Islas / Qin Thermal Sensors

1. Auflage 2014
ISBN: 978-0-12-800448-7
Verlag: Elsevier Science & Techn.
Format: EPUB
Kopierschutz: 6 - ePub Watermark

E-Book, Englisch, Band Volume 74, 394 Seiten

Reihe: Current Topics in Membranes

Current Topics in Membranes is targeted toward scientists and researchers in biochemistry and molecular and cellular biology, providing the necessary membrane research to assist them in discovering the current state of a particular field and in learning where that field is heading. This volume presents an up to date presentation of current knowledge and problems in the field of thermal receptors. This is a rapidly evolving research area and the book contains important contributions from some of the leaders in the field. - Written by leading experts - Contains original material, both textual and illustrative, that should become a very relevant reference material - The material is presented in a very comprehensive manner - Both researchers in the field and general readers should find relevant and up-to-date information

Autoren/Hrsg.

Islas, León

Qin, Feng

Inhaltsverzeichnis

1;Front
Cover;1
2;CURRENT TOPICS IN MEMBRANES, VOLUME 74;3
3;Current Topics in Membranes;4
4;Copyright;5
5;CONTENTS;6
6;CONTRIBUTORS;10
7;PREFACE;14
8;PREVIOUS VOLUMES IN SERIES;16
9;Chapter One - Thermal Effects and Sensitivity of Biological Membranes;20
9.1;1. INTRODUCTION;20
9.2;2. RESPONSE OF ORGANISMS TO CHANGES IN TEMPERATURE;21
9.3;3. GENERAL THERMAL DEPENDENCE OF MEMBRANE PROPERTIES;24
9.4;4. PYROELECTRICITY;28
9.5;5. INFRA RED RADIATION AND CAPACITANCE;29
9.6;6. ACTIVATION OF SPECIFIC CHANNELS BY IR;31
9.7;7. CONCLUSIONS;32
9.8;ACKNOWLEDGMENTS;32
9.9;REFERENCES;32
10;Chapter Two - Temperature Sensing by Thermal TRP Channels: Thermodynamic Basis and Molecular Insights;38
10.1;1. INTRODUCTION;39
10.2;2. PRINCIPLES OF TEMPERATURE ACTIVATION;41
10.3;3. TEMPERATURE DEPENDENCE OF THERMAL TRP CHANNELS;43
10.4;4. KINETICS AND ENERGETICS OF THERMAL CHANNELS;46
10.5;5. HYSTERESIS OF TEMPERATURE-DEPENDENT GATING;49
10.6;6. HEAT CAPACITY THEORY;51
10.7;7. ORIGINS OF THERMAL SENSITIVITY;54
10.8;8. DISTRIBUTION OF THERMAL SENSITIVITY: GLOBAL OR LOCAL?;56
10.9;9. IDENTIFICATION OF MOLECULAR BASIS OF THERMAL SENSITIVITY;59
10.10;10. SUMMARY;65
10.11;REFERENCES;65
11;Chapter Three - Gating of Thermally Activated Channels;70
11.1;1. INTRODUCTION;71
11.2;2. TEMPERATURE-SENSITIVE CHANNEL DIVERSITY;74
11.3;3. ENERGETICS OF TEMPERATURE-SENSITIVE CHANNELS;80
11.4;4. GATING KINETICS IN THERMOTRP CHANNELS;86
11.5;5. MOLECULAR DETERMINANTS OF TEMPERATURE SENSING IN TRP CHANNELS;91
11.6;6. CODA;97
11.7;ACKNOWLEDGMENTS;99
11.8;REFERENCES;99
12;Chapter Four - TRPA1 Channels: Chemical and Temperature Sensitivity;108
12.1;1. INTRODUCTION;109
12.2;2. ACTIVATION AND REGULATION OF TRPA1 BY CHEMICAL COMPOUNDS;110
12.3;3. TEMPERATURE SENSITIVITY OF TRPA1;120
12.4;ACKNOWLEDGMENTS;126
