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PubMed2004

Thermosensation and pain.

We feel a wide range of temperatures spanning from cold to heat. Within this range, temperatures over about 43 degrees C and below about 15 degrees C evoke not only a thermal sensation, but also a feeling of pain. In mammals, six thermosensitive ion channels have been reported, all of which belong to the TRP (transient receptor potential) superfamily. These include TRPV1 (VR1), TRPV2 (VRL-1), TRPV3, TRPV4, TRPM8 (CMR1), and TRPA1 (ANKTM1). These channels exhibit distinct thermal activation thresholds (>43 degrees C for TRPV1, >52 degrees C for TRPV2, > approximately 34-38 degrees C for TRPV3, > approximately 27-35 degrees C for TRPV4, < approximately 25-28 degrees C for TRPM8 and <17 degrees C for TRPA1), and are expressed in primary sensory neurons as well as other tissues. The involvement of TRPV1 in thermal nociception has been demonstrated by multiple methods, including the analysis of TRPV1-deficient mice. TRPV2, TRPM8, and TRPA1 are also very likely to be involved in thermal nociception, because their activation thresholds are within the noxious range of temperatures.

Animals↗
PubMed2003

Gender and laterality differences in thermosensation throughout the perceptible range.

Several studies suggest that females exhibit greater sensitivity to experimentally induced thermal pain than males. These investigations have focused mainly on the sensory-discriminative rather than the affective aspect of pain. Moreover, potential gender differences for the affective components of innocuous thermal sensations have yet to be examined. The primary aim of the present study was to evaluate gender differences in the sensory and the affective dimensions of the entire thermosensory system, including warmth, coolness, heat pain and cold pain. The secondary aim was to evaluate laterality differences in these same perceptual dimensions and ranges. Twenty healthy females and 20 healthy males immersed their hands in water baths maintained at temperatures ranging from 10 to 47 degrees C, and rated their perceived thermal intensity, (un)pleasantness, and pain intensity. There was a progressive growth in the thermal intensity ratings as bath temperatures either increased or decreased from the adapting temperature of 33 degrees C. No gender differences emerged for these thermal intensity ratings. However, a significant sex effect emerged for the pain intensity ratings (P<0.01), and a significant sex x temperature interaction for the affective ratings (P<0.01). Females provided higher unpleasantness and pain intensity ratings for the more extreme temperatures (10, 15 and 47 degrees C), compared to males. Moreover, women perceived the milder temperature baths as more pleasant than men did. For a given painful temperature, unpleasantness ratings were higher than pain intensity ratings. This relationship between unpleasantness ratings and pain ratings was not significantly different between the sexes. No laterality differences emerged for the thermal intensity ratings. However, perceived pain intensity was significantly higher for the left as compared to the right hand (P<0.01). Ratings of unpleasantness also tended to be higher for the left vs. right hand, but this difference fell just short of statistical significance (P=0.06). These findings indicate that sex differences in thermosensory perception are not general, but occur only for the painful and affective components. Of particular note is the sex difference for affective but not intensive ratings of innocuous temperatures, revealing sex differences in thermal perception outside the nociceptive system.

Adaptation, Physiological↗
PubMed1995

Thermosensation. Some like it hot.

The ability of organisms to respond to fluctuating temperatures is ubiquitous but poorly understood. Recent studies of nematodes reveal specific sensory neurons and interneurons that mediate thermotaxis.

Animals↗
PubMed2002

Identification of a cold receptor reveals a general role for TRP channels in thermosensation.

The cellular and molecular mechanisms that enable us to sense cold are not well understood. Insights into this process have come from the use of pharmacological agents, such as menthol, that elicit a cooling sensation. Here we have characterized and cloned a menthol receptor from trigeminal sensory neurons that is also activated by thermal stimuli in the cool to cold range. This cold- and menthol-sensitive receptor, CMR1, is a member of the TRP family of excitatory ion channels, and we propose that it functions as a transducer of cold stimuli in the somatosensory system. These findings, together with our previous identification of the heat-sensitive channels VR1 and VRL-1, demonstrate that TRP channels detect temperatures over a wide range and are the principal sensors of thermal stimuli in the mammalian peripheral nervous system.

Amino Acid Sequence↗
PubMed1999

Conversion of a bacterial warm sensor to a cold sensor by methylation of a single residue in the presence of an attractant.

The aspartate chemoreceptor (Tar) of Escherichia coli also serves as a thermosensor, and it is very amenable to genetic and biochemical analysis of the thermosensing mechanism. Its thermosensing properties are controlled by reversible methylation of the cytoplasmic signalling/adaptation domain of the protein. The unmethylated and the fully methylated (aspartate-bound) receptors sense, as attractant stimuli, increases (warm sensor) and decreases (cold sensor) in temperature respectively. To learn more about the mechanism of thermosensing, we replaced the four methyl-accepting glutamyl residues with non-methylatable aspartyl residues in all possible combinations. In a strain defective in both methyltransferase (CheR) and methylesterase (CheB) activities, all of the mutant Tar proteins functioned as warm sensors. To create a situation in which all of the remaining glutamyl residues were methylated, we expressed the mutant proteins in a CheB-defective, CheR-overproducing strain. The fully glutamyl-methylated proteins were designed to mimic the full range of methylation states possible for wild-type Tar. Almost all of the methylated mutant receptors, including those with single glutamyl residues, were cold sensors in the presence of aspartate. Thus, binding of aspartate to Tar and methylation of its single glutamyl residue can invert its temperature-dependent signalling properties.

