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TRP Channels

Maarten Gees, Grzegorz Owsianik, Bernd Nilius, Thomas Voets

10.1002/cphy.c110026

Source: Volume 2, Issue 1, January 2012

Published online: January 2012

Full Article on Wiley Online Library



Abstract

TRP channels constitute a large superfamily of cation channel forming proteins, all related to the gene product of the transient receptor potential (trp) locus in Drosophila. In mammals, 28 different TRP channel genes have been identified, which exhibit a large variety of functional properties and play diverse cellular and physiological roles. In this article, we provide a brief and systematic summary of expression, function, and (patho)physiological role of the mammalian TRP channels. © 2012 American Physiological Society. Compr Physiol 2:563‐608, 2012.

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Figure 1. Figure 1.

TRPA1. (A) Time course of whole‐cell TRPA1‐expressing CHO cell currents at +50 and −75 mV during cooling in the absence of both extracellular and intracellular solution free Ca2+ (left panel). Current‐voltage relations were obtained at the indicated time points (right panel) 180. (B) Time course of whole‐cell TRPA1‐expressing CHO cell currents at +50 and −75 mV, application of MO (10 mM) is indicated by bars (left panel) N‐Methyl‐D‐Glucamine (NMDG+) was used to control leak. Current‐voltage relations were obtained at the indicated time points (right panel) (reprinted from 102 with permission from Elsevier). (C) Cartoon representation of TRPA1 showing each cysteine residue as a circle (reprinted from 2520 by permission from Macmilan Publishers Ltd, copyright 2007). (D) A chemical model of reversible agonist action of TRPA1 by AITC (adapted from 1460 by permission from National Academy of Sciences, U.S.A., copyright 2006).
Figure 2. Figure 2.

TRPC1, TRPC4, and TRPC5. [(A)‐(E)] Current‐voltage relations in HEK293‐M1 cells transfected with either TRPC1, TRPC4, or TRPC5 cDNA alone or cotransfected with TRPC1 and TRPC4 or TRPC1 and TRPC5 cDNA. Currents were recorded before (con) and after application of 20 μM carbachol (carb). (F) The time course of currents via putative TRPC1/TRPC5 heteromultimers was measured at −70 mV. Application of carbachol (20 μM) and replacement of extracellular cations by NMDG

are indicated by the bars. Voltage ramps (1 mV/ms) from −100 to +60 mV were applied at 3.3 s intervals. Numbers corresponding to current‐voltage relations shown in E (reprinted from 391 with permission from Elsevier).
Figure 3. Figure 3.

TRPC2. [(A)‐(F)] Representative families of whole‐cell currents to a series of depolarizing and hyperpolarizing voltage steps recorded from an isolated WT (A, B, and C) or TRPC−/− vomeronasal sensory neurons (VSN) (D, E, and F). VSNs were exposed successively to extracellular control solution (A and D), control solution containing 50 μM of an impermeable, endogenous diacylglycerol (DAG) analogue 1‐stearoyl‐2‐arachidonoyl‐sn‐glycerol (SAG) (B and E), or 50 μM SAG in extracellular solution in which NMDG+ was the sole cation (C and D). Experiments were performed in the presence of 1 μM tetrodotoxin to block voltage‐gated Na+ channels; voltage‐activated K+ channels were blocked by using a Cs+‐based pipette solution. [(G), (H)] Plots of the steady‐state current‐voltage relationships of the SAG‐induced responses shown above with SAG‐induced currents in control solution (solid rectangles) or SAG‐induced currents in NMDG+‐based solution (open circles) for WT (G) and TRPC−/− (H). Currents obtained before SAG application (control) were digitally subtracted from the curves. Data points were fit by a polynomial function. The inset in H shows a magnification of the curve obtained with Na+. (I) Comparison of the dose dependence of averaged SAG‐induced currents (at −70 mV) from multiple WT (black bars) and TRPC−/− VSNs (gray bars). Data are the means ± SEM for the number of cells indicated above each bar (reprinted from 248 with permission from Elsevier).
Figure 4. Figure 4.

