2 resultados para whole-cell and single-channel patch-clamp recordings

em Digital Commons at Florida International University


Relevância:

100.00% 100.00%

Publicador:

Resumo:

The single spin asymmetry, ALT ′, and the polarized structure function, σ LT′, for the p( e&ar; , e′K +)Λ reaction in the resonance region have been measured and extracted using the CEBAF Large Acceptance Spectrometer (CLAS) at Jefferson Lab. Data were taken at an electron beam energy of 2.567 GeV. The large acceptance of CLAS allows for full azimuthal angle coverage over a large range of center-of-mass scattering angles. Results were obtained that span a range in Q 2 from 0.5 to 1.3 GeV2 and W from threshold up to 2.1 GeV and were compared to existing theoretical calculations. The polarized structure function is sensitive to the interferences between various resonant amplitudes, as well as to resonant and non-resonant amplitudes. This measurement is essential for understanding the structure of nucleons and searching for previously undetected nucleon excited states (resonances) predicted by quark models. The W dependence of the σ LT′ in the kinematic regions dominated by s and u channel exchange (cos qcmk = −0.50, −0.167, 0.167) indicated possible resonance structures not predicted by theoretical calculations. The σLT ′ behavior around W = 1.875 GeV could be the signature of a resonance predicted by the quark models and possibly seen in photoproduction. In the very forward angles where the reaction is dominated by the t-channel, the average σLT ′ was zero. There was no indication of the interference between resonances or resonant and non-resonant amplitudes. This might be indicating the dominance of a single t-channel exchange. Study of the sensitivity of the fifth structure function data to the resonance around 1900 MeV showed that these data were highly sensitive to the various assumptions of the models for the quantum number of this resonance. This project was part of a larger CLAS program to measure cross sections and polarization observables for kaon electroproduction in the nucleon resonance region. ^

Relevância:

100.00% 100.00%

Publicador:

Resumo:

C-reactive protein (CRP), a normally occurring human plasma protein may become elevated as much as 1,000 fold during disease states involving acute inflammation or tissue damage. Through its binding to phosphorylcholine in the presence of calcium, CRP has been shown to potentiate the activation of complement, stimulate phagocytosis and opsonize certain microorganisms. Utilizing a flow cytometric functional ligand binding assay I have demonstrated that a monocyte population in human peripheral blood and specific human-derived myelomonocytic cell lines reproducibly bind an evolutionarily conserved conformational pentraxin epitope on human CRP through a mechanism that does not involve its ligand, phosphorylcholine. ^ A variety of cell lines at different stages of differentiation were examined. The monocytic cell line, THP-1, bound the most CRP followed by U937 and KG-1a cells. The HL-60 cell line was induced towards either the granulocyte or monocyte pathway with DMSO or PMA, respectively. Untreated HL-60 cells or DMSO-treated cells did not bind CRP while cells treated with PMA showed increased binding of CRP, similar to U-937 cells. T cell and B-cell derived lines were negative. ^ Inhibition studies with Limulin and human SAP demonstrated that the binding site is a conserved pentraxin epitope. The calcium requirement necessary for binding to occur indicated that the cells recognize a conformational form of CRP. Phosphorylcholine did not inhibit the reaction therefore the possibility that CRP had bound to damaged membranes with exposed PC sites was discounted. ^ A study of 81 normal donors using flow cytometry demonstrated that a majority of peripheral blood monocytes (67.9 ± 1.3, mean ± sem) bound CRP. The percentage of binding was normally distributed and not affected by gender, age or ethnicity. Whole blood obtained from donors representing a variety of disease states showed a significant reduction in the level of CRP bound by monocytes in those donors classified with infection, inflammation or cancer. This reduction in monocyte populations binding CRP did not correlate with the concentration of plasma CRP. ^ The ability of monocytes to specifically bind CRP combined with the binding reactivity of the protein itself to a variety of phosphorylcholine containing substances may represent an important bridge between innate and adaptive immunity. ^