scholarly journals Building a Temperature-Sensitive Ion Channel

Cell ◽  
2014 ◽  
Vol 158 (5) ◽  
pp. 977-979 ◽  
Author(s):  
Ming-Feng Tsai ◽  
Christopher Miller
Keyword(s):  
Ion Channel ◽  
Temperature Sensitive

scholarly journals The Temperature-Sensitive Ion Channel TRPV2 is Endogenously Expressed and Functional in the Primary Sensory Cell Line F-11

2005 ◽  
Vol 15 (1-4) ◽  
pp. 183-194 ◽  
Author(s):  
Florian Bender ◽  
Michael Mederos y Schnitzler ◽  
Yanzhang Li ◽  
Ailing Ji ◽  
Eberhard Weihe ◽  
...  
Keyword(s):  
Ion Channel ◽  
Cell Line ◽  
Sensory Cell ◽  
Temperature Sensitive

scholarly journals Rapid characterisation of hERG channel kinetics II: temperature dependence

2019 ◽  
Author(s):  
Chon Lok Lei ◽  
Michael Clerx ◽  
Kylie A. Beattie ◽  
Dario Melgari ◽  
Jules C. Hancox ◽  
...  
Keyword(s):  
Ion Channel ◽  
Temperature Dependence ◽  
Kinetic Parameters ◽  
Room Temperature ◽  
Herg Channel ◽  
Rate Theory ◽  
Temperature Sensitive ◽  
Channel Kinetics ◽  
Voltage Dependent ◽  
The Many

ABSTRACTIon channel behaviour can depend strongly on temperature, with faster kinetics at physiological temperatures leading to considerable changes in currents relative to room temperature. These temperature-dependent changes in voltage-dependent ion channel kinetics (rates of opening, closing and inactivating) are commonly represented with Q10coefficients or an Eyring relationship. In this paper we assess the validity of these representations by characterising channel kinetics at multiple temperatures. We focus on the hERG channel, which is important in drug safety assessment and commonly screened at room temperature, so that results require extrapolation to physiological temperature. In Part I of this study we established a reliable method for high-throughput characterisation of hERG1a (Kv11.1) kinetics, using a 15 second information-rich optimised protocol. In this Part II, we use this protocol to study the temperature dependence of hERG kinetics using CHO cells over-expressing hERG1a on the Nanion SyncroPatch 384PE, a 384-well automated patch clamp platform, with temperature control. We characterise the temperature dependence of hERG gating by fitting the parameters of a mathematical model of hERG kinetics to data obtained at five distinct temperatures between 25 and 37 °C, and validate the models using different protocols. Our models reveal that activation is far more temperature sensitive than inactivation, and we observe that the temperature dependency of the kinetic parameters is not represented well by Q10coefficients: it broadly follows a generalised, but not the standardly-used, Eyring relationship. We also demonstrate that experimental estimations of Q10coefficients are protocol-dependent. Our results show that a direct fit using our 15 second protocol best represents hERG kinetics at any given temperature, and suggests that predictions from the Generalised Eyring theory may be preferentially used if no experimentally-derived data are available.Statement of SignificanceIon channel currents are highly sensitive to temperature changes. Yet because many experiments are performed more easily at room temperature, it is common to extrapolate findings to physiological temperatures through the use of Q10coefficients or Eyring rate theory. By applying short, information-rich protocols that we developed in Part I of this study we identify how kinetic parameters change over temperature. We find that the commonly-used Q10and Eyring formulations are incapable of describing the parameters’ temperature dependence, a more Generalised Eyring relationship works well, but remeasuring kinetics and refitting a model is optimal. The findings have implications for the accuracy of the many applications of Q10coefficients in electrophysiology, and suggest that care is needed to avoid misleading extrapolations in their many scientific and industrial pharmaceutical applications.

scholarly journals Noninvasive Near-Infrared Light Triggers Remote Activation of Thermo-Responsive TRPV1 Channels in Neurons Based on Biodegradable/Photothermal Polymer Micelles