TRPC3 and TRPC6. [(A), (B)] Current‐voltage relations of whole cell recordings in HEK 293 cells transiently cotransfected with plasmids encoding eGFP, the H1 histamine receptor and human TRPC3 (A) or human TRPC6 (B) before (basal) and after application of receptor agonist (histamine). Insets: time course of currents at +60 and –60 mV in TRPC3‐ and TRPC6‐expressing cells before and after application of histamine. Duration of histamine applications is indicated by bars 89. (C) Time course of whole‐cell TRPC3‐expressing HEK cell currents at −80 mV, application of OAG (100 μM), and Ca2+ (2 mM) is indicated (left panel). Current‐voltage relations were obtained at the indicated time points (right panel) 240. (D) Time course of inside‐out TRPC6‐expressing CHO‐K1 currents, application of OAG (100 μM, left panel), and SAG (10 μM, right panel) are indicated. Insets show sample traces collected at different indicated positions (reprinted from 154 by permission from Macmilan Publishers Ltd, copyright 1999).
Figure 5. Figure 5.

TRPM2. (A) Time course of whole‐cell currents at −80 and +80 mV. Only tetracycline‐induced HEK‐293 cells expressing Flag‐LTRPC2 generated large inward and outward currents when perfused with 100 μM ADPR. I‐V relationships of ADPR‐induced currents at different times after break corresponding to panel A (reprinted from 332 by permission from Macmilan Publishers Ltd, copyright 2001).
Figure 6. Figure 6.

TRPM3. (A) Time course of whole‐cell currents at +150 and −150 mV in TRPM3‐expressing HEK cells activated by temperature or pregnenolone sulphate (PS, 50 μM). (B) Representative current‐voltage relations obtained from time points indicated in A (reprinted from 454 with permission from Elsevier).
Figure 7. Figure 7.

TRPM4 and TRPM5. (A) Time course of whole‐cell TRPM4 (left) or TRPM5 (right)‐expressing HEK currents at +80 and ‐120 mV in the presence of 100 or 1 μM [Ca2+]i (respectively, for TRPM4 or TRPM5). (B) current‐voltage (I‐V) relations elicited by a voltage ramp from −150 to +100 mV corresponding to the different time points indicated in panel A. Note the increase in the outward rectification ratio in B (b‐scaled, gray). (C) Current traces of TRPM4 and TRPM5 at 10 μM [Ca2+]i. Starting from a holding potential of 0 mV, the voltage protocol consisted of 400 ms presteps ranging from −100 to +140 mV (increment 20 mV) followed by a 200 ms test step to −100 mV (reprinted from 421 with permission from Elsevier).
Figure 8. Figure 8.

TRPM6 and TRPM7. (A) Simultaneous recording of intracellular Mg2+ (top) and the whole‐cell current at 80 and –80 mV (bottom) in TRPM6 expressing HEK cells before and after flash photolysis (arrow) of DM‐nitrophen 449. (B) Outward current during a 100‐ms step to 100 mV, which was recorded during the gap in the recording shown in panel A, showing the rapid current inhibition after the flash 449. (C) Current‐voltage relations obtained at the time points indicated in panel A 449. (D) Dose‐response curve showing the inhibition of the TRPM6‐induced currents by flash‐induced increases in intracellular Mg2+ to different levels 449. (E) Time course of whole‐cell TRPM7‐expressing HEK currents at −80 and +80 mV. Cells were perfused with internal solutions containing various ATP concentrations (0 mM, 1 mM, 6 mM Mg.ATP or 2mM Na.ATP) (reprinted from 287 by permission from Macmilan Publishers Ltd, copyright 2001).
Figure 9. Figure 9.

TRPM8. (A) Current‐voltage relations of whole‐cell TRPM8 currents activated by menthol (100 μM). Currents were measured during 200‐ms voltage ramps from −100 to +100 mV. (B) Current‐voltage relations of whole‐cell TRPM8 currents activated by cold (15 °C). Currents were measured during 200‐ms voltage ramps from −100 to +100 mV. (C) Steady‐state activation curves at different temperatures for the currents shown in D. (D) TRPM8 current traces at different temperatures in response to the indicated voltage protocol (adapted from 447).
Figure 10. Figure 10.

