Abstract
Recently, scientists understood little of how peripheral neurons detect thermal and pain stimuli. In 1997, a scientist reported the discovery of the cellular receptor for capsaicin. The capsaicin receptor is a protein channel that sits in the outer membrane of specific nerve cells and allows a flood of calcium ions to enter the cells when capsaicin is present. It is also the first mammalian member of a similar proteins called transient receptor potential or TRP channels. Consequently, they have discovered five other thermosensitive TRP channels, each tuned to a specific range of temperatures. The founding member of the family became known as TRPV1 because it recognized a vanilloid molecule. It is the best-studied of the thermoTRPs. Unlike V1, V2 does not respond to capsaicin but it does to heat with threshold higher than that of V1 in cultured cells. Meanwhile, the warmth-sensing neurons fire at V3 and V4 thresholds because they contain warmth-sensitive V3 and V4 channels. In 2003, a new channel called cold and menthol receptor 1 also known as TRPM8 was discovered. The channel seems to adapt to prolonged cold stimuli, and its threshold shifts to a warmer range when menthol is present, suggesting that the stimuli act synergistically. Overall, the biophysical properties of each heat-sensing channel are unique, with different thresholds and chemical sensitivities. Mysteries of pain, linked in temperature and touch sensation are flickering into view, erasing the uncertainties in the field at a remarkable rate.
| Original language | English (US) |
|---|---|
| Pages | 326-333 |
| Number of pages | 8 |
| Volume | 95 |
| No | 4 |
| Specialist publication | American Scientist |
| DOIs | |
| State | Published - Jan 1 2007 |
| Externally published | Yes |
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ASJC Scopus subject areas
- General
Cite this
Feel the burn. / Story, Gina M.; Cruz-Orengo, Lillian.
In: American Scientist, Vol. 95, No. 4, 01.01.2007, p. 326-333.Research output: Contribution to specialist publication › Article
}
TY - GEN
T1 - Feel the burn
AU - Story, Gina M.
AU - Cruz-Orengo, Lillian
PY - 2007/1/1
Y1 - 2007/1/1
N2 - Recently, scientists understood little of how peripheral neurons detect thermal and pain stimuli. In 1997, a scientist reported the discovery of the cellular receptor for capsaicin. The capsaicin receptor is a protein channel that sits in the outer membrane of specific nerve cells and allows a flood of calcium ions to enter the cells when capsaicin is present. It is also the first mammalian member of a similar proteins called transient receptor potential or TRP channels. Consequently, they have discovered five other thermosensitive TRP channels, each tuned to a specific range of temperatures. The founding member of the family became known as TRPV1 because it recognized a vanilloid molecule. It is the best-studied of the thermoTRPs. Unlike V1, V2 does not respond to capsaicin but it does to heat with threshold higher than that of V1 in cultured cells. Meanwhile, the warmth-sensing neurons fire at V3 and V4 thresholds because they contain warmth-sensitive V3 and V4 channels. In 2003, a new channel called cold and menthol receptor 1 also known as TRPM8 was discovered. The channel seems to adapt to prolonged cold stimuli, and its threshold shifts to a warmer range when menthol is present, suggesting that the stimuli act synergistically. Overall, the biophysical properties of each heat-sensing channel are unique, with different thresholds and chemical sensitivities. Mysteries of pain, linked in temperature and touch sensation are flickering into view, erasing the uncertainties in the field at a remarkable rate.
AB - Recently, scientists understood little of how peripheral neurons detect thermal and pain stimuli. In 1997, a scientist reported the discovery of the cellular receptor for capsaicin. The capsaicin receptor is a protein channel that sits in the outer membrane of specific nerve cells and allows a flood of calcium ions to enter the cells when capsaicin is present. It is also the first mammalian member of a similar proteins called transient receptor potential or TRP channels. Consequently, they have discovered five other thermosensitive TRP channels, each tuned to a specific range of temperatures. The founding member of the family became known as TRPV1 because it recognized a vanilloid molecule. It is the best-studied of the thermoTRPs. Unlike V1, V2 does not respond to capsaicin but it does to heat with threshold higher than that of V1 in cultured cells. Meanwhile, the warmth-sensing neurons fire at V3 and V4 thresholds because they contain warmth-sensitive V3 and V4 channels. In 2003, a new channel called cold and menthol receptor 1 also known as TRPM8 was discovered. The channel seems to adapt to prolonged cold stimuli, and its threshold shifts to a warmer range when menthol is present, suggesting that the stimuli act synergistically. Overall, the biophysical properties of each heat-sensing channel are unique, with different thresholds and chemical sensitivities. Mysteries of pain, linked in temperature and touch sensation are flickering into view, erasing the uncertainties in the field at a remarkable rate.
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UR - http://www.scopus.com/inward/citedby.url?scp=34447303312&partnerID=8YFLogxK
U2 - 10.1511/2007.66.3753
DO - 10.1511/2007.66.3753
M3 - Article
AN - SCOPUS:34447303312
VL - 95
SP - 326
EP - 333
JO - American Scientist
JF - American Scientist
SN - 0003-0996
ER -