An electrogenic K(+) transport in the tormogen cell of insect chemosensilla is involved in the generation and maintenance of the transepithelial potential (TEP). To gain more information about the K(+) transport system underlying the TEP generation and the location of its components in the plasma membrane of the tormogen cell, we studied the effects of inhibitors of K(+)/H(+) P-ATPase (bafilomycin A1, omeprazole and Na-orthovanadate), of K(+)/Cl(-) co-transport (bumetanide), of Cl(-) channels (NPPB) and of a K(+) channel blocker (BaCl(2)). The relationship between TEP amplitude and spike firing activity was also studied. Experiments were performed on the labellar chemosensilla of the blowfly Protophormia terraenovae using a modified tip-recording technique. Results show that: (a) K(+)/H(+) P-ATPase inhibitors significantly decrease the TEP, when properly applied to the labellum for 20 min, so as to reach the basolateral side of the plasma membrane, while no effect was detected when applied to the apical side, (b) bumetanide, NPPB and BaCl(2) decrease the TEP value only when administered to the apical side, (c) spike activity is positively correlated with the TEP. A model is proposed of the active and passive K(+) transports sustaining the TEP associated with the blowfly chemosensilla.
We revisit the transport of spin-degrees of freedom across an electrically
And thermally biased tunnel junction between two ferromagnets with
Non-collinear magnetizations. Besides the well-known charge and spin currents
We show that a non-zero spin-quadrupole current flows between the ferromagnets....
The electronic transport properties of an SNS junction formed by an InN
nanowire (N) and Al contacts (S) with a superconducting transition temperature
T_c ~ 0.92 K were investigated. As a function of dc bias, superconducting
quasiparticle transport resonance peaks at E=2\Delta were observed, in
I hypothesize that
Plasmodium falciparum has an Achilles' heel that can be attacked with
erythritol, the well-known sweetener that is classified as generally safe. Most
organisms have in their cell membrane two types of water-channel proteins:
aquaporins to maintain hydro-homeostasis across the memb...
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