TRPML1. (A) Cartoons of three distinct patch‐clamp configurations of lysosomal recordings: lysosome‐attached, lysosome luminal‐side‐out, and whole‐lysosome. In each configuration, the pink arrow indicates the direction of the inward (at negative potentials; flow out of the lysosomes) current mediated by TRPML1 (reprinted from 93 by permission from Macmilan Publishers Ltd, copyright 2008). (B) Current‐voltage relations in lysosomes expressing TRPMLVa recorded using the luminal‐side‐out configuration and a voltage ramp from −140 to +140 mV in the presence of different Fe2+ concentrations (reprinted from 93 by permission from Macmilan Publishers Ltd, copyright 2008). (C) Current‐voltage relations in lysosomes expressing TRPML1 recorded using the whole‐endolysosome configuration and a voltage ramp from −140 to +140 mV in the presence of PI(3)P or PI(3,5)P2 (reprinted from 94 by permission from Macmilan Publishers Ltd, copyright 2010).
Figure 11. Figure 11.

TRPML3. (A) Currents elicited from wild type (black), A419P mutant (red), and I362/A419P mutant (green) in response to 5‐ms voltage steps from a holding potential of 50 mV between 200 and 100 mV in 20‐mV incremental steps. Black bars indicate zero current line. (B) Steady‐state current‐voltage plots from A normalized to cell capacitance (adapted from 130 by permission National Academy of Sciences, U.S.A., copyright 2007).
Figure 12. Figure 12.

TRPP2. (A) Comparison of whole‐cell currents in GFP‐ and TRPP2‐expressing HEK cells. Step pulses from −100 to +160 mV in 20 mV increments with a postpulse to −100 mV were applied. (B) Voltage dependence of open probabilities (Po) obtained by normalization of tail currents to the maximal amplitude of each individual cell obtained from Boltzmann fits. (C) Current‐voltage relationships for steady‐state currents (open) and instantaneous currents (closed) (adapted from 377).
Figure 13. Figure 13.

TRPV1. (A) Whole‐cell current traces of TRPV1 expressing HEK cells at different temperatures in response to voltage steps ranging from −120 to +160 mV 447. (B) Steady‐state activation curves at different temperatures for the currents shown in A 447. (C) Responses to capsaicin (10 mM) and extracts derived from four varieties of peppers in oocytes expressing TRPV1. Bottom right, relative potencies of each pepper extract are plotted. Reported pungencies for pepper varieties (in Scoville units) are: Habanero (H), 100,000‐300,000; Thai green (T), 50,000‐100,000; wax (W), 5,000‐10,000; and Poblano verde (P),1,000‐1,500. Capsaicin (C) is rated as 16 × 106 units (reprinted fron 54 by permission from Macmilan Publishers Ltd, copyright 1997).
Figure 14. Figure 14.

TRPV2. (A) Representative current responses of untransfected (water), TRPV1 (VR1), or TRPV2 (VRL‐1)‐transfected HEK cell in response to a temperature ramp (lower panel) (reprinted from 53 by permission from Macmilan Publishers Ltd, copyright 1999). (B) Representative current responses of untransfected (water), TRPV1 (VR1), or TRPV2 (VRL‐1)‐transfected HEK cell in response to capsaicin, acid, or temperature (reprinted from 53 by permission from Macmilan Publishers Ltd, copyright 1999). (C) I‐V relation in hTRPV2‐expressing HEK cells using a voltage ramp from −100 to +150 mV in control and after THC (30 μM) application.
Figure 15. Figure 15.

TRPV3. (A) Whole‐cell current traces of p‐Tracer (left) or TRPV3 (right) expressing CHO‐K1 cells in response to a temperature stimulus of 34°C using voltage steps ranging from −100 to +100 mV in 10 mV increments (reprinted from 491 by permission from Macmilan Publishers Ltd, copyright 2002). (B) Representative single‐channel currents (Vh = 60 mV) of TRPV3 expressing CHO‐K1 cells in response to a temperature ramp from 25.5 to 37 °C. Dashed lines indicate the closed state (reprinted from 491 by permission from Macmilan Publishers Ltd, copyright 2002). (C) Time course of whole‐cell mTRPV3 currents at −80 and +80 mV after repeated application of eugenol (2 mM) (reprinted from (489) by permission from Macmilan Publishers Ltd, copyright 2006).
Figure 16. Figure 16.

