trpv1  (Alomone Labs)


Bioz Verified Symbol Alomone Labs is a verified supplier
Bioz Manufacturer Symbol Alomone Labs manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Alomone Labs trpv1
    A , B , Prevention and reversal of paclitaxel-induced hyperalgesia by intrathecal injection of a <t>TRPV1</t> antagonist (AMG9810). The baseline (BL) behavioral test in A and B were collected before paclitaxel (Pac) or vehicle (Veh) treatments. In A , the gray shading indicates the time of treatment with 15 μg of AMG9810 (intrathecal) or vehicle solution. In B , paclitaxel-induced mechanical hypersensitivity was confirmed as significant from Veh–Veh-treated rats (open squares, n = 5) at 14 d after treatment (P) in two groups (open and filled circles, n = 5 each); rats were then treated with 15 μg of the TRPV1 antagonist AMG9810 intrathecally (filled circles) or vehicle solution (open circles) as indicated by the arrow. * p
    Trpv1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/trpv1/product/Alomone Labs
    Average 94 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    trpv1 - by Bioz Stars, 2022-08
    94/100 stars

    Images

    1) Product Images from "The Cancer Chemotherapeutic Paclitaxel Increases Human and Rodent Sensory Neuron Responses to TRPV1 by Activation of TLR4"

    Article Title: The Cancer Chemotherapeutic Paclitaxel Increases Human and Rodent Sensory Neuron Responses to TRPV1 by Activation of TLR4

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.1956-15.2015

    A , B , Prevention and reversal of paclitaxel-induced hyperalgesia by intrathecal injection of a TRPV1 antagonist (AMG9810). The baseline (BL) behavioral test in A and B were collected before paclitaxel (Pac) or vehicle (Veh) treatments. In A , the gray shading indicates the time of treatment with 15 μg of AMG9810 (intrathecal) or vehicle solution. In B , paclitaxel-induced mechanical hypersensitivity was confirmed as significant from Veh–Veh-treated rats (open squares, n = 5) at 14 d after treatment (P) in two groups (open and filled circles, n = 5 each); rats were then treated with 15 μg of the TRPV1 antagonist AMG9810 intrathecally (filled circles) or vehicle solution (open circles) as indicated by the arrow. * p
    Figure Legend Snippet: A , B , Prevention and reversal of paclitaxel-induced hyperalgesia by intrathecal injection of a TRPV1 antagonist (AMG9810). The baseline (BL) behavioral test in A and B were collected before paclitaxel (Pac) or vehicle (Veh) treatments. In A , the gray shading indicates the time of treatment with 15 μg of AMG9810 (intrathecal) or vehicle solution. In B , paclitaxel-induced mechanical hypersensitivity was confirmed as significant from Veh–Veh-treated rats (open squares, n = 5) at 14 d after treatment (P) in two groups (open and filled circles, n = 5 each); rats were then treated with 15 μg of the TRPV1 antagonist AMG9810 intrathecally (filled circles) or vehicle solution (open circles) as indicated by the arrow. * p

    Techniques Used: Injection

    Immunofluorescent double staining shows that TRPV1 (red, A ) is colocalized with TLR4 (green, B ) in human DRG neurons (yellow in merged image at right, C ). The red arrows in the merged image indicate cells only showing TRPV1, the green arrows indicate cells only expressing TLR4, and the yellows arrow points to cells positive for both TRPV1 and TLR4. Scale bar, 200 μm. Three types of responses were observed when human DRG neurons were tested by application of capsaicin (Cap) and paclitaxel (Pac). Type 1 neurons did not respond to either capsaicin or paclitaxel (data not shown). Type 2 neurons ( D ) responded positively to capsaicin (left column), showed no responses to paclitaxel (center column), and then showed desensitization to a second application of capsaicin (right column). Type 3 neurons ( E ) showed responses to capsaicin (left column) and to paclitaxel (center column) and then showed a facilitation of response to the repeated application of capsaicin (right column). The bar graphs at the bottom show the summarized response for the type 2 and 3 neurons. The baseline response to capsaicin was not different between groups. The second response to capsaicin was significantly reduced compared with the first in the type 2 neurons. The type 3 neurons showed significantly greater responses to paclitaxel than did type 2 neurons; and type 3 neurons showed a significantly increased response to the second application of capsaicin compared with the first. * p
    Figure Legend Snippet: Immunofluorescent double staining shows that TRPV1 (red, A ) is colocalized with TLR4 (green, B ) in human DRG neurons (yellow in merged image at right, C ). The red arrows in the merged image indicate cells only showing TRPV1, the green arrows indicate cells only expressing TLR4, and the yellows arrow points to cells positive for both TRPV1 and TLR4. Scale bar, 200 μm. Three types of responses were observed when human DRG neurons were tested by application of capsaicin (Cap) and paclitaxel (Pac). Type 1 neurons did not respond to either capsaicin or paclitaxel (data not shown). Type 2 neurons ( D ) responded positively to capsaicin (left column), showed no responses to paclitaxel (center column), and then showed desensitization to a second application of capsaicin (right column). Type 3 neurons ( E ) showed responses to capsaicin (left column) and to paclitaxel (center column) and then showed a facilitation of response to the repeated application of capsaicin (right column). The bar graphs at the bottom show the summarized response for the type 2 and 3 neurons. The baseline response to capsaicin was not different between groups. The second response to capsaicin was significantly reduced compared with the first in the type 2 neurons. The type 3 neurons showed significantly greater responses to paclitaxel than did type 2 neurons; and type 3 neurons showed a significantly increased response to the second application of capsaicin compared with the first. * p

