1. The membrane response to applied histamine of cultured endothelial cells from human umbilical vein was studied by use of whole cell and single channel patch clamp techniques. A value of -27 +/- 1.4 mV was found for the resting potential under whole cell current clamp. No voltage-gated currents were seen at either the macroscopic or single channel levels. 2. At holding potentials of -20 to -40 mV, histamine evoked slow rising, long lasting whole cell inward currents. The inward current was associated with depolarization and decreased input resistance. The calcium ionophore A23187 provoked similar whole cell inward currents. 3. Single channel currents were observed in cell-attached and inside-out patches for both histamine and A23187. The single channel conductance was about 20 pS with a mean open time of 5 ms and a reversal potential of 0 mV in symmetrical potassium solutions. Internal sodium blocked outward going currents. 4. For cell-attached patches, histamine-dependent channel activity required external calcium and was also seen when histamine was present in the bath but not the pipette. Recording from inside-out patches revealed that decreases in 'internal' calcium resulted in the disappearance of channel activity. 5. The histamine-dependent inward current appears to involve calcium-dependent activation of cationic channels.
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http://dx.doi.org/10.1111/j.1476-5381.1988.tb11663.x | DOI Listing |
In the human heart, the binding of cyclic adenosine monophosphate (cAMP), a second messenger, to hyperpolarization and cyclic nucleotide-gated (HCN) regulates the automaticity of pacemaker cells. Recent single-molecule binding studies show that cAMP bound to each subunit of purified tetrameric HCN channels independently, in contrast to findings in cells. To explore the lipid membrane's role in cAMP regulation, we reconstituted purified human HCN channels in various lipid nanodiscs and resolved single molecule ligand-binding dynamics.
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Encapsulating living cells within nanoshells offers an important approach to enhance their stability against environmental stressors and broaden their application scope. However, this often leads to impaired mass transfer at the cell biointerface. Strengthening the protective shell with well-defined, ordered transport channels is crucial to regulating molecular transport and maintaining cell viability and biofunctionality.
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Department of Physics, Chalmers University of Technology, SE-412 96 Gothenburg, Sweden.
UV-vis spectroscopy is a workhorse in analytical chemistry that finds application in life science, organic synthesis, and energy technologies like photocatalysis. In its traditional implementation with cuvettes, it requires sample volumes in the milliliter range. Here, we show how nanofluidic scattering spectroscopy (NSS), which measures visible light scattered from a single nanochannel in a spectrally resolved way, can reduce this sample volume to the attoliter range for solute concentrations in the mM regime, which corresponds to as few as 10 probed molecules.
View Article and Find Full Text PDFNat Chem
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The synthesis of mesoporous metal-organic frameworks (meso-MOFs) is desirable as these materials can be used in various applications. However, owing to the imbalance in structural tension at the micro-scale (MOF crystallization) and the meso-scales (assembly of micelles with MOF subunits), the formation of single-crystal meso-MOFs is challenging. Here we report the preparation of uniform single-crystal meso-MOF nanoparticles with ordered mesopore channels in microporous frameworks with definite arrangements, through a cooperative assembly method co-mediated by strong and weak acids.
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