Cold sensing in grapevine-Which signals are upstream of the microtubular “thermometer”

2017 ◽  
Vol 40 (11) ◽  
pp. 2844-2857 ◽  
Author(s):  
Lixin Wang ◽  
Peter Nick
Keyword(s):  
Cold Sensing

scholarly journals Odontoblast TRPC5 channels signal cold pain in teeth

2021 ◽  
Vol 7 (13) ◽  
pp. eabf5567
Author(s):  
Laura Bernal ◽  
Pamela Sotelo-Hitschfeld ◽  
Christine König ◽  
Viktor Sinica ◽  
Amanda Wyatt ◽  
...  
Keyword(s):  
Relative Sensitivity ◽  
Cellular Component ◽  
Sensory Transduction ◽  
Cold Sensation ◽  
Cold Pain ◽  
Sensing System ◽  
Cold Sensitive ◽  
Cellular Components ◽  
Cold Sensor ◽  
Cold Sensing

Teeth are composed of many tissues, covered by an inflexible and obdurate enamel. Unlike most other tissues, teeth become extremely cold sensitive when inflamed. The mechanisms of this cold sensation are not understood. Here, we clarify the molecular and cellular components of the dental cold sensing system and show that sensory transduction of cold stimuli in teeth requires odontoblasts. TRPC5 is a cold sensor in healthy teeth and, with TRPA1, is sufficient for cold sensing. The odontoblast appears as the direct site of TRPC5 cold transduction and provides a mechanism for prolonged cold sensing via TRPC5’s relative sensitivity to intracellular calcium and lack of desensitization. Our data provide concrete functional evidence that equipping odontoblasts with the cold-sensor TRPC5 expands traditional odontoblast functions and renders it a previously unknown integral cellular component of the dental cold sensing system.

scholarly journals Activation of the cold-sensing TRPM8 channel triggers UCP1-dependent thermogenesis and prevents obesity

2012 ◽  
Vol 4 (2) ◽  
pp. 88-96 ◽  
Author(s):  
Shuangtao Ma ◽  
Hao Yu ◽  
Zhigang Zhao ◽  
Zhidan Luo ◽  
Jing Chen ◽  
...  
Keyword(s):  
Trpm8 Channel ◽  
Cold Sensing

scholarly journals Non-conventional Axonal Organelles Control TRPM8 Ion Channel Trafficking and Peripheral Cold Sensing

Cell Reports ◽  
2020 ◽  
Vol 30 (13) ◽  
pp. 4505-4517.e5 ◽  
Author(s):  
Víctor Hugo Cornejo ◽  
Carolina González ◽  
Matías Campos ◽  
Leslie Vargas-Saturno ◽  
María de los Ángeles Juricic ◽  
...  
Keyword(s):  
Ion Channel ◽  
Channel Trafficking ◽  
Ion Channel Trafficking ◽  
Cold Sensing

scholarly journals TRPV1 activity and substance P release are required for corneal cold nociception

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Fengxian Li ◽  
Weishan Yang ◽  
Haowu Jiang ◽  
Changxiong Guo ◽  
Andrew J. W. Huang ◽  
...  
Keyword(s):  
Substance P ◽  
Neuronal Excitability ◽  
Thermal Sensitivity ◽  
Protective Mechanism ◽  
Trpv1 Channel ◽  
Cold Stimulation ◽  
Cold Allodynia ◽  
P Release ◽  
Substance P Release ◽  
Cold Sensing

AbstractAs a protective mechanism, the cornea is sensitive to noxious stimuli. Here, we show that in mice, a high proportion of corneal TRPM8+ cold-sensing fibers express the heat-sensitive TRPV1 channel. Despite its insensitivity to cold, TRPV1 enhances membrane potential changes and electrical firing of TRPM8+ neurons in response to cold stimulation. This elevated neuronal excitability leads to augmented ocular cold nociception in mice. In a model of dry eye disease, the expression of TRPV1 in TRPM8+ cold-sensing fibers is increased, and results in severe cold allodynia. Overexpression of TRPV1 in TRPM8+ sensory neurons leads to cold allodynia in both corneal and non-corneal tissues without affecting their thermal sensitivity. TRPV1-dependent neuronal sensitization facilitates the release of the neuropeptide substance P from TRPM8+ cold-sensing neurons to signal nociception in response to cold. Our study identifies a mechanism underlying corneal cold nociception and suggests a potential target for the treatment of ocular pain.

scholarly journals Human Dental Pulp Fibroblasts Express the “Cold-sensing” Transient Receptor Potential Channels TRPA1 and TRPM8

2011 ◽  
Vol 37 (4) ◽  
pp. 473-478 ◽  
Author(s):  
Ikhlas A. El Karim ◽  
Gerard J. Linden ◽  
Timothy M. Curtis ◽  
Imad About ◽  
Mary K. McGahon ◽  
...  
Keyword(s):  
Dental Pulp ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Transient Receptor Potential Channels ◽  
Human Dental Pulp ◽  
Potential Channels ◽  
Transient Receptor ◽  
Cold Sensing

scholarly journals Clustering and Differentiation of glr-3 Gene Function and Its Homologous Proteins

2021 ◽  
Vol 3 (3) ◽  
Author(s):  
Yue Ma ◽  
Tiantian Guo ◽  
Yihe Wang ◽  
Xinna Li ◽  
Jingyu Zhang
Keyword(s):  
Secondary Structure ◽  
Protein Glycosylation ◽  
Random Coil ◽  
Homologous Gene ◽  
Phosphorylation Sites ◽  
Homologous Proteins ◽  
Homologous Genes ◽  
Glycosylation Sites ◽  
Α Helix ◽  
Cold Sensing