    Techniques Used: Double Staining, Expressing

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94
    Alomone Labs rat trpv1
    Photomicrographs of cryosections of canine skin showing transient receptor potential vanilloid 1 <t>(TRPV1)</t> immunoreactivity (IR) in the tissues of the healthy dogs (CTRL) (a–c) and in the dogs with atopic dermatitis (AD) (d–f) . (a–c) The white arrows indicate some DAPI-labeled nuclei of the keratinocytes of the CTRL dogs showing moderate cytoplasmic <t>TRPV1-IR.</t> The open arrows indicate some DAPI-labeled nuclei of the dermal cells showing moderate TRPV1-IR. (d–f) The white arrows indicate some DAPI-labeled nuclei of the keratinocytes of the AD dogs showing bright cytoplasmic TRPV1-IR. The open arrows indicate some DAPI-labeled nuclei of the dermal cells showing bright TRPV1-IR. Bar, 50 μm.
    Rat Trpv1, 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/rat trpv1/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rat trpv1 - by Bioz Stars, 2022-08
    94/100 stars
      Buy from Supplier

    94
    Alomone Labs anti rat trpv1
    Immunofluorescence for CD88, interleukin-8 RA (IL-8RA) and transient receptor potential cation channel subfamily V member 1 <t>(TRPV1)</t> on 3rd day after administration of doxorubicin into mouse dorsal skin followed by 3-hrs compress. Box plot explanation: The median for each group is shown as a box plot with whiskers from minimum to maximum in (B, D and F). The interquartile range is shown as a box with the median marked as a horizontal line, minimum and maximum from lower and upper quartile represent error bar. (A B) Immunofluorescence for CD88 (A) and IL-8RA (C), and the number (per mm 2 ) of CD88 (B) and IL-8RA (D)-positive cells after 3-hrs cold or hot compresses. Immunofluorescence of TRPV1-positive cells (E) and the number (per mm 2 ) of TRPV1-positive nerve fascicles (F) after 3-hrs cold or hot compresses. [(a) TRPV1 (fluorescein isothiocyanate; FITC), (d) α-smooth muscle actin (α-SMA) (tetramethylrhodamine; TRITC), (g) merge TRPV1 (arrowheads); (b) TRPV1 (FITC), (e) α-SMA (TRITC), (h) merge TRPV1 (arrowheads); (c) TRPV1 (FITC), (f) α-SMA (TRITC), (i) merge TRPV1 (arrowheads)]. (a) control group. (b) cold compress group. (c) hot compress group in (A, C and E). Bar = 50 μm, *: P
    Anti Rat Trpv1, 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/anti rat trpv1/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti rat trpv1 - by Bioz Stars, 2022-08
    94/100 stars
      Buy from Supplier

    Image Search Results


    Photomicrographs of cryosections of canine skin showing transient receptor potential vanilloid 1 (TRPV1) immunoreactivity (IR) in the tissues of the healthy dogs (CTRL) (a–c) and in the dogs with atopic dermatitis (AD) (d–f) . (a–c) The white arrows indicate some DAPI-labeled nuclei of the keratinocytes of the CTRL dogs showing moderate cytoplasmic TRPV1-IR. The open arrows indicate some DAPI-labeled nuclei of the dermal cells showing moderate TRPV1-IR. (d–f) The white arrows indicate some DAPI-labeled nuclei of the keratinocytes of the AD dogs showing bright cytoplasmic TRPV1-IR. The open arrows indicate some DAPI-labeled nuclei of the dermal cells showing bright TRPV1-IR. Bar, 50 μm.

