Morning quiet-time ionospheric current reversal at mid to high latitudes

The records of an array of magnetometers set up across the Australian mainland are examined. In addition to a well-defined current whorl corresponding to the ionospheric <i>S<sub>q</sub></i> current system, another system of eastward flowing currents is often found in the early morning. The system is most easily identified at observatories poleward of the focus of the <i>S<sub>q</sub></i> system, where a morning reversal from eastward to westward currents can be seen. The time of the reversal is usually later, sometimes up to 12h local noon, in June (Southern Winter) than in other seasons. There is some evidence of a similar current system at other longitudes and in the Northern Hemisphere. An important outcome of the study is that it enables identification of which features of a daily variation of the northward magnetic field Δ<i>X</i> relate to an <i>S<sub>q</sub></i> current whorl and which must be attributed to some other current system

Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution.

Abstract CLIC1 (NCC27) is a member of the highly conserved class of chloride ion channels that exists in both soluble and integral membrane forms. Purified CLIC1 can integrate into synthetic lipid bilayers forming a chloride channel with similar properties to those observed in vivo. The structure of the soluble form of CLIC1 has been determined at 1.4-A resolution. The protein is monomeric and structurally homologous to the glutathioneS-transferase superfamily, and it has a redox-active site resembling glutaredoxin. The structure of the complex of CLIC1 with glutathione shows that glutathione occupies the redox-active site, which is adjacent to an open, elongated slot lined by basic residues. Integration of CLIC1 into the membrane is likely to require a major structural rearrangement, probably of the N-domain (residues 1–90), with the putative transmembrane helix arising from residues in the vicinity of the redox-active site. The structure indicates that CLIC1 is likely to be controlled by redox-dependent processes

IMBALANCE OF IL -1β И IL -1RA CYTOKINES IN BLOOD SERUM AND BRONCHOALVEOLAR LAVAGE IN COPD PATIENTS

Abstract. The aim of present study was to determine levels of IL-1β and its inhibitor, IL-1ra in blood serum and bronchoalveolar lavage fluid (BALF) of 20 patients with COPD, depending on severity of their disease, activity of inflammatory process, bacterial and viral complication. Methods. Twenty male patients with COPD (stage 2 to 4) were examined. It was shown that all the patients with COPD displayed high levels of IL-1β, both in the area of inflammation, and in blood serum. The latter index was dependent on the severity of disease and activity of inflammatory process. In BALF, the contents of IL-1β in all the patients under study was significantly exceeded the normal levels of this cytokine even at the earliest stages of evolving COPD. concentration in serum was depended at stage of disease and activity of inflammatory procces. There were no differences in IL-1β concentrations in BALF of 2 - 4 stage COPD patients. IL-1ra levels in the patients’ serum were within normal levels, and tended to increase in BAL, thus causing imbalanced IL-1ra/IL-1β ratio both in the inflammatory area, as well as systemically. The maximal detection of respiratory pathogens did significantly correlate with decreased IL-1ra/ IL-1β ratio, thus confirming the data on infectious agents as a pathogenetic component in COPD

Crystal Structure of a Soluble Form of the Intracellular Chloride Ion Channel CLIC1 (NCC27) at 1.4-\uc5 Resolution

CLIC1 (NCC27) is a member of the highly conserved class of chloride ion channels that exists in both soluble and integral membrane forms. Purified CLIC1 can integrate into synthetic lipid bilayers forming a chloride channel with similar properties to those observed in vivo. The structure of the soluble form of CLIC1 has been determined at 1.4-Angstrom resolution. The protein is monomeric and structurally homologous to the glutathione S-transferase superfamily, and it has a redox-active site resembling glutaredoxin. The structure of the complex of CLIC1 with glutathione shows that glutathione occupies the redox-active site, which is adjacent to an open, elongated slot lined by basic residues. Integration of CLIC1 into the membrane is likely to require a major structural rearrangement, probably of the N-domain (residues 1-90), with the putative transmembrane helix arising from residues in the vicinity of the redox-active site. The structure indicates that CLIC1 is likely to be controlled by redox-dependent processes