TRPV4. [(A)‐(C)] Time course of TRPV4 currents at −150 and +150 mV before and during application of (A) 4α‐PDD (1 μM), (B) hypotonic solution (240 mOsm) or AA (10 μM). (D) I‐V relationships of control and AA‐induced currents corresponding to panel C.
Figure 17. Figure 17.

TRPV5 and TRPV6. (A) Current‐voltage (I‐V) relation obtained in TRPV5 expressing CHO‐K1 cells during a 500‐ms linear voltage‐ramp from −100 to 100 mV (reprinted from 503 by permission from Macmilan Publishers Ltd, copyright 2002). (B) I‐V relation obtained in TRPV6 expressing HEK cells during a 200‐ms linear voltage‐ramp from −150 to 100 mV 448. (C) Whole‐cell current traces in TRPV5 expressing CHO‐K1 cells using voltage steps ranging from −120 to +80 mV in 20 mV increments from a holding potential of 0 mV (reprinted from 503 by permission from Macmilan Publishers Ltd, copyright 2002). (D) Whole‐cell current traces in TRPV6 expressing HEK cells using voltage steps ranging from −180 to +100 mV in 20 mV increments from a holding potential of 0 mV 448.


Figure 1.

TRPA1. (A) Time course of whole‐cell TRPA1‐expressing CHO cell currents at +50 and −75 mV during cooling in the absence of both extracellular and intracellular solution free Ca2+ (left panel). Current‐voltage relations were obtained at the indicated time points (right panel) 180. (B) Time course of whole‐cell TRPA1‐expressing CHO cell currents at +50 and −75 mV, application of MO (10 mM) is indicated by bars (left panel) N‐Methyl‐D‐Glucamine (NMDG+) was used to control leak. Current‐voltage relations were obtained at the indicated time points (right panel) (reprinted from 102 with permission from Elsevier). (C) Cartoon representation of TRPA1 showing each cysteine residue as a circle (reprinted from 2520 by permission from Macmilan Publishers Ltd, copyright 2007). (D) A chemical model of reversible agonist action of TRPA1 by AITC (adapted from 1460 by permission from National Academy of Sciences, U.S.A., copyright 2006).



Figure 2.

TRPC1, TRPC4, and TRPC5. [(A)‐(E)] Current‐voltage relations in HEK293‐M1 cells transfected with either TRPC1, TRPC4, or TRPC5 cDNA alone or cotransfected with TRPC1 and TRPC4 or TRPC1 and TRPC5 cDNA. Currents were recorded before (con) and after application of 20 μM carbachol (carb). (F) The time course of currents via putative TRPC1/TRPC5 heteromultimers was measured at −70 mV. Application of carbachol (20 μM) and replacement of extracellular cations by NMDG

are indicated by the bars. Voltage ramps (1 mV/ms) from −100 to +60 mV were applied at 3.3 s intervals. Numbers corresponding to current‐voltage relations shown in E (reprinted from 391 with permission from Elsevier).



Figure 3.

TRPC2. [(A)‐(F)] Representative families of whole‐cell currents to a series of depolarizing and hyperpolarizing voltage steps recorded from an isolated WT (A, B, and C) or TRPC−/− vomeronasal sensory neurons (VSN) (D, E, and F). VSNs were exposed successively to extracellular control solution (A and D), control solution containing 50 μM of an impermeable, endogenous diacylglycerol (DAG) analogue 1‐stearoyl‐2‐arachidonoyl‐sn‐glycerol (SAG) (B and E), or 50 μM SAG in extracellular solution in which NMDG+ was the sole cation (C and D). Experiments were performed in the presence of 1 μM tetrodotoxin to block voltage‐gated Na+ channels; voltage‐activated K+ channels were blocked by using a Cs+‐based pipette solution. [(G), (H)] Plots of the steady‐state current‐voltage relationships of the SAG‐induced responses shown above with SAG‐induced currents in control solution (solid rectangles) or SAG‐induced currents in NMDG+‐based solution (open circles) for WT (G) and TRPC−/− (H). Currents obtained before SAG application (control) were digitally subtracted from the curves. Data points were fit by a polynomial function. The inset in H shows a magnification of the curve obtained with Na+. (I) Comparison of the dose dependence of averaged SAG‐induced currents (at −70 mV) from multiple WT (black bars) and TRPC−/− VSNs (gray bars). Data are the means ± SEM for the number of cells indicated above each bar (reprinted from 248 with permission from Elsevier).