    Journal: Frontiers in Veterinary Science

    Article Title: Distribution of Cannabinoid Receptors in Keratinocytes of Healthy Dogs and Dogs With Atopic Dermatitis

    doi: 10.3389/fvets.2022.915896

    Figure Lengend Snippet: Photomicrographs of cryosections of canine skin showing transient receptor potential vanilloid 1 (TRPV1) immunoreactivity (IR) in the tissues of the healthy dogs (CTRL) (a–c) and in the dogs with atopic dermatitis (AD) (d–f) . (a–c) The white arrows indicate some DAPI-labeled nuclei of the keratinocytes of the CTRL dogs showing moderate cytoplasmic TRPV1-IR. The open arrows indicate some DAPI-labeled nuclei of the dermal cells showing moderate TRPV1-IR. (d–f) The white arrows indicate some DAPI-labeled nuclei of the keratinocytes of the AD dogs showing bright cytoplasmic TRPV1-IR. The open arrows indicate some DAPI-labeled nuclei of the dermal cells showing bright TRPV1-IR. Bar, 50 μm.

    Article Snippet: The immunogen of the rabbit anti-TRPV1 (ACC-030) was the peptide (C)EDAEVFK DSMVPGEK (824–838) of rat TRPV1.

    Techniques: Labeling

    Quantification of the intensity of the expression of CB1R (a) , CB2R (b) , GPR55 (c) , PPARα (d) , TRPV1 (e) , TRPA1 (f) , 5-HT1aR (g) , in the suprabasal layers of 7 CTRL- and 8 AD-dogs. Data are represented as Mean ± SD and were analyzed using the Student T -test. P

    Journal: Frontiers in Veterinary Science

    Article Title: Distribution of Cannabinoid Receptors in Keratinocytes of Healthy Dogs and Dogs With Atopic Dermatitis

    doi: 10.3389/fvets.2022.915896

    Figure Lengend Snippet: Quantification of the intensity of the expression of CB1R (a) , CB2R (b) , GPR55 (c) , PPARα (d) , TRPV1 (e) , TRPA1 (f) , 5-HT1aR (g) , in the suprabasal layers of 7 CTRL- and 8 AD-dogs. Data are represented as Mean ± SD and were analyzed using the Student T -test. P

    Article Snippet: The immunogen of the rabbit anti-TRPV1 (ACC-030) was the peptide (C)EDAEVFK DSMVPGEK (824–838) of rat TRPV1.

    Techniques: Expressing

    Photomicrographs of cryosections of canine skin showing transient receptor potential ankyrin 1 (TRPA1) immunoreactivity (IR) in the tissues of the healthy dogs (CTRL) (a–c) and in the dogs with atopic dermatitis (AD) (d–f) . (a–c) The white arrows indicate some DAPI-labeled nuclei of the keratinocytes of the CTRL dogs showing moderate cytoplasmic TRPV1-IR. The TRPA1 immunolabelling was brighter in the more superficial cells. The open arrows indicate some DAPI-labeled nuclei of the dermal cells showing moderate TRPV1-IR. (d–f) The white arrows indicate some DAPI-labeled nuclei of the keratinocytes of the AD dogs showing bright cytoplasmic TRPV1-IR. Not all the cells of the suprabasal layer showed the same degree of TRPA1-IR which was brighter in the cytoplasm of the more superficial cells. The open arrows indicate some DAPI-labeled nuclei of the dermal cells showing bright TRPA1-IR. Bar, 50 μm.

    Journal: Frontiers in Veterinary Science

    Article Title: Distribution of Cannabinoid Receptors in Keratinocytes of Healthy Dogs and Dogs With Atopic Dermatitis

    doi: 10.3389/fvets.2022.915896

    Figure Lengend Snippet: Photomicrographs of cryosections of canine skin showing transient receptor potential ankyrin 1 (TRPA1) immunoreactivity (IR) in the tissues of the healthy dogs (CTRL) (a–c) and in the dogs with atopic dermatitis (AD) (d–f) . (a–c) The white arrows indicate some DAPI-labeled nuclei of the keratinocytes of the CTRL dogs showing moderate cytoplasmic TRPV1-IR. The TRPA1 immunolabelling was brighter in the more superficial cells. The open arrows indicate some DAPI-labeled nuclei of the dermal cells showing moderate TRPV1-IR. (d–f) The white arrows indicate some DAPI-labeled nuclei of the keratinocytes of the AD dogs showing bright cytoplasmic TRPV1-IR. Not all the cells of the suprabasal layer showed the same degree of TRPA1-IR which was brighter in the cytoplasm of the more superficial cells. The open arrows indicate some DAPI-labeled nuclei of the dermal cells showing bright TRPA1-IR. Bar, 50 μm.

