In order to control the spread of COVID-19, social distancing measures were implemented in many countries. This study investigated changes in air pollution during the social distancing after the COVID-19 outbreak in Korea. Ambient PM 2.5 , PM 10 , NO 2 , and CO that are particularly related to industrial activities and traffic were reduced during the social distancing in response to the COVID-19 outbreak. In March 2020, immediately after social distancing, mean levels of PM 2.5 , PM 10 , NO 2 , and CO decreased nationwide from last year's mean levels by 16.98 μg/m 3 , 21.61 μg/m 3 , 4.16 ppb, and 0.09 ppm, respectively ( p -value for the year-to-year difference < 0.001 , =0.001 , =0.008 , <0.001 ), a decrease by 45.45%, 35.56%, 20.41%, and 17.33%, respectively. Changes in ambient O 3 or SO 2 were not observed to be attributable to social distancing. Our findings, that such effort for a short period of time resulted in a significant reduction in air pollution, may point toward reducing air pollution as a public health problem in a more sustainable post-COVID-19 world.

Ca(2+)-permeable cation channels consisting of canonical transient receptor potential 1 (TRPC1) proteins mediate Ca(2+) influx pathways in vascular smooth muscle cells (VSMCs), which regulate physiological and pathological functions. We investigated properties conferred by TRPC1 proteins to native single TRPC channels in acutely isolated mesenteric artery VSMCs from wild-type (WT) and TRPC1-deficient (TRPC1(-/-)) mice using patch-clamp techniques. In WT VSMCs, the intracellular Ca(2+) store-depleting agents cyclopiazonic acid (CPA) and 1,2-bis-(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid (BAPTA-AM) both evoked channel currents, which had unitary conductances of ∼2 pS. In TRPC1(-/-) VSMCs, CPA-induced channel currents had 3 subconductance states of 14, 32, and 53 pS. Passive depletion of intracellular Ca(2+) stores activated whole-cell cation currents in WT but not TRPC1(-/-) VSMCs. Differential blocking actions of anti-TRPC antibodies and coimmunoprecipitation studies revealed that CPA induced heteromeric TRPC1/C5 channels in WT VSMCs and TRPC5 channels in TRPC1(-/-) VSMCs. CPA-evoked TRPC1/C5 channel activity was prevented by the protein kinase C (PKC) inhibitor chelerythrine. In addition, the PKC activator phorbol 12,13-dibutyrate (PDBu), a PKC catalytic subunit, and phosphatidylinositol-4,5-bisphosphate (PIP(2)) and phosphatidylinositol-3,4,5-trisphosphate (PIP(3)) activated TRPC1/C5 channel activity, which was prevented by chelerythrine. In contrast, CPA-evoked TRPC5 channel activity was potentiated by chelerythrine, and inhibited by PDBu, PIP(2), and PIP(3). TRPC5 channels in TRPC1(-/-) VSMCs were activated by increasing intracellular Ca(2+) concentrations ([Ca(2+)](i)), whereas increasing [Ca(2+)](i) had no effect in WT VSMCs. We conclude that agents that deplete intracellular Ca(2+) stores activate native heteromeric TRPC1/C5 channels in VSMCs, and that TRPC1 subunits are important in determining unitary conductance and conferring channel activation by PKC, PIP(2), and PIP(3).

The human and rat forms of the Kv2.1 channel have identical amino acids over the membrane-spanning regions and differ only in the N-and C-terminal intracellular regions. Rat Kv2.1 activates much faster than human Kv2.1. Here we have studied the role of the N-and C-terminal residues that determine this difference in activation kinetics between the two channels. For this, we constructed mutants and chimeras between the two channels, expressed them in oocytes, and recorded currents by two-electrode voltage clamping. In the N-terminal region, mutation Q67E in the rat channel displayed a slowing of activation relative to rat wild type, whereas mutation D75E in the human channel showed faster activation than human wild type. In the C-terminal region, we found that some residues within the region of amino acids 740 -853 ("CTA" domain) were also involved in determining activation kinetics. The electrophysiological data also suggested interactions between the N and C termini. Such an interaction was confirmed directly by using a glutathione S-transferase (GST) fusion protein with the N terminus of Kv2.1, which we showed to bind to the C terminus of Kv2.1. Taken together, these data suggest that exposed residues in the T1 domain of the N terminus, as well as the CTA domain in the C terminus, are important in determining channel activation kinetics and that these N-and C-terminal regions interact.

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The goal of this study was to design a robot system for assisting in the rehabilitation of patients with neuromuscular disorders by performing various facilitation movements. The robot should be able to guide patient's wrist to move along planned linear or circular trajectories. A hybrid position/force controller incorporating fuzzy logic was developed to constrain the movement in the desired direction and to maintain a constant force along the moving direction. The controller was stable in the application range of movements and forces. Offline analyses of data were used to quantitatively assess the progress of rehabilitation. The results show that the robot could guide the upper limbs of subjects in linear and circular movements under predefined external force levels and apply a desired force along the tangential direction of the movements.

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We report the molecular cloning from foetal brain of the human potassium channel heag2. The cDNA encodes a protein of 988 amino acids, 73% identical to heag1. Heag2 is expressed in the brain, but is also found in a range of tissues including skeletal muscle. In oocytes, the channel is a non-inactivating outward recti¢er, with dependence of activation rate on holding potential. Compared with heag1, the conductancev oltage curve for heag2 was shifted to the left, the voltage sensitivity was less, activation kinetics were di¡erent, and the sensitivity to terfenadine was lower. The heag2 channel may have important physiological roles. ß 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

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