Figure 4.

TRPC3 and TRPC6. [(A), (B)] Current‐voltage relations of whole cell recordings in HEK 293 cells transiently cotransfected with plasmids encoding eGFP, the H1 histamine receptor and human TRPC3 (A) or human TRPC6 (B) before (basal) and after application of receptor agonist (histamine). Insets: time course of currents at +60 and –60 mV in TRPC3‐ and TRPC6‐expressing cells before and after application of histamine. Duration of histamine applications is indicated by bars 89. (C) Time course of whole‐cell TRPC3‐expressing HEK cell currents at −80 mV, application of OAG (100 μM), and Ca2+ (2 mM) is indicated (left panel). Current‐voltage relations were obtained at the indicated time points (right panel) 240. (D) Time course of inside‐out TRPC6‐expressing CHO‐K1 currents, application of OAG (100 μM, left panel), and SAG (10 μM, right panel) are indicated. Insets show sample traces collected at different indicated positions (reprinted from 154 by permission from Macmilan Publishers Ltd, copyright 1999).



Figure 5.

TRPM2. (A) Time course of whole‐cell currents at −80 and +80 mV. Only tetracycline‐induced HEK‐293 cells expressing Flag‐LTRPC2 generated large inward and outward currents when perfused with 100 μM ADPR. I‐V relationships of ADPR‐induced currents at different times after break corresponding to panel A (reprinted from 332 by permission from Macmilan Publishers Ltd, copyright 2001).



Figure 6.

TRPM3. (A) Time course of whole‐cell currents at +150 and −150 mV in TRPM3‐expressing HEK cells activated by temperature or pregnenolone sulphate (PS, 50 μM). (B) Representative current‐voltage relations obtained from time points indicated in A (reprinted from 454 with permission from Elsevier).



Figure 7.

TRPM4 and TRPM5. (A) Time course of whole‐cell TRPM4 (left) or TRPM5 (right)‐expressing HEK currents at +80 and ‐120 mV in the presence of 100 or 1 μM [Ca2+]i (respectively, for TRPM4 or TRPM5). (B) current‐voltage (I‐V) relations elicited by a voltage ramp from −150 to +100 mV corresponding to the different time points indicated in panel A. Note the increase in the outward rectification ratio in B (b‐scaled, gray). (C) Current traces of TRPM4 and TRPM5 at 10 μM [Ca2+]i. Starting from a holding potential of 0 mV, the voltage protocol consisted of 400 ms presteps ranging from −100 to +140 mV (increment 20 mV) followed by a 200 ms test step to −100 mV (reprinted from 421 with permission from Elsevier).



Figure 8.

TRPM6 and TRPM7. (A) Simultaneous recording of intracellular Mg2+ (top) and the whole‐cell current at 80 and –80 mV (bottom) in TRPM6 expressing HEK cells before and after flash photolysis (arrow) of DM‐nitrophen 449. (B) Outward current during a 100‐ms step to 100 mV, which was recorded during the gap in the recording shown in panel A, showing the rapid current inhibition after the flash 449. (C) Current‐voltage relations obtained at the time points indicated in panel A 449. (D) Dose‐response curve showing the inhibition of the TRPM6‐induced currents by flash‐induced increases in intracellular Mg2+ to different levels 449. (E) Time course of whole‐cell TRPM7‐expressing HEK currents at −80 and +80 mV. Cells were perfused with internal solutions containing various ATP concentrations (0 mM, 1 mM, 6 mM Mg.ATP or 2mM Na.ATP) (reprinted from 287 by permission from Macmilan Publishers Ltd, copyright 2001).



Figure 9.