    Article Snippet: The immunogen of the rabbit anti-TRPV1 (ACC-030) was the peptide (C)EDAEVFK DSMVPGEK (824–838) of rat TRPV1.

    Techniques: Labeling

    Immunofluorescence for CD88, interleukin-8 RA (IL-8RA) and transient receptor potential cation channel subfamily V member 1 (TRPV1) on 3rd day after administration of doxorubicin into mouse dorsal skin followed by 3-hrs compress. Box plot explanation: The median for each group is shown as a box plot with whiskers from minimum to maximum in (B, D and F). The interquartile range is shown as a box with the median marked as a horizontal line, minimum and maximum from lower and upper quartile represent error bar. (A B) Immunofluorescence for CD88 (A) and IL-8RA (C), and the number (per mm 2 ) of CD88 (B) and IL-8RA (D)-positive cells after 3-hrs cold or hot compresses. Immunofluorescence of TRPV1-positive cells (E) and the number (per mm 2 ) of TRPV1-positive nerve fascicles (F) after 3-hrs cold or hot compresses. [(a) TRPV1 (fluorescein isothiocyanate; FITC), (d) α-smooth muscle actin (α-SMA) (tetramethylrhodamine; TRITC), (g) merge TRPV1 (arrowheads); (b) TRPV1 (FITC), (e) α-SMA (TRITC), (h) merge TRPV1 (arrowheads); (c) TRPV1 (FITC), (f) α-SMA (TRITC), (i) merge TRPV1 (arrowheads)]. (a) control group. (b) cold compress group. (c) hot compress group in (A, C and E). Bar = 50 μm, *: P

    Journal: International Journal of Clinical and Experimental Pathology

    Article Title: Effect of cold and hot compress on neutrophilic migration to the site of doxorubicin extravasation

    doi:

    Figure Lengend Snippet: Immunofluorescence for CD88, interleukin-8 RA (IL-8RA) and transient receptor potential cation channel subfamily V member 1 (TRPV1) on 3rd day after administration of doxorubicin into mouse dorsal skin followed by 3-hrs compress. Box plot explanation: The median for each group is shown as a box plot with whiskers from minimum to maximum in (B, D and F). The interquartile range is shown as a box with the median marked as a horizontal line, minimum and maximum from lower and upper quartile represent error bar. (A B) Immunofluorescence for CD88 (A) and IL-8RA (C), and the number (per mm 2 ) of CD88 (B) and IL-8RA (D)-positive cells after 3-hrs cold or hot compresses. Immunofluorescence of TRPV1-positive cells (E) and the number (per mm 2 ) of TRPV1-positive nerve fascicles (F) after 3-hrs cold or hot compresses. [(a) TRPV1 (fluorescein isothiocyanate; FITC), (d) α-smooth muscle actin (α-SMA) (tetramethylrhodamine; TRITC), (g) merge TRPV1 (arrowheads); (b) TRPV1 (FITC), (e) α-SMA (TRITC), (h) merge TRPV1 (arrowheads); (c) TRPV1 (FITC), (f) α-SMA (TRITC), (i) merge TRPV1 (arrowheads)]. (a) control group. (b) cold compress group. (c) hot compress group in (A, C and E). Bar = 50 μm, *: P

    Article Snippet: We then fixed the sections with cold acetone (4°C) for 10 min, followed by addition of 3% skim milk (Morinaga Milk Industry, Tokyo, Japan) dissolved in PBS after washing in 0.01 M phosphate-buffered saline, pH 7.4 (PBS), for 15 min. For double immunofluorescence, slide-mounted tissue sections were incubated with a primary antibody [anti-CD88 (C5aR) antibody (rabbit, polyclonal, Santa Cruz Biotechnology, Santa Cruz, CA), anti-rat IL-8RA antibody (recognizing mouse IL-8RA, goat polyclonal, Santa Cruz Biotechnology), anti-rat TRPV1 (recognizing mouse TRPV1, rabbit, polyclonal, Alomone Labs, Jerusalem, Israel) and mouse monoclonal anti-α-SMA antibody (Clone 1A4, mouse IgG2a, Dako, Glostrup, Denmark)] overnight at 4°C.

    Techniques: Immunofluorescence

    Reverse transcription-polymerase chain reaction (RT-PCR) for CD88, interleukin-8 RA (IL-8RA), and transient receptor potential cation channel subfamily V member 1 (TRPV1). mRNAs of CD88, IL-8RA, and TRPV1 including glyceraldehyde-3-phosphate dehydrogenase (GAPDH) were expressed in skin tissue on the first day after doxorubicin administration. MM: molecular marker, Lane 1; positive control (brain), Lane 2; control (no compress), Lane 3; cold compress, Lane 4; hot compress, Lane 5; negative control.