12.5;REFERENCES;126
13;Chapter Five - Temperature Sensitivity of Two-Pore (K2P) Potassium Channels;132
13.1;1. INTRODUCTION;133
13.2;PHYSIOLOGICAL ROLE OF HEAT-ACTIVATED K2P CHANNELS;134
13.3;3. MOLECULAR MECHANISM OF TEMPERATURE GATING OF TREK-1, TREK-2, AND TRAAK;136
13.4;4. HEAT- AND MECHANOSENSITIVITY OF K2PS: DIFFERENT FACETS OF THE SAME PROCESS?;143
13.5;5. FUTURE STUDIES OF K2P CHANNEL THERMAL SENSITIVITY;144
13.6;ACKNOWLEDGMENTS;146
13.7;REFERENCES;146
14;Chapter Six - Lipid Modulation of Thermal Transient Receptor Potential Channels;154
14.1;1. INTRODUCTION;155
14.2;2. PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE (PIP2);158
14.3;3. GPCR SIGNALING PATHWAYS;167
14.4;4. N-3 PUFAS AND DERIVATIVES;174
14.5;5. OXIDIZED LIPIDS;176
14.6;6. LYSOPHOSPHOLIPIDS;177
14.7;7. CHOLESTEROL AND STEROIDS;179
14.8;8. OTHER LIPIDS;181
14.9;9. CONCLUDING REMARKS;182
14.10;ACKNOWLEDGMENTS;183
14.11;REFERENCES;183
15;Chapter Seven - Structure of Thermally Activated TRP Channels;200
15.1;1. INTRODUCTION;201
15.2;2. TRP CHANNELS AS THERMAL SENSORS;203
15.3;3. OUTLOOK AND PROSPECTIVE;222
15.4;REFERENCES;223
16;Chapter Eight - Thermal Sensitivity of CLC and TMEM16 Chloride Channels and Transporters;232
16.1;1. INTRODUCTION;232
16.2;2. THERMAL NOCICEPTION;233
16.3;3. TMEM16A;234
16.4;4. CLC PROTEINS;238
16.5;5. CONCLUSIONS;245
16.6;ACKNOWLEDGMENTS;245
16.7;REFERENCES;245
17;Chapter Nine - Structure and Function of the ThermoTRP Channel Pore;252
17.1;1. INTRODUCTION;253
17.2;2. STRUCTURAL FEATURES OF A THERMOTRP CHANNEL PORE;254
17.3;3. FUNCTIONAL TESTS OF PORE STRUCTURES;257
17.4;4. ACTIVATION GATING OF TRPV1;262
17.5;5. PORE DILATION;269
17.6;6. CONCLUDING REMARKS;271
17.7;ACKNOWLEDGMENTS;272
17.8;REFERENCES;272
18;Chapter Ten - Temperature-Sensitive Gating of Voltage-Gated Proton Channels;278
18.1;1. INTRODUCTION;279
18.2;2. PROPERTIES AND PHYSIOLOGICAL FUNCTIONS OF HV;280
18.3;3. THERMOSENSITIVE FUNCTIONS OF CELLS EXPRESSING HV;285
18.4;4. TEMPERATURE DEPENDENCE OF NATIVE HV;288
18.5;5. MOLECULAR STRUCTURE OF HV1/VSOP;289
18.6;6. THERMAL STABILITY OF THE COILED-COIL DOMAIN AND THE THERMAL SENSITIVITY OF HV;296
18.7;7. MODEL OF THERMOSENSITIVE CHANNEL GATING;305
18.8;REFERENCES;307
19;Chapter Eleven - Intimacies and Physiological Role of the Polymodal Cold-Sensitive Ion Channel TRPM8;312
19.1;1. INTRODUCTION;313
19.2;2. TRPM8, A COLD-ACTIVATED POLYMODAL ION CHANNEL;313
19.3;3. PHYSIOLOGICAL ROLE OF TRPM8;319
19.4;4. TRAFFICKING, N-GLYCOSYLATION AND MODULATION OF TRPM8 CHANNEL FUNCTION;327
19.5;5. CONCLUSIONS;336
19.6;ACKNOWLEDGMENTS;336
19.7;REFERENCES;337
20;Chapter Twelve - Thermally Activated TRPV3 Channels;344
20.1;1. INTRODUCTION;345
20.2;2. EXPRESSION AND FUNCTION OF TRPV3;347
20.3;3. TRPV3 ACTIVATORS;360
20.4;4. TRPV3 REGULATORS;368
20.5;5. CONCLUSIONS;374
20.6;ACKNOWLEDGMENTS;374
20.7;REFERENCES;375
21;Index;384
22;COLOR PLATES;396