TRPM8. (A) Current‐voltage relations of whole‐cell TRPM8 currents activated by menthol (100 μM). Currents were measured during 200‐ms voltage ramps from −100 to +100 mV. (B) Current‐voltage relations of whole‐cell TRPM8 currents activated by cold (15 °C). Currents were measured during 200‐ms voltage ramps from −100 to +100 mV. (C) Steady‐state activation curves at different temperatures for the currents shown in D. (D) TRPM8 current traces at different temperatures in response to the indicated voltage protocol (adapted from 447).



Figure 10.

TRPML1. (A) Cartoons of three distinct patch‐clamp configurations of lysosomal recordings: lysosome‐attached, lysosome luminal‐side‐out, and whole‐lysosome. In each configuration, the pink arrow indicates the direction of the inward (at negative potentials; flow out of the lysosomes) current mediated by TRPML1 (reprinted from 93 by permission from Macmilan Publishers Ltd, copyright 2008). (B) Current‐voltage relations in lysosomes expressing TRPMLVa recorded using the luminal‐side‐out configuration and a voltage ramp from −140 to +140 mV in the presence of different Fe2+ concentrations (reprinted from 93 by permission from Macmilan Publishers Ltd, copyright 2008). (C) Current‐voltage relations in lysosomes expressing TRPML1 recorded using the whole‐endolysosome configuration and a voltage ramp from −140 to +140 mV in the presence of PI(3)P or PI(3,5)P2 (reprinted from 94 by permission from Macmilan Publishers Ltd, copyright 2010).



Figure 11.

TRPML3. (A) Currents elicited from wild type (black), A419P mutant (red), and I362/A419P mutant (green) in response to 5‐ms voltage steps from a holding potential of 50 mV between 200 and 100 mV in 20‐mV incremental steps. Black bars indicate zero current line. (B) Steady‐state current‐voltage plots from A normalized to cell capacitance (adapted from 130 by permission National Academy of Sciences, U.S.A., copyright 2007).



Figure 12.

TRPP2. (A) Comparison of whole‐cell currents in GFP‐ and TRPP2‐expressing HEK cells. Step pulses from −100 to +160 mV in 20 mV increments with a postpulse to −100 mV were applied. (B) Voltage dependence of open probabilities (Po) obtained by normalization of tail currents to the maximal amplitude of each individual cell obtained from Boltzmann fits. (C) Current‐voltage relationships for steady‐state currents (open) and instantaneous currents (closed) (adapted from 377).



Figure 13.

TRPV1. (A) Whole‐cell current traces of TRPV1 expressing HEK cells at different temperatures in response to voltage steps ranging from −120 to +160 mV 447. (B) Steady‐state activation curves at different temperatures for the currents shown in A 447. (C) Responses to capsaicin (10 mM) and extracts derived from four varieties of peppers in oocytes expressing TRPV1. Bottom right, relative potencies of each pepper extract are plotted. Reported pungencies for pepper varieties (in Scoville units) are: Habanero (H), 100,000‐300,000; Thai green (T), 50,000‐100,000; wax (W), 5,000‐10,000; and Poblano verde (P),1,000‐1,500. Capsaicin (C) is rated as 16 × 106 units (reprinted fron 54 by permission from Macmilan Publishers Ltd, copyright 1997).



Figure 14.

TRPV2. (A) Representative current responses of untransfected (water), TRPV1 (VR1), or TRPV2 (VRL‐1)‐transfected HEK cell in response to a temperature ramp (lower panel) (reprinted from 53 by permission from Macmilan Publishers Ltd, copyright 1999). (B) Representative current responses of untransfected (water), TRPV1 (VR1), or TRPV2 (VRL‐1)‐transfected HEK cell in response to capsaicin, acid, or temperature (reprinted from 53 by permission from Macmilan Publishers Ltd, copyright 1999). (C) I‐V relation in hTRPV2‐expressing HEK cells using a voltage ramp from −100 to +150 mV in control and after THC (30 μM) application.



Figure 15.

