Voltage dependence of calcium current deactivation in the somatic membrane of mouse sensory neurons

1988 ◽  
Vol 20 (2) ◽  
pp. 137-143
Author(s):  
R. E. Shirokov
Keyword(s):  
Sensory Neurons ◽  
Calcium Current ◽  
Voltage Dependence ◽  
Somatic Membrane

scholarly journals 5-HT Inhibits Calcium Current and Synaptic Transmission from Sensory Neurons in Lamprey

1997 ◽  
Vol 17 (5) ◽  
pp. 1786-1794 ◽  
Author(s):  
Abdeljabbar El Manira ◽  
Weiqi Zhang ◽  
Erik Svensson ◽  
Nathalie Bussières
Keyword(s):  
Synaptic Transmission ◽  
Sensory Neurons ◽  
Calcium Current

scholarly journals Cell-Specific Alterations of T-Type Calcium Current in Painful Diabetic Neuropathy Enhance Excitability of Sensory Neurons

2007 ◽  
Vol 27 (12) ◽  
pp. 3305-3316 ◽  
Author(s):  
M. M. Jagodic ◽  
S. Pathirathna ◽  
M. T. Nelson ◽  
S. Mancuso ◽  
P. M. Joksovic ◽  
...  
Keyword(s):  
Diabetic Neuropathy ◽  
Sensory Neurons ◽  
Calcium Current ◽  
Painful Diabetic Neuropathy

Voltage-activated potassium currents in the somatic membrane of sensory neurons of early postnatal rats

1998 ◽  
Vol 30 (1) ◽  
pp. 19-27
Author(s):  
D. A. Vasilyev ◽  
N. S. Veselovsky ◽  
S. A. Fedulova
Keyword(s):  
Sensory Neurons ◽  
Potassium Currents ◽  
Somatic Membrane ◽  
Postnatal Rats

Opioid modulation of calcium current in cultured sensory neurons: μ-modulation of baroreceptor input

1999 ◽  
Vol 277 (2) ◽  
pp. H705-H713 ◽  
Author(s):  
Mary Hamra ◽  
Robert S. McNeil ◽  
Martin Runciman ◽  
Diana L. Kunze
Keyword(s):  
G Protein ◽  
Sensory Neurons ◽  
Mechanism Of Action ◽  
Pertussis Toxin ◽  
Calcium Current ◽  
Receptor Agonist ◽  
Age Groups ◽  
Opiate Receptor ◽  
Μ Opiate Receptor ◽  
Patch Technique

We used the whole cell open-patch or perforated-patch technique to characterize μ-opioid modulation of Ca2+ current ( I Ca) in nodose sensory neurons and in a specific subpopulation of nodose cells, aortic baroreceptor neurons. The μ-opiate receptor agonist Tyr-d-Ala-Gly-MePhe-Gly-ol enkephalin (DAGO) inhibited I Ca in 95% of neonatal [postnatal day (P)1–P3] nodose neurons. To the contrary, only 64% of juvenile cells (P20–P35) and 61% of adult cells (P60–P110) responded to DAGO. DAGO-mediated inhibition of I Ca was naloxone sensitive, irreversible in the presence of guanosine 5′- O-(3-thiotriphosphate), absent with guanosine 5′- O-(2-thiodiphosphate), and eliminated with pertussis toxin; DAGO’s inhibition of I Ca was G protein mediated. Incubation of neurons with ω-conotoxin GVIA eliminated the effect of DAGO in neonatal but not in juvenile cells. In the latter, DAGO reduced 37% of the current remaining in the presence of ω-conotoxin. In the subset of nodose neurons, aortic baroafferents, the effect of DAGO was concentration dependent, with an IC50 of 1.82 × 10−8 M. DAGO slowed activation of I Ca, but activation curves constructed from tail currents were the same with and without DAGO (100 nM). In summary, μ-opiate modulation of I Ca in nodose neurons was demonstrated in three age groups, including specifically labeled baroafferents. The demonstration of a mechanism of action of μ-opioids on baroreceptor afferents provides a basis for the attenuation of the baroreflex that occurs at the level of the nucleus tractus solitarii.

scholarly journals Decay of the slow calcium current in twitch muscle fibers of the frog is influenced by intracellular EGTA.

