rtx  (Alomone Labs)


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    Alomone Labs rtx
    Rtx, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rtx  (Alomone Labs)


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    Structured Review

    Alomone Labs rtx
    Rtx, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 1 article reviews
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    rtx  (Alomone Labs)


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    Structured Review

    Alomone Labs rtx
    Rtx, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rtx/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
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    rtx  (Alomone Labs)


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    Alomone Labs rtx
    a A representative macroscopic current time-course (top panel) recorded from a HEK-293T cell expressing <t>rat</t> <t>TRPV1</t> in response to the temperature ramp (10–50 °C) at a membrane potential of −60 mV and then followed by a saturating concentration of <t>RTx</t> (50 nM) and 20 µM ruthenium red (RR). The dashed line indicates zero current. The recorded temperature is shown in the middle panel. The Arrhenius plot for the temperature activation was shown in the bottom panel. Fitted Q 10 values for high (blue line) and low (red line) temperature ranges are shown. A representative time-course recording for RTx-bound TRPV1 temperature sensitivity. First the channel was challenged by 10 nM RTx for ~20 s followed by a temperature ramp (10–48 °C), then a saturating concentration of RTx (50 nM) was introduced, and finally RR (20 µM) was applied to completely block the channel. The dashed line indicates zero current. The recorded temperature is shown in the middle panel and the Arrhenius plot for the temperature activation is shown in the bottom panel. Fitted Q 10 values for high and low temperature (T) ranges are shown. c Q 10 values as a function of I/I 50nM RTx for low and high temperature ranges. Each experiment was conducted as shown in a and . The low T range Q 10 value is steady at 1.7, while the high T range Q 10 rapidly collapses from ~38 to ~3. Each pair of high and low temperature sensitivity data points represents independent time-course recordings from individual cells ( n = 17 cells). Source data are provided as a Source Data file. d Representative micrographs of TRPV1 recorded in the presence of 50 μM RTx at 4 °C, 25 °C and 48 °C, respectively. Cryo-EM maps of RTx-TRPV1 determined at 4 °C (class I, class II, and class III), 25 °C (class A and class B), and 48 °C (class α). Note the differences between central pore sizes amongst different classes at 4 °C. The classes not found in each dataset are shown as transparent. The pie charts depict particle distributions among classes for each dataset along with representative micrographs. Each pie chart represents an average value for four independent data processes (Supplementary Fig. , ).
    Rtx, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rtx/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rtx - by Bioz Stars, 2023-02
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    1) Product Images from "Vanilloid-dependent TRPV1 opening trajectory from cryoEM ensemble analysis"

    Article Title: Vanilloid-dependent TRPV1 opening trajectory from cryoEM ensemble analysis

    Journal: Nature Communications

    doi: 10.1038/s41467-022-30602-2

    a A representative macroscopic current time-course (top panel) recorded from a HEK-293T cell expressing rat TRPV1 in response to the temperature ramp (10–50 °C) at a membrane potential of −60 mV and then followed by a saturating concentration of RTx (50 nM) and 20 µM ruthenium red (RR). The dashed line indicates zero current. The recorded temperature is shown in the middle panel. The Arrhenius plot for the temperature activation was shown in the bottom panel. Fitted Q 10 values for high (blue line) and low (red line) temperature ranges are shown. A representative time-course recording for RTx-bound TRPV1 temperature sensitivity. First the channel was challenged by 10 nM RTx for ~20 s followed by a temperature ramp (10–48 °C), then a saturating concentration of RTx (50 nM) was introduced, and finally RR (20 µM) was applied to completely block the channel. The dashed line indicates zero current. The recorded temperature is shown in the middle panel and the Arrhenius plot for the temperature activation is shown in the bottom panel. Fitted Q 10 values for high and low temperature (T) ranges are shown. c Q 10 values as a function of I/I 50nM RTx for low and high temperature ranges. Each experiment was conducted as shown in a and . The low T range Q 10 value is steady at 1.7, while the high T range Q 10 rapidly collapses from ~38 to ~3. Each pair of high and low temperature sensitivity data points represents independent time-course recordings from individual cells ( n = 17 cells). Source data are provided as a Source Data file. d Representative micrographs of TRPV1 recorded in the presence of 50 μM RTx at 4 °C, 25 °C and 48 °C, respectively. Cryo-EM maps of RTx-TRPV1 determined at 4 °C (class I, class II, and class III), 25 °C (class A and class B), and 48 °C (class α). Note the differences between central pore sizes amongst different classes at 4 °C. The classes not found in each dataset are shown as transparent. The pie charts depict particle distributions among classes for each dataset along with representative micrographs. Each pie chart represents an average value for four independent data processes (Supplementary Fig. , ).
    Figure Legend Snippet: a A representative macroscopic current time-course (top panel) recorded from a HEK-293T cell expressing rat TRPV1 in response to the temperature ramp (10–50 °C) at a membrane potential of −60 mV and then followed by a saturating concentration of RTx (50 nM) and 20 µM ruthenium red (RR). The dashed line indicates zero current. The recorded temperature is shown in the middle panel. The Arrhenius plot for the temperature activation was shown in the bottom panel. Fitted Q 10 values for high (blue line) and low (red line) temperature ranges are shown. A representative time-course recording for RTx-bound TRPV1 temperature sensitivity. First the channel was challenged by 10 nM RTx for ~20 s followed by a temperature ramp (10–48 °C), then a saturating concentration of RTx (50 nM) was introduced, and finally RR (20 µM) was applied to completely block the channel. The dashed line indicates zero current. The recorded temperature is shown in the middle panel and the Arrhenius plot for the temperature activation is shown in the bottom panel. Fitted Q 10 values for high and low temperature (T) ranges are shown. c Q 10 values as a function of I/I 50nM RTx for low and high temperature ranges. Each experiment was conducted as shown in a and . The low T range Q 10 value is steady at 1.7, while the high T range Q 10 rapidly collapses from ~38 to ~3. Each pair of high and low temperature sensitivity data points represents independent time-course recordings from individual cells ( n = 17 cells). Source data are provided as a Source Data file. d Representative micrographs of TRPV1 recorded in the presence of 50 μM RTx at 4 °C, 25 °C and 48 °C, respectively. Cryo-EM maps of RTx-TRPV1 determined at 4 °C (class I, class II, and class III), 25 °C (class A and class B), and 48 °C (class α). Note the differences between central pore sizes amongst different classes at 4 °C. The classes not found in each dataset are shown as transparent. The pie charts depict particle distributions among classes for each dataset along with representative micrographs. Each pie chart represents an average value for four independent data processes (Supplementary Fig. , ).