    Journal: International Journal of Clinical and Experimental Pathology

    Article Title: Effect of cold and hot compress on neutrophilic migration to the site of doxorubicin extravasation

    doi:

    Figure Lengend Snippet: Reverse transcription-polymerase chain reaction (RT-PCR) for CD88, interleukin-8 RA (IL-8RA), and transient receptor potential cation channel subfamily V member 1 (TRPV1). mRNAs of CD88, IL-8RA, and TRPV1 including glyceraldehyde-3-phosphate dehydrogenase (GAPDH) were expressed in skin tissue on the first day after doxorubicin administration. MM: molecular marker, Lane 1; positive control (brain), Lane 2; control (no compress), Lane 3; cold compress, Lane 4; hot compress, Lane 5; negative control.

    Article Snippet: We then fixed the sections with cold acetone (4°C) for 10 min, followed by addition of 3% skim milk (Morinaga Milk Industry, Tokyo, Japan) dissolved in PBS after washing in 0.01 M phosphate-buffered saline, pH 7.4 (PBS), for 15 min. For double immunofluorescence, slide-mounted tissue sections were incubated with a primary antibody [anti-CD88 (C5aR) antibody (rabbit, polyclonal, Santa Cruz Biotechnology, Santa Cruz, CA), anti-rat IL-8RA antibody (recognizing mouse IL-8RA, goat polyclonal, Santa Cruz Biotechnology), anti-rat TRPV1 (recognizing mouse TRPV1, rabbit, polyclonal, Alomone Labs, Jerusalem, Israel) and mouse monoclonal anti-α-SMA antibody (Clone 1A4, mouse IgG2a, Dako, Glostrup, Denmark)] overnight at 4°C.

    Techniques: Reverse Transcription Polymerase Chain Reaction, Marker, Positive Control, Negative Control

    Sleep responses induced by sleep deprivation were attenuated in P2X7 receptor knockout (KO) mice compared with wild type (WT) control mice. Mice were deprived of sleep from 0600 to 1200 and then allowed to sleep ad libitum. WT mice exhibited typical NREMS rebound ( right , inset ) and EEG SWA enhancements ( left ). In contrast, P2X7 receptor KO mice had attenuated NREMS and EEG SWA responses during the same period. Both strains had reduced EEG SWA for postdeprivation hours 6–22 ). * P

    Journal: Journal of Applied Physiology

    Article Title: ATP and the purine type 2 X7 receptor affect sleep

    doi: 10.1152/japplphysiol.00586.2010

    Figure Lengend Snippet: Sleep responses induced by sleep deprivation were attenuated in P2X7 receptor knockout (KO) mice compared with wild type (WT) control mice. Mice were deprived of sleep from 0600 to 1200 and then allowed to sleep ad libitum. WT mice exhibited typical NREMS rebound ( right , inset ) and EEG SWA enhancements ( left ). In contrast, P2X7 receptor KO mice had attenuated NREMS and EEG SWA responses during the same period. Both strains had reduced EEG SWA for postdeprivation hours 6–22 ). * P

    Article Snippet: After centrifugation the supernatant (20 μg) was subjected to 4–20% SDS-PAGE gel (Bio-Rad, Hercules, CA), transferred to nitrocellulose membranes, and then incubated overnight with a rabbit polyclonal antibody against rat P2X7 receptor (1:15,000, Alomone Labs, Jerusalem, Israel) and 1:40,000 dilution of monoclonal mouse antibody β-actin (Sigma-Aldrich).

    Techniques: Knock-Out, Mouse Assay

    Expression of P2X7 receptor mRNA in the somatosensory cortex and hypothalamus after 6 h of sleep deprivation (SD) or 2 h and 5 h after intracerebroventricular injection of 2.5 ng of IL1. Left : SD significantly decreased the levels of P2X7 receptor mRNA in the somatosensory cortex, and IL1 enhanced P2X7 mRNA levels both 2 and 5 h after the injection. Right : in the hypothalamus SD enhanced P2X7 mRNA levels, and IL1 significantly decreased P2X7 receptor mRNA. *Significant difference from corresponding control (C).

    Journal: Journal of Applied Physiology

    Article Title: ATP and the purine type 2 X7 receptor affect sleep

    doi: 10.1152/japplphysiol.00586.2010

    Figure Lengend Snippet: Expression of P2X7 receptor mRNA in the somatosensory cortex and hypothalamus after 6 h of sleep deprivation (SD) or 2 h and 5 h after intracerebroventricular injection of 2.5 ng of IL1. Left : SD significantly decreased the levels of P2X7 receptor mRNA in the somatosensory cortex, and IL1 enhanced P2X7 mRNA levels both 2 and 5 h after the injection. Right : in the hypothalamus SD enhanced P2X7 mRNA levels, and IL1 significantly decreased P2X7 receptor mRNA. *Significant difference from corresponding control (C).