In order to adapt to the low temperature environment, organisms transmitexcitement to the central system through the thermal sensing system, whichis a classic reflex reaction. The cold receptor GLR-3 perceives cold and produces cold avoidance behavior through peripheral sensory neurons ASER.In order to further understand the gene encoding of the cold sensing glr-3gene and the evolution of its homologous gene group function and proteinfunction, the nucleotide sequence and amino acid sequence of the glr-3gene and its homologous gene in 24 species were obtained and compared.By clustering with the GRIK2 gene sequence of Rana chensinensis, the bioinformatics method was used to predict and sequence analyze the change ofgene, evolution rate, physical and chemical properties of protein, glycosylation sites, phosphorylation sites, secondary structure and tertiary structureof protein. The analysis results show that the glr-3 gene and its homologousgene have obvious positive selection effect. The protein prediction analysisshowed that the glr-3 gene and its homologous genes encoded proteinsin these 25 species were hydrophilic proteins, and the proportion of sidechains of aliphatic amino acids was high. The transmembrane helix waswidespread and there were more N-glycosylation sites and O-glycosylationsites. The protein phosphorylation sites encoded were serine, threonine andtyrosine phosphorylation sites. Secondary structure prediction showed thatthe secondary structure units of the encoded protein were α-helix, β-turn,random coil and extended chain, and the proportion of α-helix was the largest. This study provides useful information on the evolution and function ofthe cold sensing gene glr-3 and its homologous genes.

scholarly journals Silent cold-sensing neurons drive cold allodynia in neuropathic pain states

2020 ◽  
Author(s):  
Donald Iain MacDonald ◽  
Ana P. Luiz ◽  
Queensta Millet ◽  
Edward C. Emery ◽  
John N. Wood
Keyword(s):  
Neuropathic Pain ◽  
Calcium Imaging ◽  
De Novo ◽  
Large Diameter ◽  
Cold Sensitivity ◽  
Peripheral Sensitization ◽  
Cold Allodynia ◽  
Pain Patients ◽  
Cold Sensing

SummaryNeuropathic pain patients often experience innocuous cooling as excruciating pain. The cell and molecular basis of this cold allodynia is little understood. We used in vivo calcium imaging of sensory ganglia to investigate the activity of peripheral cold-sensing neurons in three mouse models of neuropathic pain: oxaliplatin-induced neuropathy, partial sciatic nerve ligation and ciguatera poisoning. In control mice, cold-sensing neurons were few in number and small in size. In neuropathic animals with cold allodynia, a set of normally silent large-diameter neurons became sensitive to cooling. Many silent cold-sensing neurons expressed the nociceptor markers NaV1.8 and CGRPα. Ablating these neurons diminished cold allodynia. Blocking KV1 voltage-gated potassium channels was sufficient to trigger de novo cold sensitivity in silent cold-sensing neurons. Thus silent cold-sensing neurons are unmasked in diverse neuropathic pain states and cold allodynia results from peripheral sensitization caused by altered nociceptor excitability.Graphical Abstract

scholarly journals Cold sensing by NaV1.8-positive and NaV1.8-negative sensory neurons

2019 ◽  
Vol 116 (9) ◽  
pp. 3811-3816 ◽  
Author(s):  
A. P. Luiz ◽  
D. I. MacDonald ◽  
S. Santana-Varela ◽  
Q. Millet ◽  
S. Sikandar ◽  
...  
Keyword(s):  
Sensory Neurons ◽  
Transcriptional Profiling ◽  
Relative Number ◽  
Trp Channel ◽  
Maximal Response ◽  
Cold Plate ◽  
Cold Temperatures ◽  
Extreme Cold ◽  
Cold Sensing

The ability to detect environmental cold serves as an important survival tool. The sodium channels NaV1.8 and NaV1.9, as well as the TRP channel Trpm8, have been shown to contribute to cold sensation in mice. Surprisingly, transcriptional profiling shows that NaV1.8/NaV1.9 and Trpm8 are expressed in nonoverlapping neuronal populations. Here we have used in vivo GCaMP3 imaging to identify cold-sensing populations of sensory neurons in live mice. We find that ∼80% of neurons responsive to cold down to 1 °C do not express NaV1.8, and that the genetic deletion of NaV1.8 does not affect the relative number, distribution, or maximal response of cold-sensitive neurons. Furthermore, the deletion of NaV1.8 had no observable effect on transient cold-induced (≥5 °C) behaviors in mice, as measured by the cold-plantar, cold-plate (5 and 10 °C), or acetone tests. In contrast, nocifensive-like behavior to extreme cold-plate stimulation (−5 °C) was completely absent in mice lacking NaV1.8. Fluorescence-activated cell sorting (FACS) and subsequent microarray analysis of sensory neurons activated at 4 °C identified an enriched repertoire of ion channels, which include the Trp channel Trpm8 and potassium channel Kcnk9, that are potentially required for cold sensing above freezing temperatures in mouse DRG neurons. These data demonstrate the complexity of cold-sensing mechanisms in mouse sensory neurons, revealing a principal role for NaV1.8-negative neurons in sensing both innocuous and acute noxious cooling down to 1 °C, while NaV1.8-positive neurons are likely responsible for the transduction of prolonged extreme cold temperatures, where tissue damage causes pan-nociceptor activation.

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