Aspartic Acid↗
PubMed2007

Temperature sensing across species.

The ability to detect changes in temperature is a fundamental sensory mechanism for every species and provides organisms with a detailed view of the environment. This review focuses on what is known of the neuronal and molecular substrates for thermosensation across species, focusing on the three robust model systems extensively used to study sensory signaling, the nematode Caenorhabditis elegans, the fruit fly Drosophila melanogaster, and the laboratory mouse. Nematodes migrate to thermal climes that are amenable to their survival, a behavior that is regulated primarily through a single sensory neuron. Additionally, nematodes "learn" to seek out this temperate zone based upon their prior experience, a robust model of learning and memory. Drosophila larvae also prefer select thermal zones that are optimal for growth and have also developed vigorous mechanisms to avoid unfavorable conditions. In mammals, the transduction mechanisms for thermosensation have been identified primarily due to the fact that naturally occurring plant products evoke distinct psychophysical sensation of temperature change. More remarkably, the elucidation of the molecular sensors in mammals, along with those in Drosophila, has demonstrated conservation in the molecular mediators of temperature sensation across diverse species.

Adaptation, Physiological↗
PubMed2004

Mutational analysis of the energetics of the GrpE.DnaK binding interface: equilibrium association constants by sedimentation velocity analytical ultracentrifugation.

DnaK, the prokaryotic Hsp70 molecular chaperone, requires the nucleotide exchange factor and heat shock protein GrpE to release ADP. GrpE and DnaK are tightly associated molecules with an extensive protein-protein interface, and in the absence of ADP, the dissociation constant for GrpE and DnaK is in the low nanomolar range. GrpE reduces the affinity of DnaK for ADP, and the reciprocal linkage is also true: ADP reduces the affinity of DnaK for GrpE. The energetic contributions of GrpE side-chains to GrpE-DnaK binding were probed by alanine-scanning mutagenesis. Sedimentation velocity (SV) analytical ultracentrifugation (AUC) was used to measure the equilibrium constants (Keq) for GrpE binding to the ATPase domain of DnaK in the presence of ADP. ADP-bound DnaK is the natural target of GrpE, and the addition of ADP (final concentration of 5 microM) to the preformed GrpE-DnaK(ATPase) complexes allowed the equilibrium association constants to be brought into an experimentally accessible range. Under these experimental conditions, the substitution of one single GrpE amino acid residue, arginine 183 with alanine, resulted in a GrpE-DnaK(ATPase) complex that was weakly associated (Keq =9.4 x 10(4) M). This residue has been previously shown to be part of a thermodynamic linkage between two structural domains of GrpE: the thermosensing long helices and the C-terminal beta-domains. Several other GrpE side-chains were found to have a significant change in the free energy of binding (DeltaDeltaG approximately 1.5 to 1.7 kcal mol(-1)), compared to wild-type GrpE.DnaK(ATPase) in the same experimental conditions. Overall, the strong interactions between GrpE and DnaK appear to be dominated by electrostatics, not unlike barnase and barstar, another well-characterized protein-protein interaction. GrpE, an inherent thermosensor, exhibits non-Arrhenius behavior with respect to its nucleotide exchange function at bacterial heat shock temperatures, and mutation of several solvent-exposed side-chains located along the thermosensing indicated that these residues are indeed important for GrpE-DnaK interactions.

Alanine↗
PubMed1995

Neural regulation of thermotaxis in Caenorhabditis elegans.

Thermal stimulus is an important environmental factor influencing animal behaviour. However, the mechanisms underlying thermosensation and thermal adaptation are poorly understood. The nematode Caenorhabditis elegans can sense a range of environmental temperatures and migrate towards the cultivation temperature on a thermal gradient. This modifiable thermotactic response provides an ideal system for studying the cellular and molecular processes involved in thermosensation and thermal information storage. We have identified neurons critical for thermotaxis by killing individual cells in live animals. The results indicate that an amphid sensory neuron, AFD, is a major thermosensory neuron. Some of the genetically defined cryophilic and thermophilic mutant phenotypes were mimicked when amphid interneurons AIY and AIZ, respectively, were killed, indicating that AIY is responsible for thermophilic movement and AIZ for cryophilic movement. We propose a neural model in which regulation of the activities of the two interneurons in opposite directions, depending on the cultivation temperature, is essential for thermotaxis.

Animals↗
PubMed1998

Temperature sensing in bacterial gene regulation--what it all boils down to.

Many bacterial gene regulatory circuits are controlled by temperature. Temperature-mediated regulation occurs at the level of transcription and translation. Supercoiling, changes in mRNA conformation and protein conformation are all implicated in thermosensing. Bacterial virulence functions are often temperature regulated and thus many an example of thermoregulation comes from pathogenic organisms. H-NS is at the crossroads of regulation in many such systems. mRNA melting has also been shown to act as a thermosensing mechanism in various contexts. Proteins can also act as temperature sensors as exemplified by the gene regulator TlpA in Salmonella typhimurium.

Bacterial Proteins↗