    Article Snippet: After centrifugation the supernatant (20 μg) was subjected to 4–20% SDS-PAGE gel (Bio-Rad, Hercules, CA), transferred to nitrocellulose membranes, and then incubated overnight with a rabbit polyclonal antibody against rat P2X7 receptor (1:15,000, Alomone Labs, Jerusalem, Israel) and 1:40,000 dilution of monoclonal mouse antibody β-actin (Sigma-Aldrich).

    Techniques: Expressing, Injection

    Extracellular ATP involvement in sleep regulation. ATP is released into the extracellular space as a consequence of cell activity during neuro- or gliotransmission. Extracellular ATP then activates P2 receptors (R), e.g., P2X7, that in turn are involved in IL1 processing and release as well as release of other sleep regulatory substances such as tumor necrosis factor and brain-derived neurotrophic factor (not shown). IL1, in turn, activates nuclear factor-κB (NF-κB), leading to changes in receptor trafficking. This changes the cell's long-term sensitivity to neurotransmitters such as glutamate (glu) and to neuromodulators such as adenosine. Extracellular ATP is also catabolized to adenosine via the actions of ectonucleotidases such as CD39 and CD73; this action is faster than the ATP-P2-induced changes in transcription and translation. Both actions of ATP are likely involved in sleep regulation. AMPA, amino-3-hydroxy-5-methyl-4-isoxazole proprionic acid.

    Journal: Journal of Applied Physiology

    Article Title: ATP and the purine type 2 X7 receptor affect sleep

    doi: 10.1152/japplphysiol.00586.2010

    Figure Lengend Snippet: Extracellular ATP involvement in sleep regulation. ATP is released into the extracellular space as a consequence of cell activity during neuro- or gliotransmission. Extracellular ATP then activates P2 receptors (R), e.g., P2X7, that in turn are involved in IL1 processing and release as well as release of other sleep regulatory substances such as tumor necrosis factor and brain-derived neurotrophic factor (not shown). IL1, in turn, activates nuclear factor-κB (NF-κB), leading to changes in receptor trafficking. This changes the cell's long-term sensitivity to neurotransmitters such as glutamate (glu) and to neuromodulators such as adenosine. Extracellular ATP is also catabolized to adenosine via the actions of ectonucleotidases such as CD39 and CD73; this action is faster than the ATP-P2-induced changes in transcription and translation. Both actions of ATP are likely involved in sleep regulation. AMPA, amino-3-hydroxy-5-methyl-4-isoxazole proprionic acid.

    Article Snippet: After centrifugation the supernatant (20 μg) was subjected to 4–20% SDS-PAGE gel (Bio-Rad, Hercules, CA), transferred to nitrocellulose membranes, and then incubated overnight with a rabbit polyclonal antibody against rat P2X7 receptor (1:15,000, Alomone Labs, Jerusalem, Israel) and 1:40,000 dilution of monoclonal mouse antibody β-actin (Sigma-Aldrich).

    Techniques: Activity Assay, Derivative Assay

    Both P2X7 receptor antagonists, injected at light onset (filled bars, ●), suppressed NREMS compared with saline injections (open bars, ○). oxidized ATP (OxATP) attenuated SWA during the first 12 h at the 1–4 Hz frequencies. Although EEG SWA was not significantly affected by A438079 during the first 6 h. With select 2-h time bins A438079 induced a biphasic effect, initially suppressing but then augmenting the EEG power spectra at different frequencies (see text for details, data not shown). Two smaller doses of A438079 were also tested, 1 nmol and 10 nmol; neither dose affected any of the parameters measured (* P

    Journal: Journal of Applied Physiology

    Article Title: ATP and the purine type 2 X7 receptor affect sleep

    doi: 10.1152/japplphysiol.00586.2010

    Figure Lengend Snippet: Both P2X7 receptor antagonists, injected at light onset (filled bars, ●), suppressed NREMS compared with saline injections (open bars, ○). oxidized ATP (OxATP) attenuated SWA during the first 12 h at the 1–4 Hz frequencies. Although EEG SWA was not significantly affected by A438079 during the first 6 h. With select 2-h time bins A438079 induced a biphasic effect, initially suppressing but then augmenting the EEG power spectra at different frequencies (see text for details, data not shown). Two smaller doses of A438079 were also tested, 1 nmol and 10 nmol; neither dose affected any of the parameters measured (* P

    Article Snippet: After centrifugation the supernatant (20 μg) was subjected to 4–20% SDS-PAGE gel (Bio-Rad, Hercules, CA), transferred to nitrocellulose membranes, and then incubated overnight with a rabbit polyclonal antibody against rat P2X7 receptor (1:15,000, Alomone Labs, Jerusalem, Israel) and 1:40,000 dilution of monoclonal mouse antibody β-actin (Sigma-Aldrich).