Leseproben

Chapter Two Temperature Sensing by Thermal TRP Channels
Thermodynamic Basis and Molecular Insights
Qin Feng     Department of Physiology and Biophysics, State University of New York, Buffalo, New York, USA Abstract
All organisms need to sense temperature in order to survive and adapt. But how they detect and perceive temperature remains poorly understood. Recent discoveries of thermal Transient Receptor Potential (TRP) ion channels have shed light on the problem and unravel molecular entities for temperature detection and transduction in mammals. Thermal TRP channels belong to the large family of transient receptor potential channels. They are directly activated by heat or cold in physiologically relevant temperature ranges, and the activation is exquisitely sensitive to temperature changes. Thermodynamically, this strong temperature dependence of thermal channels occurs due to large enthalpy and entropy changes associated with channel opening. Thus understanding how the channel proteins obtain their exceptionally large energetics is central toward determining functional mechanisms of thermal TRP channels. The purpose of this chapter is to provide a comprehensive review on critical issues and challenges facing the problem, with emphases on underlying biophysical and molecular mechanisms. Keywords
Temperature-dependent gating; Temperature sensor; Thermal receptors; TRP channels 1. Introduction
The detection of ambient temperature is necessary for most organisms to seek preferred living temperatures and to avoid potentially damaging conditions. The detection of internal body temperature is also required for species capable of thermal regulation. In some species thermal sensation has even become the sixth sense. Snakes possess heat vision to detect a temperature difference between a moving prey and its surroundings on the scale of milliKelvins (Bulloc & Dieck, 1956). Fire-chasing beetles can sense infrared radiation produced by fires up to 130 km (Hart, 1998; Schmitz & Bleckmann, 1998). Despite such remarkable features, however, how temperature is detected, perceived, and regulated remains poorly understood in most organisms. Thermal sensation in mammals involves peripheral sensory nerves innervating the skin and internal organs. The other end of the nerves enters the central nervous systems in the superficial dorsal horn of the spinal cord and end in the thalamus and somatosensory cortex where consciousness is made about what is happening on the surface—warm, cool, hot, or cold. As early as 1882, Blix discovered that a person's thermal sensations were associated with the stimulation of localized sensory spots on the skin (Blix, 1882). The modern pursuit of thermal sensation based on electrical recordings from skin-nerve preparations demonstrated unequivocally the existence of thermoreceptors (Hensel, 1974; Spray, 1986). On the basis of their conduction velocities, they are known to be small-diameter, slowly conducting unmyelinated C fibers and larger, more rapidly conducting, thinly myelinated Ad fibers. The sensations of temperature and pain are closely related. They both involve the C fibers, which are responsive to noxious thermal, mechanical, and chemical stimuli. The pain evoked by heat produces a sensation of burning (LaMotte & Campbell, 1978; Torebjork & Hallin, 1973), whereas the pain induced by cold can have various qualities including aching, burning, and pricking (Chery-Croze, 1983; Kreh et al., 1984; Lewis & Love, 1926; Rainville et al., 1992; Wahren, Torebjork, & Jorum, 1989; Wolf & Hardy, 1941; Yarnitsky & Ochoa, 1990). Temperatures that are normally innocuous can become noxious under pathological conditions (Julius & Basbaum, 2001; Levine et al., 1999; Sato et al., 2000; Takahashi, Sato, & Mizumura, 2003). Many forms of clinical pain are related to disorders of thermal sensation. Although cutaneous thermal receptors had been implied decades ago, their molecular entities have only begun to emerge recently. Capsaicin-activated ion channels are well known for their roles in nociception and underlie the hallmark sensitivity of nociceptive neurons to chili peppers (Jancso, 1955; Jancso, Jancso-Gabor, & Szolcsanyi, 1967; Szolcsanyi & Jancso-Gabor, 1975, 1976; Wood, 1993). The seminal study of cloning and characterization of the channel leads to identification of the first molecular transducer in