    Techniques Used: Expressing, Concentration Assay, Activation Assay, Blocking Assay, Cryo-EM Sample Prep

    a Comparison of the pore domain structures, only two subunits are shown for clarity, with the S6 gate (S6b), selectivity filter (SF), pore loop (PL) and pore helix (PH) as indicated. The pore profiles are shown as surfaces (gray). The red arrows indicate direction of movement. b Comparison of TRPV1 C,RTx (gray) and TRPV1 IC,RTx (green) structures (left) and close-up view of TRPV1 C,RTx and TRPV1 IC,RTx pore region (right). c The cryo-EM densities and the models for M644 in TRPV1 IC,RTx (green) and TRPV1 IO,RTx (gold). The cryo-EM map thresholdings are 0.03, and 0.04, respectively. d Comparison of TRPV1 IO, RTx (gold) and TRPV1 O, RTx (pink) outer pore region. Representative residues showing large motions are shown as sticks. TJ, turret junction. Phospholipids are shown as sticks and cryo-EM densities, with thresholding at 0.035 and 0.029, respectively.
    Figure Legend Snippet: a Comparison of the pore domain structures, only two subunits are shown for clarity, with the S6 gate (S6b), selectivity filter (SF), pore loop (PL) and pore helix (PH) as indicated. The pore profiles are shown as surfaces (gray). The red arrows indicate direction of movement. b Comparison of TRPV1 C,RTx (gray) and TRPV1 IC,RTx (green) structures (left) and close-up view of TRPV1 C,RTx and TRPV1 IC,RTx pore region (right). c The cryo-EM densities and the models for M644 in TRPV1 IC,RTx (green) and TRPV1 IO,RTx (gold). The cryo-EM map thresholdings are 0.03, and 0.04, respectively. d Comparison of TRPV1 IO, RTx (gold) and TRPV1 O, RTx (pink) outer pore region. Representative residues showing large motions are shown as sticks. TJ, turret junction. Phospholipids are shown as sticks and cryo-EM densities, with thresholding at 0.035 and 0.029, respectively.

    Techniques Used: Cryo-EM Sample Prep

    The cryo-EM densities (grey surface) and respective models (cartoon) depicting bottom-up views of the S6 gate (top), top-down views of the selectivity filter (middle), top-down views of the monomeric outer pore (bottom), and local estimated resolutions for TRPV1 C, RTx a , blue, thresholding 0.12); TRPV1 IC, RTx b , cyan, thresholding 0.035); TRPV1 IO, RTx c , orange, thresholding 0.09); TRPV1 O, RTx,4 °C d , green, thresholding 0.1); TRPV1 O, RTx,25 °C e , brown, thresholding 0.08); and TRPV1 O, RTx,48 °C f , red, thresholding 0.033).
    Figure Legend Snippet: The cryo-EM densities (grey surface) and respective models (cartoon) depicting bottom-up views of the S6 gate (top), top-down views of the selectivity filter (middle), top-down views of the monomeric outer pore (bottom), and local estimated resolutions for TRPV1 C, RTx a , blue, thresholding 0.12); TRPV1 IC, RTx b , cyan, thresholding 0.035); TRPV1 IO, RTx c , orange, thresholding 0.09); TRPV1 O, RTx,4 °C d , green, thresholding 0.1); TRPV1 O, RTx,25 °C e , brown, thresholding 0.08); and TRPV1 O, RTx,48 °C f , red, thresholding 0.033).

    Techniques Used: Cryo-EM Sample Prep

    a Cylinder representation of TRPV1 in turquoise (one subunit) and gray (the rest of the channel). The approximate distances from the RTx binding site (reference residue Y511) to subdomains are shown. b The cryo-EM densities (surface) and respective models (sticks) depicting close-up views of the vanilloid binding sites in TRPV1 C, RTx (skyblue), thresholding 0.19, TRPV1 IO, RTx (yellow), thresholding 0.04, and TRPV1 O, RTx (pink), thresholding 0.033. c The cryo-EM densities (surface) and respective models (sticks) depicting close-up views of the selectivity filter in TRPV1 C,RTx (skyblue), thresholding 0.19, TRPV1 IC,RTx (green), thresholding 0.04, TRPV1 IO,RTx (yellow), thresholding 0.1, and TRPV1 O,RTx (pink), thresholding 0.033. d – e Close-up view of the overlays of TRPV1 C, RTx (skyblue), TRPV1 IO, RTx (yellow), and TRPV1 O, RTx (pink) regarding the cytoplasmic domain, and S6 gate e , respectively.
    Figure Legend Snippet: a Cylinder representation of TRPV1 in turquoise (one subunit) and gray (the rest of the channel). The approximate distances from the RTx binding site (reference residue Y511) to subdomains are shown. b The cryo-EM densities (surface) and respective models (sticks) depicting close-up views of the vanilloid binding sites in TRPV1 C, RTx (skyblue), thresholding 0.19, TRPV1 IO, RTx (yellow), thresholding 0.04, and TRPV1 O, RTx (pink), thresholding 0.033. c The cryo-EM densities (surface) and respective models (sticks) depicting close-up views of the selectivity filter in TRPV1 C,RTx (skyblue), thresholding 0.19, TRPV1 IC,RTx (green), thresholding 0.04, TRPV1 IO,RTx (yellow), thresholding 0.1, and TRPV1 O,RTx (pink), thresholding 0.033. d – e Close-up view of the overlays of TRPV1 C, RTx (skyblue), TRPV1 IO, RTx (yellow), and TRPV1 O, RTx (pink) regarding the cytoplasmic domain, and S6 gate e , respectively.