TRPV3. (A) Whole‐cell current traces of p‐Tracer (left) or TRPV3 (right) expressing CHO‐K1 cells in response to a temperature stimulus of 34°C using voltage steps ranging from −100 to +100 mV in 10 mV increments (reprinted from 491 by permission from Macmilan Publishers Ltd, copyright 2002). (B) Representative single‐channel currents (Vh = 60 mV) of TRPV3 expressing CHO‐K1 cells in response to a temperature ramp from 25.5 to 37 °C. Dashed lines indicate the closed state (reprinted from 491 by permission from Macmilan Publishers Ltd, copyright 2002). (C) Time course of whole‐cell mTRPV3 currents at −80 and +80 mV after repeated application of eugenol (2 mM) (reprinted from (489) by permission from Macmilan Publishers Ltd, copyright 2006).



Figure 16.

TRPV4. [(A)‐(C)] Time course of TRPV4 currents at −150 and +150 mV before and during application of (A) 4α‐PDD (1 μM), (B) hypotonic solution (240 mOsm) or AA (10 μM). (D) I‐V relationships of control and AA‐induced currents corresponding to panel C.



Figure 17.

TRPV5 and TRPV6. (A) Current‐voltage (I‐V) relation obtained in TRPV5 expressing CHO‐K1 cells during a 500‐ms linear voltage‐ramp from −100 to 100 mV (reprinted from 503 by permission from Macmilan Publishers Ltd, copyright 2002). (B) I‐V relation obtained in TRPV6 expressing HEK cells during a 200‐ms linear voltage‐ramp from −150 to 100 mV 448. (C) Whole‐cell current traces in TRPV5 expressing CHO‐K1 cells using voltage steps ranging from −120 to +80 mV in 20 mV increments from a holding potential of 0 mV (reprinted from 503 by permission from Macmilan Publishers Ltd, copyright 2002). (D) Whole‐cell current traces in TRPV6 expressing HEK cells using voltage steps ranging from −180 to +100 mV in 20 mV increments from a holding potential of 0 mV 448.

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Further Reading
 1. Basbaum AI, Bautista DM, Scherrer G, Julius D. Cellular and molecular mechanisms of pain. Cell 139: 267‐284, 2009.
 2. Clapham DE. TRP channels as cellular sensors. Nature 426: 517‐524, 2003.
 3. Montell C. The history of TRP channels, a commentary and reflection. Pflugers Arch, 2011.
 4. Montell C, Birnbaumer L, Flockerzi V, Bindels RJ, Bruford EA, Caterina MJ, Clapham DE, Harteneck C, Heller S, Julius D, Kojima I, Mori Y, Penner R, Prawitt D, Scharenberg AM, Schultz G, Shimizu N, Zhu MX. A unified nomenclature for the superfamily of TRP cation channels. Mol Cell 9: 229‐231, 2002.
 5. Nilius B, Owsianik G, Voets T, Peters JA. Transient receptor potential cation channels in disease. Physiol Rev 87: 165‐217, 2007.
 6. Owsianik G, Talavera K, Voets T, Nilius B. Permeation and selectivity of TRP channels. Annu Rev Physiol 68: 685‐717, 2006.

Further Reading:

Montell C. The history of TRP channels, a commentary and reflection. Pflugers Arch, 2011.

Montell C, Birnbaumer L, Flockerzi V, Bindels RJ, Bruford EA, Caterina MJ, Clapham DE, Harteneck C, Heller S, Julius D, Kojima I, Mori Y, Penner R, Prawitt D, Scharenberg AM, Schultz G, Shimizu N, and Zhu MX. A unified nomenclature for the superfamily of TRP cation channels. Mol Cell 9: 229-231, 2002.

Clapham DE. TRP channels as cellular sensors. Nature 426: 517-524, 2003.

Owsianik G, Talavera K, Voets T, and Nilius B. Permeation and selectivity of TRP channels. Annu Rev Physiol 68: 685-717, 2006.

Basbaum AI, Bautista DM, Scherrer G, and Julius D. Cellular and molecular mechanisms of pain. Cell 139: 267-284, 2009.

Nilius B, Owsianik G, Voets T, and Peters JA. Transient receptor potential cation channels in disease. Physiol Rev 87: 165-217, 2007.

 


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Maarten Gees, Grzegorz Owsianik, Bernd Nilius, Thomas Voets. TRP Channels. Compr Physiol 2012, 2: 563-608. doi: 10.1002/cphy.c110026