antigen capture efficiency and detection signals were significantly improved on the microchips by using this strategy. The optimal grafting conditions were also experimentally determined: the biotin grafting ratio of 0.189 in the PLL-g-PEG molecule and the mixture ratio of 85% (biotin-PLL-g-PEG to PLL-g-PEG). This surface modification can be applied for targeted drug delivery, biosensor and other immunoassay applications.
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PMID:Specific antibody immobilization with biotin-poly(L-lysine)-g-poly(ethylene glycol) and protein A on microfluidic chips. 1964 44