    Techniques Used: Binding Assay, Cryo-EM Sample Prep

    a The cryo-EM maps (surface) and respective models (sticks) depicting the tripartite hydrogen bond network of PH-S5-S6 in TRPV1 C, RTx (skyblue), thresholding 0.15, TRPV1 IC, RTx (yellow), thresholding 0.045, TRPV1 IO, RTx (gold), thresholding 0.1, and TRPV1 O, RTx (pink), thresholding 0.04. The black dotted-lines indicate hydrogen bonds. The red dotted-lines indicate distance measurements between atoms where hydrogen bonds are broken. b – e TRPV1 Y584F and T641A reduce large cation permeabilty (YO-PRO-1, M.W. 376 Da) in the presence of RTx. Representative inside-out current traces of TRPV1 WT b , TRPV1 Y584F c , and TRPV1 T641A d . Current traces for basal, RTx (200 nM) activation (red trace) and intracellular application of 10 μM YO-PRO-1 (blue trace). e Summary of current inhibition by YO-PRO-1 (10 µM) of TRPV1 WT, TRPV1 Y584F and TRPV1 T641A after application of a saturating concentration of RTx (200 nM). Data are presented as mean ± s.e.m.; P < 0.0001 for T641A and Y584F, two-tailed unpaired Student’s t test. (For WT, n = 5, for Y584F and T641A, n = 4). Source data are provided as a Source Data file.
    Figure Legend Snippet: a The cryo-EM maps (surface) and respective models (sticks) depicting the tripartite hydrogen bond network of PH-S5-S6 in TRPV1 C, RTx (skyblue), thresholding 0.15, TRPV1 IC, RTx (yellow), thresholding 0.045, TRPV1 IO, RTx (gold), thresholding 0.1, and TRPV1 O, RTx (pink), thresholding 0.04. The black dotted-lines indicate hydrogen bonds. The red dotted-lines indicate distance measurements between atoms where hydrogen bonds are broken. b – e TRPV1 Y584F and T641A reduce large cation permeabilty (YO-PRO-1, M.W. 376 Da) in the presence of RTx. Representative inside-out current traces of TRPV1 WT b , TRPV1 Y584F c , and TRPV1 T641A d . Current traces for basal, RTx (200 nM) activation (red trace) and intracellular application of 10 μM YO-PRO-1 (blue trace). e Summary of current inhibition by YO-PRO-1 (10 µM) of TRPV1 WT, TRPV1 Y584F and TRPV1 T641A after application of a saturating concentration of RTx (200 nM). Data are presented as mean ± s.e.m.; P < 0.0001 for T641A and Y584F, two-tailed unpaired Student’s t test. (For WT, n = 5, for Y584F and T641A, n = 4). Source data are provided as a Source Data file.

    Techniques Used: Cryo-EM Sample Prep, Activation Assay, Inhibition, Concentration Assay, Two Tailed Test

    rtx  (Alomone Labs)


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    Structured Review

    Alomone Labs rtx
    a A representative macroscopic current time-course (top panel) recorded from a HEK-293T cell expressing <t>rat</t> <t>TRPV1</t> in response to the temperature ramp (10–50 °C) at a membrane potential of −60 mV and then followed by a saturating concentration of <t>RTx</t> (50 nM) and 20 µM ruthenium red (RR). The dashed line indicates zero current. The recorded temperature is shown in the middle panel. The Arrhenius plot for the temperature activation was shown in the bottom panel. Fitted Q 10 values for high (blue line) and low (red line) temperature ranges are shown. A representative time-course recording for RTx-bound TRPV1 temperature sensitivity. First the channel was challenged by 10 nM RTx for ~20 s followed by a temperature ramp (10–48 °C), then a saturating concentration of RTx (50 nM) was introduced, and finally RR (20 µM) was applied to completely block the channel. The dashed line indicates zero current. The recorded temperature is shown in the middle panel and the Arrhenius plot for the temperature activation is shown in the bottom panel. Fitted Q 10 values for high and low temperature (T) ranges are shown. c Q 10 values as a function of I/I 50nM RTx for low and high temperature ranges. Each experiment was conducted as shown in a and . The low T range Q 10 value is steady at 1.7, while the high T range Q 10 rapidly collapses from ~38 to ~3. Each pair of high and low temperature sensitivity data points represents independent time-course recordings from individual cells ( n = 17 cells). Source data are provided as a Source Data file. d Representative micrographs of TRPV1 recorded in the presence of 50 μM RTx at 4 °C, 25 °C and 48 °C, respectively. Cryo-EM maps of RTx-TRPV1 determined at 4 °C (class I, class II, and class III), 25 °C (class A and class B), and 48 °C (class α). Note the differences between central pore sizes amongst different classes at 4 °C. The classes not found in each dataset are shown as transparent. The pie charts depict particle distributions among classes for each dataset along with representative micrographs. Each pie chart represents an average value for four independent data processes (Supplementary Fig. , ).
    Rtx, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rtx/product/Alomone Labs
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rtx - by Bioz Stars, 2023-02
    86/100 stars

    Images

    1) Product Images from "Vanilloid-dependent TRPV1 opening trajectory from cryoEM ensemble analysis"

    Article Title: Vanilloid-dependent TRPV1 opening trajectory from cryoEM ensemble analysis

    Journal: Nature Communications

    doi: 10.1038/s41467-022-30602-2

    a A representative macroscopic current time-course (top panel) recorded from a HEK-293T cell expressing rat TRPV1 in response to the temperature ramp (10–50 °C) at a membrane potential of −60 mV and then followed by a saturating concentration of RTx (50 nM) and 20 µM ruthenium red (RR). The dashed line indicates zero current. The recorded temperature is shown in the middle panel. The Arrhenius plot for the temperature activation was shown in the bottom panel. Fitted Q 10 values for high (blue line) and low (red line) temperature ranges are shown. A representative time-course recording for RTx-bound TRPV1 temperature sensitivity. First the channel was challenged by 10 nM RTx for ~20 s followed by a temperature ramp (10–48 °C), then a saturating concentration of RTx (50 nM) was introduced, and finally RR (20 µM) was applied to completely block the channel. The dashed line indicates zero current. The recorded temperature is shown in the middle panel and the Arrhenius plot for the temperature activation is shown in the bottom panel. Fitted Q 10 values for high and low temperature (T) ranges are shown. c Q 10 values as a function of I/I 50nM RTx for low and high temperature ranges. Each experiment was conducted as shown in a and . The low T range Q 10 value is steady at 1.7, while the high T range Q 10 rapidly collapses from ~38 to ~3. Each pair of high and low temperature sensitivity data points represents independent time-course recordings from individual cells ( n = 17 cells). Source data are provided as a Source Data file. d Representative micrographs of TRPV1 recorded in the presence of 50 μM RTx at 4 °C, 25 °C and 48 °C, respectively. Cryo-EM maps of RTx-TRPV1 determined at 4 °C (class I, class II, and class III), 25 °C (class A and class B), and 48 °C (class α). Note the differences between central pore sizes amongst different classes at 4 °C. The classes not found in each dataset are shown as transparent. The pie charts depict particle distributions among classes for each dataset along with representative micrographs. Each pie chart represents an average value for four independent data processes (Supplementary Fig. , ).
    Figure Legend Snippet: a A representative macroscopic current time-course (top panel) recorded from a HEK-293T cell expressing rat TRPV1 in response to the temperature ramp (10–50 °C) at a membrane potential of −60 mV and then followed by a saturating concentration of RTx (50 nM) and 20 µM ruthenium red (RR). The dashed line indicates zero current. The recorded temperature is shown in the middle panel. The Arrhenius plot for the temperature activation was shown in the bottom panel. Fitted Q 10 values for high (blue line) and low (red line) temperature ranges are shown. A representative time-course recording for RTx-bound TRPV1 temperature sensitivity. First the channel was challenged by 10 nM RTx for ~20 s followed by a temperature ramp (10–48 °C), then a saturating concentration of RTx (50 nM) was introduced, and finally RR (20 µM) was applied to completely block the channel. The dashed line indicates zero current. The recorded temperature is shown in the middle panel and the Arrhenius plot for the temperature activation is shown in the bottom panel. Fitted Q 10 values for high and low temperature (T) ranges are shown. c Q 10 values as a function of I/I 50nM RTx for low and high temperature ranges. Each experiment was conducted as shown in a and . The low T range Q 10 value is steady at 1.7, while the high T range Q 10 rapidly collapses from ~38 to ~3. Each pair of high and low temperature sensitivity data points represents independent time-course recordings from individual cells ( n = 17 cells). Source data are provided as a Source Data file. d Representative micrographs of TRPV1 recorded in the presence of 50 μM RTx at 4 °C, 25 °C and 48 °C, respectively. Cryo-EM maps of RTx-TRPV1 determined at 4 °C (class I, class II, and class III), 25 °C (class A and class B), and 48 °C (class α). Note the differences between central pore sizes amongst different classes at 4 °C. The classes not found in each dataset are shown as transparent. The pie charts depict particle distributions among classes for each dataset along with representative micrographs. Each pie chart represents an average value for four independent data processes (Supplementary Fig. , ).