Nanoscale ◽  
2022 ◽  
Author(s):  
Wei-Hsu Chen ◽  
Taiki Onoe ◽  
Masao Kamimura
Keyword(s):  
Ion Channel ◽  
Near Infrared ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Cation Channel ◽  
Infrared Light ◽  
Temperature Sensitive ◽  
Polymer Micelle ◽  
Trpv1 Channels ◽  
Transient Receptor

In this study, we developed a novel biodegradable/photothermal polymer micelle-based remote-activation method for a temperature-sensitive ion channel, namely transient receptor potential cation channel subfamily V member 1 (TRPV1). Biodegradable/photothermal polymer...

scholarly journals Mutation of the Axonal Transport Motor Kinesin Enhances paralytic and Suppresses Shaker in Drosophila

Genetics ◽  
1996 ◽  
Vol 142 (1) ◽  
pp. 195-204 ◽  
Author(s):  
Daryl D Hurd ◽  
Michael Stern ◽  
William M Saxton
Keyword(s):  
Ion Channel ◽  
Axonal Transport ◽  
Sodium Channels ◽  
Synthetic Lethality ◽  
Genetic Interactions ◽  
Temperature Sensitive ◽  
Channel Activity ◽  
Synergistic Enhancement ◽  
Anterograde Axonal Transport ◽  
Physiological Tests

To investigate the possibility that kinesin transports vesicles bearing proteins essential for ion channel activity, the effects of kinesin (Khc) and ion channel mutations were compared in Drosophila using established tests. Our results show that Khc mutations produce defects and genetic interactions characteristic of paralytic (para) and maleless (mle) mutations that cause reduced expression or function of the alpha-subunit of voltage-gated sodium channels. Like para and mle mutations, Khc mutations cause temperature-sensitive (TS) paralysis. When combined with para or mle mutations, Khc mutations cause synthetic lethality and a synergistic enhancement of TS-paralysis. Furthermore, Khc mutations suppress Shaker and ether-a-go-go mutations that disrupt potassium channel activity. In light of previous physiological tests that show that Khc mutations inhibit compound action potential propagation in segmental nerves, these data indicate that kinesin activity is required for normal inward sodium currents during neuronal action potentials. Tests for phenotypic similarities and genetic interactions between kinesin and sodium/potassium ATPase mutations suggest that impaired kinesin function does not affect the driving force on sodium ions. We hypothesize that a loss of kinesin function inhibits the anterograde axonal transport of vesicles bearing sodium channels.

Oncogenesis and the Lucké Virus

1968 ◽  
Vol 26 ◽  
pp. 200-201
Author(s):  
A. E. Vatter ◽  
J. Zambernard
Keyword(s):  
Rna Viruses ◽  
Vegetative State ◽  
Temperature Sensitive ◽  
Structural Level ◽  
Oncogenic Viruses ◽  
Dna Viruses ◽  
Leopard Frogs ◽  
Renal Adenocarcinoma ◽  
Induced Tumors ◽  
Northern Leopard Frogs

Oncogenic viruses, like viruses in general, can be divided into two classes, those that contain deoxyribonucleic acid (DNA) and those that contain ribonucleic acid (RNA). The RNA viruses have been recovered readily from the tumors which they cause whereas, the DNA-virus induced tumors have not yielded the virus. Since DNA viruses cannot be recovered, the bulk of present day investigations have been concerned with RNA viruses.The Lucké renal adenocarcinoma is a spontaneous tumor which occurs in northern leopard frogs (Rana pipiens) and has received increased attention in recent years because of its probable viral etiology. This hypothesis was first advanced by Lucké after he observed intranuclear inclusions in some of the tumor cells. Tumors with inclusions were examined at the fine structural level by Fawcett who showed that they contained immature and mature virus˗like particles.The use of this system in the study of oncogenic tumors offers several unique features, the virus has been shown to contain DNA and it can be recovered from the tumor, also, it is temperature sensitive. This latter feature is of importance because the virus can be transformed from a latent to a vegetative state by lowering or elevating the environmental temperature.

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