    Techniques: Injection

    Diurnal variation in the relative amount of interleukin-1β (IL1) mRNA and P2X7 receptor mRNA and protein in the hypothalamus and somatosensory cortex. A : Western blot analyses of somatosensory cortex samples showed variation of P2X7 receptor protein levels at 1500 (3 h after light onset) or 0300 (3 h after dark onset). No differences in time of day were observed in the standard, β-actin. B : time course of P2X7 receptor mRNA and protein (▴) and IL1 mRNA (●). The levels of P2X7 receptor protein (somatosensory cortex) and mRNA [(hypothalamus (□) and somatosensory cortex (▼)] were greater during the light period than during the dark period (black horizontal bar indicates dark period). Expression of protein levels was normalized to β-actin levels. *Statistical significance ( P

    Journal: Journal of Applied Physiology

    Article Title: ATP and the purine type 2 X7 receptor affect sleep

    doi: 10.1152/japplphysiol.00586.2010

    Figure Lengend Snippet: Diurnal variation in the relative amount of interleukin-1β (IL1) mRNA and P2X7 receptor mRNA and protein in the hypothalamus and somatosensory cortex. A : Western blot analyses of somatosensory cortex samples showed variation of P2X7 receptor protein levels at 1500 (3 h after light onset) or 0300 (3 h after dark onset). No differences in time of day were observed in the standard, β-actin. B : time course of P2X7 receptor mRNA and protein (▴) and IL1 mRNA (●). The levels of P2X7 receptor protein (somatosensory cortex) and mRNA [(hypothalamus (□) and somatosensory cortex (▼)] were greater during the light period than during the dark period (black horizontal bar indicates dark period). Expression of protein levels was normalized to β-actin levels. *Statistical significance ( P

    Article Snippet: After centrifugation the supernatant (20 μg) was subjected to 4–20% SDS-PAGE gel (Bio-Rad, Hercules, CA), transferred to nitrocellulose membranes, and then incubated overnight with a rabbit polyclonal antibody against rat P2X7 receptor (1:15,000, Alomone Labs, Jerusalem, Israel) and 1:40,000 dilution of monoclonal mouse antibody β-actin (Sigma-Aldrich).

    Techniques: Western Blot, Expressing

    Immunohistochemical detection of TRPC1 protein in rat hearts. Sections were incubated with primary antibody for TRPC1 (A, B, C, D), without primary antibody (E, F, G, H) or with primary antibody preabsorbed by TRPC1 peptide for negative control (I). Positive signals in brown color can be visualized in the myocytes of the left ventricle (A) and atrium (B), endothelial and smooth muscle layers of coronary arterioles (C), and skeletal muscle cells (D, as positive control). No positive signal could be observed in control experiments without primary antibody. A faint signal was occasionally observed in antigen preabsorption control (I). There are negative cells in the edge of ventricular tissues (J) and also the fibroblasts between ventricular myocytes which showed blue nuclei without positive signals. The right ventricle shows the same distribution of TRPC1 positive signal (K) as the left ventricle. TRPC1 showed intense staining on the cell membranes of ventricular myocytes (A, K, L) and skeletal muscle cells (D). The longitudinal section of left ventricle also shows striated distribution of TRPC1 (L). Scale bar =10 µm, except scale bar = 50 µm in panel J.

    Journal: European Journal of Histochemistry : EJH

    Article Title: TRPC1 expression and distribution in rat hearts

    doi: 10.4081/ejh.2009.e26

    Figure Lengend Snippet: Immunohistochemical detection of TRPC1 protein in rat hearts. Sections were incubated with primary antibody for TRPC1 (A, B, C, D), without primary antibody (E, F, G, H) or with primary antibody preabsorbed by TRPC1 peptide for negative control (I). Positive signals in brown color can be visualized in the myocytes of the left ventricle (A) and atrium (B), endothelial and smooth muscle layers of coronary arterioles (C), and skeletal muscle cells (D, as positive control). No positive signal could be observed in control experiments without primary antibody. A faint signal was occasionally observed in antigen preabsorption control (I). There are negative cells in the edge of ventricular tissues (J) and also the fibroblasts between ventricular myocytes which showed blue nuclei without positive signals. The right ventricle shows the same distribution of TRPC1 positive signal (K) as the left ventricle. TRPC1 showed intense staining on the cell membranes of ventricular myocytes (A, K, L) and skeletal muscle cells (D). The longitudinal section of left ventricle also shows striated distribution of TRPC1 (L). Scale bar =10 µm, except scale bar = 50 µm in panel J.