    Techniques Used: Expressing, Concentration Assay, Activation Assay, Blocking Assay, Cryo-EM Sample Prep

    a Comparison of the pore domain structures, only two subunits are shown for clarity, with the S6 gate (S6b), selectivity filter (SF), pore loop (PL) and pore helix (PH) as indicated. The pore profiles are shown as surfaces (gray). The red arrows indicate direction of movement. b Comparison of TRPV1 C,RTx (gray) and TRPV1 IC,RTx (green) structures (left) and close-up view of TRPV1 C,RTx and TRPV1 IC,RTx pore region (right). c The cryo-EM densities and the models for M644 in TRPV1 IC,RTx (green) and TRPV1 IO,RTx (gold). The cryo-EM map thresholdings are 0.03, and 0.04, respectively. d Comparison of TRPV1 IO, RTx (gold) and TRPV1 O, RTx (pink) outer pore region. Representative residues showing large motions are shown as sticks. TJ, turret junction. Phospholipids are shown as sticks and cryo-EM densities, with thresholding at 0.035 and 0.029, respectively.
    Figure Legend Snippet: a Comparison of the pore domain structures, only two subunits are shown for clarity, with the S6 gate (S6b), selectivity filter (SF), pore loop (PL) and pore helix (PH) as indicated. The pore profiles are shown as surfaces (gray). The red arrows indicate direction of movement. b Comparison of TRPV1 C,RTx (gray) and TRPV1 IC,RTx (green) structures (left) and close-up view of TRPV1 C,RTx and TRPV1 IC,RTx pore region (right). c The cryo-EM densities and the models for M644 in TRPV1 IC,RTx (green) and TRPV1 IO,RTx (gold). The cryo-EM map thresholdings are 0.03, and 0.04, respectively. d Comparison of TRPV1 IO, RTx (gold) and TRPV1 O, RTx (pink) outer pore region. Representative residues showing large motions are shown as sticks. TJ, turret junction. Phospholipids are shown as sticks and cryo-EM densities, with thresholding at 0.035 and 0.029, respectively.

    Techniques Used: Cryo-EM Sample Prep

    The cryo-EM densities (grey surface) and respective models (cartoon) depicting bottom-up views of the S6 gate (top), top-down views of the selectivity filter (middle), top-down views of the monomeric outer pore (bottom), and local estimated resolutions for TRPV1 C, RTx a , blue, thresholding 0.12); TRPV1 IC, RTx b , cyan, thresholding 0.035); TRPV1 IO, RTx c , orange, thresholding 0.09); TRPV1 O, RTx,4 °C d , green, thresholding 0.1); TRPV1 O, RTx,25 °C e , brown, thresholding 0.08); and TRPV1 O, RTx,48 °C f , red, thresholding 0.033).
    Figure Legend Snippet: The cryo-EM densities (grey surface) and respective models (cartoon) depicting bottom-up views of the S6 gate (top), top-down views of the selectivity filter (middle), top-down views of the monomeric outer pore (bottom), and local estimated resolutions for TRPV1 C, RTx a , blue, thresholding 0.12); TRPV1 IC, RTx b , cyan, thresholding 0.035); TRPV1 IO, RTx c , orange, thresholding 0.09); TRPV1 O, RTx,4 °C d , green, thresholding 0.1); TRPV1 O, RTx,25 °C e , brown, thresholding 0.08); and TRPV1 O, RTx,48 °C f , red, thresholding 0.033).

    Techniques Used: Cryo-EM Sample Prep

    a Cylinder representation of TRPV1 in turquoise (one subunit) and gray (the rest of the channel). The approximate distances from the RTx binding site (reference residue Y511) to subdomains are shown. b The cryo-EM densities (surface) and respective models (sticks) depicting close-up views of the vanilloid binding sites in TRPV1 C, RTx (skyblue), thresholding 0.19, TRPV1 IO, RTx (yellow), thresholding 0.04, and TRPV1 O, RTx (pink), thresholding 0.033. c The cryo-EM densities (surface) and respective models (sticks) depicting close-up views of the selectivity filter in TRPV1 C,RTx (skyblue), thresholding 0.19, TRPV1 IC,RTx (green), thresholding 0.04, TRPV1 IO,RTx (yellow), thresholding 0.1, and TRPV1 O,RTx (pink), thresholding 0.033. d – e Close-up view of the overlays of TRPV1 C, RTx (skyblue), TRPV1 IO, RTx (yellow), and TRPV1 O, RTx (pink) regarding the cytoplasmic domain, and S6 gate e , respectively.
    Figure Legend Snippet: a Cylinder representation of TRPV1 in turquoise (one subunit) and gray (the rest of the channel). The approximate distances from the RTx binding site (reference residue Y511) to subdomains are shown. b The cryo-EM densities (surface) and respective models (sticks) depicting close-up views of the vanilloid binding sites in TRPV1 C, RTx (skyblue), thresholding 0.19, TRPV1 IO, RTx (yellow), thresholding 0.04, and TRPV1 O, RTx (pink), thresholding 0.033. c The cryo-EM densities (surface) and respective models (sticks) depicting close-up views of the selectivity filter in TRPV1 C,RTx (skyblue), thresholding 0.19, TRPV1 IC,RTx (green), thresholding 0.04, TRPV1 IO,RTx (yellow), thresholding 0.1, and TRPV1 O,RTx (pink), thresholding 0.033. d – e Close-up view of the overlays of TRPV1 C, RTx (skyblue), TRPV1 IO, RTx (yellow), and TRPV1 O, RTx (pink) regarding the cytoplasmic domain, and S6 gate e , respectively.

