The vanilloid receptor: a molecular gateway to the pain pathway.
@article{Caterina2001TheVR, title={The vanilloid receptor: a molecular gateway to the pain pathway.}, author={Michael J. Caterina and David Julius}, journal={Annual review of neuroscience}, year={2001}, volume={24}, pages={ 487-517 } }
The detection of painful stimuli occurs primarily at the peripheral terminals of specialized sensory neurons called nociceptors. These small-diameter neurons transduce signals of a chemical, mechanical, or thermal nature into action potentials and transmit this information to the central nervous system, ultimately eliciting a perception of pain or discomfort. Little is known about the proteins that detect noxious stimuli, especially those of a physical nature. Here we review recent advances in…
1,480 Citations
TRPV1 Receptors and Signal Transduction
- Biology
- 2007
Since its cloning in 1997, many amino acid regions within the TPRV1 protein have been shown to be involved in specific functions, such as capsaicin, proton, and heat activation; voltage dependence; permeability and ion selectivity; antagonist regions; desensitization; phosphorylation; modulation by lipids; and multimerization.
TRP channels and pain.
- BiologyAnnual review of cell and developmental biology
- 2013
Analysis of TRP channel function and expression has validated the existence of nociceptors as a specialized group of somatosensory neurons devoted to the detection of noxious stimuli and is providing insight into the coding logic of nnociception and how specification of nOCiceptor subtypes underlies behavioral discrimination ofNoxious thermal, chemical, and mechanical stimuli.
Heterogeneity in primary nociceptive neurons: From molecules to pathology
- BiologyArchives of pharmacal research
- 2010
An extraordinary diversity among nociceptors likely reflects the evolutionary adaptation required to respond to an extremely variety of circumstances.
Functional Interaction Between ATP and TRPV1 Receptors
- Biology
- 2007
In this chapter, regulation mechanisms of TRPV1 function by the inflammatory mediators are discussed by focusing on ATP action.
TRPV1: on the road to pain relief.
- BiologyCurrent molecular pharmacology
- 2008
A general picture of the physiological and pathophysiological roles of the TRPV1 channel and of its structural, pharmacological and biophysical properties is provided.
A new tr(i)p to sense pain: TRPA1 channel as a target for novel analgesics
- BiologyExpert review of neurotherapeutics
- 2008
The TRPA1 channel represents a new target for novel analgesics to specifically eliminate pain sensation of various stimuli.
The Role of the Vanilloid and Related Receptors in Nociceptor Function and Neuroimmune Regulation
- Biology
- 2009
Understanding the signaling and transmission of visceral nociceptive events.
- BiologyJournal of neurobiology
- 2004
Current evidence on the mechanisms of activation and sensitization of visceral nociceptive afferents and on their role in the triggering and maintenance of clinically relevant visceral pain states is reviewed.
Transient Receptor Potential Vanilloid 1 Involvement inAnimal Pain Perception
- Biology
- 2015
The aim of this review is to give to the readers a short overview of the TRPV1 involvement in pain perception and possible therapeutic applications, highlighting this topic in species of interest in veterinary medicine.
References
SHOWING 1-10 OF 163 REFERENCES
Impaired nociception and pain sensation in mice lacking the capsaicin receptor.
- BiologyScience
- 2000
Sensory neurons from mice lacking VR1 are severely deficient in their responses to each of these noxious stimuli and are impaired in the detection of painful heat, and showed little thermal hypersensitivity in the setting of inflammation.
Vanilloid receptor-1 is essential for inflammatory thermal hyperalgesia
- BiologyNature
- 2000
It is concluded that VR1 is required for inflammatory sensitization to noxious thermal stimuli but also that alternative mechanisms are sufficient for normal sensation of noxious heat.
A capsaicin-receptor homologue with a high threshold for noxious heat
- BiologyNature
- 1999
It is proposed that responses to noxious heat involve these related, but distinct, ion-channel subtypes that together detect a range of stimulus intensities.
A novel heat-activated current in nociceptive neurons and its sensitization by bradykinin.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1996
It is reported here that application of pulses of noxious heat to a subpopulation of isolated primary sensory neurons rapidly activates an inward current, and it is concluded that bradykinin sensitizes the response to heat by activating protein kinase C.
Acid potentiation of the capsaicin receptor determined by a key extracellular site.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 2000
It is demonstrated that protons, vanilloids, and heat promote channel opening through distinct pathways, because mutations at a second site selectively abrogate proton-evoked channel activation without diminishing responses to other noxious stimuli.
The capsaicin receptor: a heat-activated ion channel in the pain pathway
- BiologyNature
- 1997
The cloned capsaicin receptor is also activated by increases in temperature in the noxious range, suggesting that it functions as a transducer of painful thermal stimuli in vivo.
The sensory-efferent function of capsaicin-sensitive sensory neurons.
- BiologyGeneral pharmacology
- 1988