    Article Snippet: Sections were incubated at 4°C overnight with rabbit anti-rat TRPC1 primary antibodies (1:100 dilution, batch number AN-04, Alomone Labs, Jerusalem, Israel).

    Techniques: Immunohistochemistry, Incubation, Negative Control, Positive Control, Staining

    T-PCR based detection of TRPC1 in rat hearts. PCR products were observed in ethidium bromide-stained agarose gel. TRPC1 DNA fragments (467 bp) were amplified from left atrium, right atrium, left ventricle and right ventricle of rats.

    Journal: European Journal of Histochemistry : EJH

    Article Title: TRPC1 expression and distribution in rat hearts

    doi: 10.4081/ejh.2009.e26

    Figure Lengend Snippet: T-PCR based detection of TRPC1 in rat hearts. PCR products were observed in ethidium bromide-stained agarose gel. TRPC1 DNA fragments (467 bp) were amplified from left atrium, right atrium, left ventricle and right ventricle of rats.

    Article Snippet: Sections were incubated at 4°C overnight with rabbit anti-rat TRPC1 primary antibodies (1:100 dilution, batch number AN-04, Alomone Labs, Jerusalem, Israel).

    Techniques: Polymerase Chain Reaction, Staining, Agarose Gel Electrophoresis, Amplification

    Distribution of TRPC1 in Purkinje cells. These sections were contiguous tissue cross-sections. Endocardial layers were shown. Positive signals, brown in color, could be visualized in Purkinje cells (A, black arrows showed Purkinje cells). The cells beneath the endocardium with loose cytoplasmic structure and without any structure around nuclei were Purkinje cells according to HE staining (B, black arrows showed Purkinje cells). No positive signal could be observed in control experiments (C). Scale bar = 10 µm.

    Journal: European Journal of Histochemistry : EJH

    Article Title: TRPC1 expression and distribution in rat hearts

    doi: 10.4081/ejh.2009.e26

    Figure Lengend Snippet: Distribution of TRPC1 in Purkinje cells. These sections were contiguous tissue cross-sections. Endocardial layers were shown. Positive signals, brown in color, could be visualized in Purkinje cells (A, black arrows showed Purkinje cells). The cells beneath the endocardium with loose cytoplasmic structure and without any structure around nuclei were Purkinje cells according to HE staining (B, black arrows showed Purkinje cells). No positive signal could be observed in control experiments (C). Scale bar = 10 µm.

    Article Snippet: Sections were incubated at 4°C overnight with rabbit anti-rat TRPC1 primary antibodies (1:100 dilution, batch number AN-04, Alomone Labs, Jerusalem, Israel).

    Techniques: Staining

    Localization of TRPC1 in rat cardiomyocytes shown by confocal images. Cardiac myocytes were double stained by anti-TRPC1 antibody (A and D) and phalloidin (B and E). Panels C and F show a merged image of panel A/B and D/E respectively, where TRPC1 is colored in red and phalloidin in green. The transverse striation of actin filaments can be seen both in the ventricular myocytes (B) and the atrial myocytes (E). Note that TRPC1 in the ventricular myocyte (A) are parallel to and close to transverse striation of actin filaments, suggesting that they are located at T-tubules while TRPC1 in the atrial myocytes (D) do not show the striation-like distribution. Scale bar =25 µm.

    Journal: European Journal of Histochemistry : EJH

    Article Title: TRPC1 expression and distribution in rat hearts

    doi: 10.4081/ejh.2009.e26

    Figure Lengend Snippet: Localization of TRPC1 in rat cardiomyocytes shown by confocal images. Cardiac myocytes were double stained by anti-TRPC1 antibody (A and D) and phalloidin (B and E). Panels C and F show a merged image of panel A/B and D/E respectively, where TRPC1 is colored in red and phalloidin in green. The transverse striation of actin filaments can be seen both in the ventricular myocytes (B) and the atrial myocytes (E). Note that TRPC1 in the ventricular myocyte (A) are parallel to and close to transverse striation of actin filaments, suggesting that they are located at T-tubules while TRPC1 in the atrial myocytes (D) do not show the striation-like distribution. Scale bar =25 µm.

    Article Snippet: Sections were incubated at 4°C overnight with rabbit anti-rat TRPC1 primary antibodies (1:100 dilution, batch number AN-04, Alomone Labs, Jerusalem, Israel).

    Techniques: Staining