    Techniques Used: Binding Assay, Cryo-EM Sample Prep

    a The cryo-EM maps (surface) and respective models (sticks) depicting the tripartite hydrogen bond network of PH-S5-S6 in TRPV1 C, RTx (skyblue), thresholding 0.15, TRPV1 IC, RTx (yellow), thresholding 0.045, TRPV1 IO, RTx (gold), thresholding 0.1, and TRPV1 O, RTx (pink), thresholding 0.04. The black dotted-lines indicate hydrogen bonds. The red dotted-lines indicate distance measurements between atoms where hydrogen bonds are broken. b – e TRPV1 Y584F and T641A reduce large cation permeabilty (YO-PRO-1, M.W. 376 Da) in the presence of RTx. Representative inside-out current traces of TRPV1 WT b , TRPV1 Y584F c , and TRPV1 T641A d . Current traces for basal, RTx (200 nM) activation (red trace) and intracellular application of 10 μM YO-PRO-1 (blue trace). e Summary of current inhibition by YO-PRO-1 (10 µM) of TRPV1 WT, TRPV1 Y584F and TRPV1 T641A after application of a saturating concentration of RTx (200 nM). Data are presented as mean ± s.e.m.; P < 0.0001 for T641A and Y584F, two-tailed unpaired Student’s t test. (For WT, n = 5, for Y584F and T641A, n = 4). Source data are provided as a Source Data file.
    Figure Legend Snippet: a The cryo-EM maps (surface) and respective models (sticks) depicting the tripartite hydrogen bond network of PH-S5-S6 in TRPV1 C, RTx (skyblue), thresholding 0.15, TRPV1 IC, RTx (yellow), thresholding 0.045, TRPV1 IO, RTx (gold), thresholding 0.1, and TRPV1 O, RTx (pink), thresholding 0.04. The black dotted-lines indicate hydrogen bonds. The red dotted-lines indicate distance measurements between atoms where hydrogen bonds are broken. b – e TRPV1 Y584F and T641A reduce large cation permeabilty (YO-PRO-1, M.W. 376 Da) in the presence of RTx. Representative inside-out current traces of TRPV1 WT b , TRPV1 Y584F c , and TRPV1 T641A d . Current traces for basal, RTx (200 nM) activation (red trace) and intracellular application of 10 μM YO-PRO-1 (blue trace). e Summary of current inhibition by YO-PRO-1 (10 µM) of TRPV1 WT, TRPV1 Y584F and TRPV1 T641A after application of a saturating concentration of RTx (200 nM). Data are presented as mean ± s.e.m.; P < 0.0001 for T641A and Y584F, two-tailed unpaired Student’s t test. (For WT, n = 5, for Y584F and T641A, n = 4). Source data are provided as a Source Data file.

    Techniques Used: Cryo-EM Sample Prep, Activation Assay, Inhibition, Concentration Assay, Two Tailed Test

    rtx  (Alomone Labs)


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    rtx  (Alomone Labs)


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    Alomone Labs rtx
    Stimulation of brown adipogenesis by supra-pharmacological capsaicin in a Trpv1-independent manner. ( A ) HB2 brown preadipocytes loaded with Fluo-8 AM were treated with capsaicin (100 μM) or A23187 (1 μM) in the absence of extracellular calcium and in the presence or absence of <t>I-RTX</t> (1 μM), and cytosolic calcium level was evaluated. ( B – D ) HB2 brown preadipocytes were cultured with 100 μM of capsaicin in the presence or absence of I-RTX (1 μM) during brown adipogenesis. ( B ) Oil Red O staining of cells on day 8 was performed and the dye intensity was quantified (n = 2). ( C and D ) Expression levels of Ucp1 ( C ) or Pref-1 ( D ) on day 8 were examined by RT-qPCR analysis. Black bar: vehicle; Hatched bar: capsaicin. The data are presented as the mean ± SE (n = 4). ** P < 0.01 vs . cells treated with vehicle and corresponding reagent (vehicle or I-RTX). ‡ P < 0.01 vs . cells treated with vehicle and corresponding reagent (vehicle or capsaicin).
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    1) Product Images from "Supra-pharmacological concentration of capsaicin stimulates brown adipogenesis through induction of endoplasmic reticulum stress"

    Article Title: Supra-pharmacological concentration of capsaicin stimulates brown adipogenesis through induction of endoplasmic reticulum stress

    Journal: Scientific Reports

    doi: 10.1038/s41598-018-19223-2

    Stimulation of brown adipogenesis by supra-pharmacological capsaicin in a Trpv1-independent manner. ( A ) HB2 brown preadipocytes loaded with Fluo-8 AM were treated with capsaicin (100 μM) or A23187 (1 μM) in the absence of extracellular calcium and in the presence or absence of I-RTX (1 μM), and cytosolic calcium level was evaluated. ( B – D ) HB2 brown preadipocytes were cultured with 100 μM of capsaicin in the presence or absence of I-RTX (1 μM) during brown adipogenesis. ( B ) Oil Red O staining of cells on day 8 was performed and the dye intensity was quantified (n = 2). ( C and D ) Expression levels of Ucp1 ( C ) or Pref-1 ( D ) on day 8 were examined by RT-qPCR analysis. Black bar: vehicle; Hatched bar: capsaicin. The data are presented as the mean ± SE (n = 4). ** P < 0.01 vs . cells treated with vehicle and corresponding reagent (vehicle or I-RTX). ‡ P < 0.01 vs . cells treated with vehicle and corresponding reagent (vehicle or capsaicin).
    Figure Legend Snippet: Stimulation of brown adipogenesis by supra-pharmacological capsaicin in a Trpv1-independent manner. ( A ) HB2 brown preadipocytes loaded with Fluo-8 AM were treated with capsaicin (100 μM) or A23187 (1 μM) in the absence of extracellular calcium and in the presence or absence of I-RTX (1 μM), and cytosolic calcium level was evaluated. ( B – D ) HB2 brown preadipocytes were cultured with 100 μM of capsaicin in the presence or absence of I-RTX (1 μM) during brown adipogenesis. ( B ) Oil Red O staining of cells on day 8 was performed and the dye intensity was quantified (n = 2). ( C and D ) Expression levels of Ucp1 ( C ) or Pref-1 ( D ) on day 8 were examined by RT-qPCR analysis. Black bar: vehicle; Hatched bar: capsaicin. The data are presented as the mean ± SE (n = 4). ** P < 0.01 vs . cells treated with vehicle and corresponding reagent (vehicle or I-RTX). ‡ P < 0.01 vs . cells treated with vehicle and corresponding reagent (vehicle or capsaicin).