1989 ◽  
Vol 94 (5) ◽  
pp. 953-969 ◽  
Author(s):  
F Francini ◽  
E Stefani
Keyword(s):  
Rate Constant ◽  
Calcium Current ◽  
Voltage Dependence ◽  
Muscle Fibers ◽  
Calcium Depletion ◽  
Similar Time ◽  
Internal Solution ◽  
Gap Technique ◽  
Long Pulse ◽  
Single Exponential

The mechanism(s) of the decay of slow calcium current (ICa) in cut twitch skeletal muscle fibers of the frog were studied in voltage-clamp experiments using the double vaseline-gap technique. ICa decay followed a single exponential in 10 mM external Ca2+ and 20 mM internal EGTA solutions in all pulse protocols tested: single depolarizing pulses (activation protocol), two pulses (inactivation protocol), and during a long pulse preceded by a short prepulse (400 ms) to 80 mV (tail protocol). In single pulses the rate constant of ICa decay was approximately 0.75 s-1 at 0 mV and became faster with larger depolarizations. ICa had different amplitudes during the second pulses of the inactivation protocol (0 mV) and of the tail protocol (-20 to 40 mV) and had similar time constants of decay. The time constant of decay did not change significantly at each potential after replacing 10 mM Ca2+ with a Ca2+-buffered solution with malate. With 70 mM intracellular EGTA and 10 mM external Ca2+ solutions, ICa also decayed with a single-exponential curve, but it was about four times faster (approximately 3.5 s-1 at 0 mV pulse). In these solutions the rate constant showed a direct relationship with ICa amplitude at different potentials. With 70 mM EGTA, replacing the external 10 mM Ca2+ solution with the Ca2+-buffered solution caused the decay of ICa to become slower and to have the same relationship with membrane potential and ICa amplitude as in fibers with 20 mM EGTA internal solution. The mechanism of ICa decay depends on the intracellular EGTA concentration: (a) internal EGTA (both 20 and 70 mM) significantly reduces the voltage dependence of the inactivation process and (b) 70 mM EGTA dramatically increases the rate of tubular calcium depletion during the flow of ICa.

scholarly journals The voltage dependence of the TMEM16B/anoctamin2 calcium-activated chloride channel is modified by mutations in the first putative intracellular loop

2012 ◽  
Vol 139 (4) ◽  
pp. 285-294 ◽  
Author(s):  
Valentina Cenedese ◽  
Giulia Betto ◽  
Fulvio Celsi ◽  
O. Lijo Cherian ◽  
Simone Pifferi ◽  
...  
Keyword(s):  
Structure Function ◽  
Sensory Neurons ◽  
Molecular Mechanisms ◽  
Voltage Dependence ◽  
Cell Voltage ◽  
Site Directed Mutagenesis ◽  
Initial Structure ◽  
Intracellular Loop ◽  
Retinal Photoreceptors ◽  
Cl Channels

Ca2+-activated Cl− channels (CaCCs) are involved in several physiological processes. Recently, TMEM16A/anoctamin1 and TMEM16B/anoctamin2 have been shown to function as CaCCs, but very little information is available on the structure–function relations of these channels. TMEM16B is expressed in the cilia of olfactory sensory neurons, in microvilli of vomeronasal sensory neurons, and in the synaptic terminals of retinal photoreceptors. Here, we have performed the first site-directed mutagenesis study on TMEM16B to understand the molecular mechanisms of voltage and Ca2+ dependence. We have mutated amino acids in the first putative intracellular loop and measured the properties of the wild-type and mutant TMEM16B channels expressed in HEK 293T cells using the whole cell voltage-clamp technique in the presence of various intracellular Ca2+ concentrations. We mutated E367 into glutamine or deleted the five consecutive glutamates 386EEEEE390 and 399EYE401. The EYE deletion did not significantly modify the apparent Ca2+ dependence nor the voltage dependence of channel activation. E367Q and deletion of the five glutamates did not greatly affect the apparent Ca2+ affinity but modified the voltage dependence, shifting the conductance–voltage relations toward more positive voltages. These findings indicate that glutamates E367 and 386EEEEE390 in the first intracellular putative loop play an important role in the voltage dependence of TMEM16B, thus providing an initial structure–function study for this channel.

scholarly journals Prostaglandin E 2 inhibits calcium current in two sub‐populations of acutely isolated mouse trigeminal sensory neurons

2002 ◽  
Vol 539 (2) ◽  
pp. 433-444 ◽  
Author(s):  
Stephanie L. Borgland ◽  
Mark Connor ◽  
Renae M. Ryan ◽  
Helen J. Ball ◽  
MacDonald J. Christie
Keyword(s):  
Sensory Neurons ◽  
Calcium Current ◽  
Prostaglandin E

Steady-state characteristics of the proton receptor in the somatic membrane of rat sensory neurons

1984 ◽  
Vol 15 (6) ◽  
pp. 469-474
Author(s):  
A. O. Korkushko ◽  
O. A. Kryshtal' ◽  
N. I. Chernevskaya
Keyword(s):  
Steady State ◽  
Sensory Neurons ◽  
Somatic Membrane
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