thermal sensation and nociception (Caterina et al., 1997). Subsequent searches for its homologs uncover a large number of related proteins in mammalian genomes. Collectively these channels fund the now rapidly growing transient receptor potential superfamily. Today, the TRP family contains 28 members and falls into seven main subfamilies (Clapham, 2003), TRPC (canonical), TRPV (vanilloid), TRPM (mela-statin), TRPP (polycystin), TRPML (mucolipin), TRPA (ankyrin), and TRPN (NOMPC). Several members across different subfamilies have been found to be activated by temperature with distinct thermal properties. Their responsiveness ranges are correlated well with physiological temperatures causing the sensations of warm, cool, hot, and cold, thus supporting a general role for these thermal TRP channels in nociception and thermal sensation (Patapoutian et al., 2003). Plant-derived natural products that mimic temperature sensations also activate thermal TRP channels (Xu et al., 2006). The disruption of thermal TRP genes in mice results in deficient thermal sensitivity and reduced chemical and thermal hyperalgesia (Bautista et al., 2007; Caterina et al., 2000; Davis et al., 2000; Dhaka et al., 2007; Moqrich et al., 2005). Both pharmacological and behavioral characteristics support thermal TRP channels as key components on thermal and pain transduction pathways. Thermal TRP channels are not only essential to acute nociception but are also substrates of chronic inflammatory mediators released in pathological pain states. It has been suggested that they contribute to such physiopathological conditions as inflammatory hyperalgesia, diabetic neuropathy, neuropathic pain associated with nerve lesion, etc. (Akbar et al., 2008; Cantero-Recasens et al., 2010; Engler et al., 2007; Meents, Neeb, & Reuter, 2010; Szallasi, 2002; Tsavaler et al., 2001; Valdes et al., 2011; Wondergem & Bartley, 2009; Wondergem et al., 2008; Yamamura et al., 2008). Owing to their significant roles in chronic pain, thermal TRP channels have become attractive targets for development of novel pain therapies that prevent generation and transduction of pain (Szallasi, Cruz, & Geppetti, 2006; TRPM, 2011). Exquisite thermal sensitivity is a unique feature of thermal TRP channels and underlies their biological functions. All ion channels are sensitive to temperature, but few are directly activated by temperature and none has a sensitivity close to that of thermal TRP channels. Q10 is a common measurement of temperature dependence of a protein and describes the fold-change in response when temperature is increased by 10°. Whereas most ion channels have a Q10 in the range of 2–3 (DeCoursey & Cherny, 1998; Hille, 2001), thermal TRP channels reach a Q10 > 100 (Leffler et al., 2007; Yao, Liu, & Qin, 2010a, 2010b, 2011). This strong temperature dependence enables thermal TRP channels to discriminate small temperature gradients, but it also raises interesting questions on how these channels obtain the unusually strong thermal sensitivity. Presently, there is still a limited understanding of the issue owing to inherent complexity of the problem. Compared to voltage- or ligand-gated channels, the study of thermal TRP channels is still in its infancy. Below we will provide an overview on the status of the field, focusing on the biophysical and thermodynamic mechanisms and the molecular basis underlying the thermal sensitivity of the channels. 2. Principles of Temperature Activation
By Boltzmann equation the opening of an ion channel is determined by its free energy difference between the closed state and the open state (Hille, 2001): o=11+e?GRT where ?G is the free energy change and R and T have their standard definitions. The free energy change is temperature dependent and can be represented explicitly in T by ?G = ?H - T ?S where ?H and ?S are enthalpy change and entropy change, respectively. Thus the opening of a channel is related to temperature by o=11+e?HRT-?SR. This simple equation indicates that the thermal sensitivity of a channel lies in the enthalpy change during opening. The sign of the enthalpy change dictates the polarity of the thermal sensitivity: the channel is heat sensitive if ?H > 0 and conversely cold sensitive. The opening becomes temperature independent if the net enthalpy change is vanished, which could occur if the opening and closing rates involve...