    Techniques Used: Cell Culture, Staining, Expressing, Quantitative RT-PCR

    rtx treatment  (Alomone Labs)


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    Alomone Labs rtx treatment
    Phenotypic changes in prostatic acid phosphatase (PAP)(+) dorsal root ganglion neurons in resiniferatoxin <t>(RTX)-induced</t> neuropathy. (a–e) Double immunofluorescence staining was performed with anti-activating transcription factor 3 (ATF3; a–e in red) and anti-PAP (a–e in green) antisera in the vehicle (a), RTX (b), 4-methylcatechol (4MC) <t>(c),</t> <t>NGF</t> (RTX + 2.5S NGF; d), and (e) abNGF (4MC + anti-NGF antisera) groups. (f–h) The graphs quantify the density changes in (f) PAP(+) and (g) ATF3(+) neurons and (h) the ratio changes in ATF3(+)/PAP(+) neurons according to Panels (a) to (e). (i) The mechanical thresholds were assessed using the up-and-down method with von Frey monofilaments, as described in the Materials and Methods. The graph indicates the changes in the mechanical thresholds in the vehicle (open bar), RTX (filled bar), 4MC (grey bar), NGF (slashed bar), and abNGF (dotted bar) groups. (j, k) The graphs indicate that the mechanical thresholds correlated with PAP expression, that is, a linear correlation with (j) PAP densities and (k) an inverse correlation with the ratio of ATF3(+)/PAP(+) neurons. (l, m) The graphs show the diameter histogram of ATF3(+)/PAP(+) neurons in the RTX (l) and 4MC (M) groups. The diameter histogram shows no difference between the RTX and 4MC groups, but higher numbers of ATF3(+)/PAP(+) neurons in the RTX group. Bar, 50 µm. * p < 0.05, ** p < 0.01, *** p < 0.001.
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    1) Product Images from "NGF-trkA signaling modulates the analgesic effects of prostatic acid phosphatase in resiniferatoxin-induced neuropathy"

    Article Title: NGF-trkA signaling modulates the analgesic effects of prostatic acid phosphatase in resiniferatoxin-induced neuropathy

    Journal: Molecular Pain

    doi: 10.1177/1744806916656846

    Phenotypic changes in prostatic acid phosphatase (PAP)(+) dorsal root ganglion neurons in resiniferatoxin (RTX)-induced neuropathy. (a–e) Double immunofluorescence staining was performed with anti-activating transcription factor 3 (ATF3; a–e in red) and anti-PAP (a–e in green) antisera in the vehicle (a), RTX (b), 4-methylcatechol (4MC) (c), NGF (RTX + 2.5S NGF; d), and (e) abNGF (4MC + anti-NGF antisera) groups. (f–h) The graphs quantify the density changes in (f) PAP(+) and (g) ATF3(+) neurons and (h) the ratio changes in ATF3(+)/PAP(+) neurons according to Panels (a) to (e). (i) The mechanical thresholds were assessed using the up-and-down method with von Frey monofilaments, as described in the Materials and Methods. The graph indicates the changes in the mechanical thresholds in the vehicle (open bar), RTX (filled bar), 4MC (grey bar), NGF (slashed bar), and abNGF (dotted bar) groups. (j, k) The graphs indicate that the mechanical thresholds correlated with PAP expression, that is, a linear correlation with (j) PAP densities and (k) an inverse correlation with the ratio of ATF3(+)/PAP(+) neurons. (l, m) The graphs show the diameter histogram of ATF3(+)/PAP(+) neurons in the RTX (l) and 4MC (M) groups. The diameter histogram shows no difference between the RTX and 4MC groups, but higher numbers of ATF3(+)/PAP(+) neurons in the RTX group. Bar, 50 µm. * p < 0.05, ** p < 0.01, *** p < 0.001.
    Figure Legend Snippet: Phenotypic changes in prostatic acid phosphatase (PAP)(+) dorsal root ganglion neurons in resiniferatoxin (RTX)-induced neuropathy. (a–e) Double immunofluorescence staining was performed with anti-activating transcription factor 3 (ATF3; a–e in red) and anti-PAP (a–e in green) antisera in the vehicle (a), RTX (b), 4-methylcatechol (4MC) (c), NGF (RTX + 2.5S NGF; d), and (e) abNGF (4MC + anti-NGF antisera) groups. (f–h) The graphs quantify the density changes in (f) PAP(+) and (g) ATF3(+) neurons and (h) the ratio changes in ATF3(+)/PAP(+) neurons according to Panels (a) to (e). (i) The mechanical thresholds were assessed using the up-and-down method with von Frey monofilaments, as described in the Materials and Methods. The graph indicates the changes in the mechanical thresholds in the vehicle (open bar), RTX (filled bar), 4MC (grey bar), NGF (slashed bar), and abNGF (dotted bar) groups. (j, k) The graphs indicate that the mechanical thresholds correlated with PAP expression, that is, a linear correlation with (j) PAP densities and (k) an inverse correlation with the ratio of ATF3(+)/PAP(+) neurons. (l, m) The graphs show the diameter histogram of ATF3(+)/PAP(+) neurons in the RTX (l) and 4MC (M) groups. The diameter histogram shows no difference between the RTX and 4MC groups, but higher numbers of ATF3(+)/PAP(+) neurons in the RTX group. Bar, 50 µm. * p < 0.05, ** p < 0.01, *** p < 0.001.

    Techniques Used: Double Immunofluorescence Staining, Expressing

    Colocalization of prostatic acid phosphatase (PAP) and high-affinity nerve growth factor (trkA) receptor after resiniferatoxin (RTX)-induced neuropathy. (a–j) Double immunofluorescence staining of dorsal root ganglia sections was performed with anti-PAP (a–e) and trkA (f-j) in the vehicle (a, f), RTX (b, g), 4-methylcatechol (4MC; c, h), (d, i) NGF (RTX + 2.5S NGF), and (e, j) abNGF (4MC + anti-NGF antisera) groups. (k, l) The graphs show the changes in (k) trkA density and (l) the colocalized ratios of PAP(+)/trkA(+) neurons in the vehicle (open bar), RTX (filled bar), 4MC (grey bar), NGF (slashed bar), and abNGF groups (dotted bar) according to Panels (a) to (j). (m) The graph shows that the mechanical thresholds correlate linearly with the ratios of PAP(+)/trkA(+) neurons. Bar, 50 µm. * p < 0.05, ** p < 0.01.
    Figure Legend Snippet: Colocalization of prostatic acid phosphatase (PAP) and high-affinity nerve growth factor (trkA) receptor after resiniferatoxin (RTX)-induced neuropathy. (a–j) Double immunofluorescence staining of dorsal root ganglia sections was performed with anti-PAP (a–e) and trkA (f-j) in the vehicle (a, f), RTX (b, g), 4-methylcatechol (4MC; c, h), (d, i) NGF (RTX + 2.5S NGF), and (e, j) abNGF (4MC + anti-NGF antisera) groups. (k, l) The graphs show the changes in (k) trkA density and (l) the colocalized ratios of PAP(+)/trkA(+) neurons in the vehicle (open bar), RTX (filled bar), 4MC (grey bar), NGF (slashed bar), and abNGF groups (dotted bar) according to Panels (a) to (j). (m) The graph shows that the mechanical thresholds correlate linearly with the ratios of PAP(+)/trkA(+) neurons. Bar, 50 µm. * p < 0.05, ** p < 0.01.

    Techniques Used: Double Immunofluorescence Staining

    Diagram of prostatic acid phosphatase (PAP) pathology modulates the pain perception in resiniferatoxin (RTX) neuropathy. This diagram illustrates the PAP pathology mediating pain development follows a NGF-trkA-dependent manner, as described in the following steps: (1) RTX sensitizes the transient receptor potential vanilloid subtype 1 (TRPV1). (2) RTX then induces activating transcription factor 3 (ATF3) upregulation on PAP(+) neurons, indicating the PAP pathology. (3) The PAP pathology reduces the AMP hydrolysis. (4) This reduction evokes pain perception because of the decrease in the adenosine analgesic effect. (5) Nerve growth factor (NGF) binds to high-affinity NGF receptor (trkA) and (6) reverses the induction of the ATF3 and PAP pathology. (7) This recovers the PAP-mediated analgesic effect by returning the ability of AMP hydrolysis.
    Figure Legend Snippet: Diagram of prostatic acid phosphatase (PAP) pathology modulates the pain perception in resiniferatoxin (RTX) neuropathy. This diagram illustrates the PAP pathology mediating pain development follows a NGF-trkA-dependent manner, as described in the following steps: (1) RTX sensitizes the transient receptor potential vanilloid subtype 1 (TRPV1). (2) RTX then induces activating transcription factor 3 (ATF3) upregulation on PAP(+) neurons, indicating the PAP pathology. (3) The PAP pathology reduces the AMP hydrolysis. (4) This reduction evokes pain perception because of the decrease in the adenosine analgesic effect. (5) Nerve growth factor (NGF) binds to high-affinity NGF receptor (trkA) and (6) reverses the induction of the ATF3 and PAP pathology. (7) This recovers the PAP-mediated analgesic effect by returning the ability of AMP hydrolysis.

    Techniques Used:

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    Phenotypic changes in prostatic acid phosphatase (PAP)(+) dorsal root ganglion neurons in resiniferatoxin <t>(RTX)-induced</t> neuropathy. (a–e) Double immunofluorescence staining was performed with anti-activating transcription factor 3 (ATF3; a–e in red) and anti-PAP (a–e in green) antisera in the vehicle (a), RTX (b), 4-methylcatechol (4MC) <t>(c),</t> <t>NGF</t> (RTX + 2.5S NGF; d), and (e) abNGF (4MC + anti-NGF antisera) groups. (f–h) The graphs quantify the density changes in (f) PAP(+) and (g) ATF3(+) neurons and (h) the ratio changes in ATF3(+)/PAP(+) neurons according to Panels (a) to (e). (i) The mechanical thresholds were assessed using the up-and-down method with von Frey monofilaments, as described in the Materials and Methods. The graph indicates the changes in the mechanical thresholds in the vehicle (open bar), RTX (filled bar), 4MC (grey bar), NGF (slashed bar), and abNGF (dotted bar) groups. (j, k) The graphs indicate that the mechanical thresholds correlated with PAP expression, that is, a linear correlation with (j) PAP densities and (k) an inverse correlation with the ratio of ATF3(+)/PAP(+) neurons. (l, m) The graphs show the diameter histogram of ATF3(+)/PAP(+) neurons in the RTX (l) and 4MC (M) groups. The diameter histogram shows no difference between the RTX and 4MC groups, but higher numbers of ATF3(+)/PAP(+) neurons in the RTX group. Bar, 50 µm. * p < 0.05, ** p < 0.01, *** p < 0.001.
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    Phenotypic changes in prostatic acid phosphatase (PAP)(+) dorsal root ganglion neurons in resiniferatoxin (RTX)-induced neuropathy. (a–e) Double immunofluorescence staining was performed with anti-activating transcription factor 3 (ATF3; a–e in red) and anti-PAP (a–e in green) antisera in the vehicle (a), RTX (b), 4-methylcatechol (4MC) (c), NGF (RTX + 2.5S NGF; d), and (e) abNGF (4MC + anti-NGF antisera) groups. (f–h) The graphs quantify the density changes in (f) PAP(+) and (g) ATF3(+) neurons and (h) the ratio changes in ATF3(+)/PAP(+) neurons according to Panels (a) to (e). (i) The mechanical thresholds were assessed using the up-and-down method with von Frey monofilaments, as described in the Materials and Methods. The graph indicates the changes in the mechanical thresholds in the vehicle (open bar), RTX (filled bar), 4MC (grey bar), NGF (slashed bar), and abNGF (dotted bar) groups. (j, k) The graphs indicate that the mechanical thresholds correlated with PAP expression, that is, a linear correlation with (j) PAP densities and (k) an inverse correlation with the ratio of ATF3(+)/PAP(+) neurons. (l, m) The graphs show the diameter histogram of ATF3(+)/PAP(+) neurons in the RTX (l) and 4MC (M) groups. The diameter histogram shows no difference between the RTX and 4MC groups, but higher numbers of ATF3(+)/PAP(+) neurons in the RTX group. Bar, 50 µm. * p < 0.05, ** p < 0.01, *** p < 0.001.

    Journal: Molecular Pain

    Article Title: NGF-trkA signaling modulates the analgesic effects of prostatic acid phosphatase in resiniferatoxin-induced neuropathy

    doi: 10.1177/1744806916656846

    Figure Lengend Snippet: Phenotypic changes in prostatic acid phosphatase (PAP)(+) dorsal root ganglion neurons in resiniferatoxin (RTX)-induced neuropathy. (a–e) Double immunofluorescence staining was performed with anti-activating transcription factor 3 (ATF3; a–e in red) and anti-PAP (a–e in green) antisera in the vehicle (a), RTX (b), 4-methylcatechol (4MC) (c), NGF (RTX + 2.5S NGF; d), and (e) abNGF (4MC + anti-NGF antisera) groups. (f–h) The graphs quantify the density changes in (f) PAP(+) and (g) ATF3(+) neurons and (h) the ratio changes in ATF3(+)/PAP(+) neurons according to Panels (a) to (e). (i) The mechanical thresholds were assessed using the up-and-down method with von Frey monofilaments, as described in the Materials and Methods. The graph indicates the changes in the mechanical thresholds in the vehicle (open bar), RTX (filled bar), 4MC (grey bar), NGF (slashed bar), and abNGF (dotted bar) groups. (j, k) The graphs indicate that the mechanical thresholds correlated with PAP expression, that is, a linear correlation with (j) PAP densities and (k) an inverse correlation with the ratio of ATF3(+)/PAP(+) neurons. (l, m) The graphs show the diameter histogram of ATF3(+)/PAP(+) neurons in the RTX (l) and 4MC (M) groups. The diameter histogram shows no difference between the RTX and 4MC groups, but higher numbers of ATF3(+)/PAP(+) neurons in the RTX group. Bar, 50 µm. * p < 0.05, ** p < 0.01, *** p < 0.001.

    Article Snippet: Briefly, 2.5S NGF (Alomone Labs, Jerusalem, Israel) was dissolved in Dulbecco’s Modified Eagle Medium, and mice received NGF (1 µg/10 g) immediately after RTX treatment (the NGF group).

    Techniques: Double Immunofluorescence Staining, Expressing

    Colocalization of prostatic acid phosphatase (PAP) and high-affinity nerve growth factor (trkA) receptor after resiniferatoxin (RTX)-induced neuropathy. (a–j) Double immunofluorescence staining of dorsal root ganglia sections was performed with anti-PAP (a–e) and trkA (f-j) in the vehicle (a, f), RTX (b, g), 4-methylcatechol (4MC; c, h), (d, i) NGF (RTX + 2.5S NGF), and (e, j) abNGF (4MC + anti-NGF antisera) groups. (k, l) The graphs show the changes in (k) trkA density and (l) the colocalized ratios of PAP(+)/trkA(+) neurons in the vehicle (open bar), RTX (filled bar), 4MC (grey bar), NGF (slashed bar), and abNGF groups (dotted bar) according to Panels (a) to (j). (m) The graph shows that the mechanical thresholds correlate linearly with the ratios of PAP(+)/trkA(+) neurons. Bar, 50 µm. * p < 0.05, ** p < 0.01.

    Journal: Molecular Pain

    Article Title: NGF-trkA signaling modulates the analgesic effects of prostatic acid phosphatase in resiniferatoxin-induced neuropathy

    doi: 10.1177/1744806916656846

    Figure Lengend Snippet: Colocalization of prostatic acid phosphatase (PAP) and high-affinity nerve growth factor (trkA) receptor after resiniferatoxin (RTX)-induced neuropathy. (a–j) Double immunofluorescence staining of dorsal root ganglia sections was performed with anti-PAP (a–e) and trkA (f-j) in the vehicle (a, f), RTX (b, g), 4-methylcatechol (4MC; c, h), (d, i) NGF (RTX + 2.5S NGF), and (e, j) abNGF (4MC + anti-NGF antisera) groups. (k, l) The graphs show the changes in (k) trkA density and (l) the colocalized ratios of PAP(+)/trkA(+) neurons in the vehicle (open bar), RTX (filled bar), 4MC (grey bar), NGF (slashed bar), and abNGF groups (dotted bar) according to Panels (a) to (j). (m) The graph shows that the mechanical thresholds correlate linearly with the ratios of PAP(+)/trkA(+) neurons. Bar, 50 µm. * p < 0.05, ** p < 0.01.

    Article Snippet: Briefly, 2.5S NGF (Alomone Labs, Jerusalem, Israel) was dissolved in Dulbecco’s Modified Eagle Medium, and mice received NGF (1 µg/10 g) immediately after RTX treatment (the NGF group).

    Techniques: Double Immunofluorescence Staining

    Diagram of prostatic acid phosphatase (PAP) pathology modulates the pain perception in resiniferatoxin (RTX) neuropathy. This diagram illustrates the PAP pathology mediating pain development follows a NGF-trkA-dependent manner, as described in the following steps: (1) RTX sensitizes the transient receptor potential vanilloid subtype 1 (TRPV1). (2) RTX then induces activating transcription factor 3 (ATF3) upregulation on PAP(+) neurons, indicating the PAP pathology. (3) The PAP pathology reduces the AMP hydrolysis. (4) This reduction evokes pain perception because of the decrease in the adenosine analgesic effect. (5) Nerve growth factor (NGF) binds to high-affinity NGF receptor (trkA) and (6) reverses the induction of the ATF3 and PAP pathology. (7) This recovers the PAP-mediated analgesic effect by returning the ability of AMP hydrolysis.

    Journal: Molecular Pain

    Article Title: NGF-trkA signaling modulates the analgesic effects of prostatic acid phosphatase in resiniferatoxin-induced neuropathy

    doi: 10.1177/1744806916656846

    Figure Lengend Snippet: Diagram of prostatic acid phosphatase (PAP) pathology modulates the pain perception in resiniferatoxin (RTX) neuropathy. This diagram illustrates the PAP pathology mediating pain development follows a NGF-trkA-dependent manner, as described in the following steps: (1) RTX sensitizes the transient receptor potential vanilloid subtype 1 (TRPV1). (2) RTX then induces activating transcription factor 3 (ATF3) upregulation on PAP(+) neurons, indicating the PAP pathology. (3) The PAP pathology reduces the AMP hydrolysis. (4) This reduction evokes pain perception because of the decrease in the adenosine analgesic effect. (5) Nerve growth factor (NGF) binds to high-affinity NGF receptor (trkA) and (6) reverses the induction of the ATF3 and PAP pathology. (7) This recovers the PAP-mediated analgesic effect by returning the ability of AMP hydrolysis.

    Article Snippet: Briefly, 2.5S NGF (Alomone Labs, Jerusalem, Israel) was dissolved in Dulbecco’s Modified Eagle Medium, and mice received NGF (1 µg/10 g) immediately after RTX treatment (the NGF group).

    Techniques: