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    Structured Review

    Alomone Labs dmso
    TRPA1 and TRPM8 are involved in cold-induced vascular response. Vascular responses with cold (4 °C) water treatment in mice pre-treated with combined TRPA1 antagonist <t>A967079</t> (100 mg kg –1 ) and TRPM8 antagonist AMTB (10 mg kg –1 ), or vehicle control (Veh - 10 % <t>DMSO,</t> 10 % Tween in saline) i.p. 30 min before cold treatment. ( a–c ) % change in hindpaw blood flow from baseline to 0–2 min following cold treatment (maximum vasoconstriction) in mice treated with combined antagonist ( a ) A967079+ AMTB, ( b ) A967079, and ( c ) AMTB. ( d-f ) Maximum vasoconstriction caused by cold water treatment in mice treated with combined antagonist ( d ) A967079+ AMTB, ( e ) A967079, and ( f ) AMTB normalised against vehicle treated mice. (n = 5–10) ( g–h ) RT-PCR CT analysis shows fold change of ( g ) Trpa1 and ( h ) Trpm8 normalised to three housekeeping genes in DRG. (n = 14–15) ( i ) Representative western blot of TRPM8 in DRG of young and aged mice and densitometric analysis normalised to Tubulin (Y = young, A = aged) (n = 9). All results are shown as mean ± s.e.m. *p
    Dmso, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 92 stars, based on 27 article reviews
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    1) Product Images from "Dysfunctional TRPM8 signalling in the vascular response to environmental cold in ageing"

    Article Title: Dysfunctional TRPM8 signalling in the vascular response to environmental cold in ageing

    Journal: eLife

    doi: 10.7554/eLife.70153

    TRPA1 and TRPM8 are involved in cold-induced vascular response. Vascular responses with cold (4 °C) water treatment in mice pre-treated with combined TRPA1 antagonist A967079 (100 mg kg –1 ) and TRPM8 antagonist AMTB (10 mg kg –1 ), or vehicle control (Veh - 10 % DMSO, 10 % Tween in saline) i.p. 30 min before cold treatment. ( a–c ) % change in hindpaw blood flow from baseline to 0–2 min following cold treatment (maximum vasoconstriction) in mice treated with combined antagonist ( a ) A967079+ AMTB, ( b ) A967079, and ( c ) AMTB. ( d-f ) Maximum vasoconstriction caused by cold water treatment in mice treated with combined antagonist ( d ) A967079+ AMTB, ( e ) A967079, and ( f ) AMTB normalised against vehicle treated mice. (n = 5–10) ( g–h ) RT-PCR CT analysis shows fold change of ( g ) Trpa1 and ( h ) Trpm8 normalised to three housekeeping genes in DRG. (n = 14–15) ( i ) Representative western blot of TRPM8 in DRG of young and aged mice and densitometric analysis normalised to Tubulin (Y = young, A = aged) (n = 9). All results are shown as mean ± s.e.m. *p
    Figure Legend Snippet: TRPA1 and TRPM8 are involved in cold-induced vascular response. Vascular responses with cold (4 °C) water treatment in mice pre-treated with combined TRPA1 antagonist A967079 (100 mg kg –1 ) and TRPM8 antagonist AMTB (10 mg kg –1 ), or vehicle control (Veh - 10 % DMSO, 10 % Tween in saline) i.p. 30 min before cold treatment. ( a–c ) % change in hindpaw blood flow from baseline to 0–2 min following cold treatment (maximum vasoconstriction) in mice treated with combined antagonist ( a ) A967079+ AMTB, ( b ) A967079, and ( c ) AMTB. ( d-f ) Maximum vasoconstriction caused by cold water treatment in mice treated with combined antagonist ( d ) A967079+ AMTB, ( e ) A967079, and ( f ) AMTB normalised against vehicle treated mice. (n = 5–10) ( g–h ) RT-PCR CT analysis shows fold change of ( g ) Trpa1 and ( h ) Trpm8 normalised to three housekeeping genes in DRG. (n = 14–15) ( i ) Representative western blot of TRPM8 in DRG of young and aged mice and densitometric analysis normalised to Tubulin (Y = young, A = aged) (n = 9). All results are shown as mean ± s.e.m. *p

    Techniques Used: Mouse Assay, Reverse Transcription Polymerase Chain Reaction, Western Blot

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    Alomone Labs dmso
    TRPA1 and TRPM8 are involved in cold-induced vascular response. Vascular responses with cold (4 °C) water treatment in mice pre-treated with combined TRPA1 antagonist <t>A967079</t> (100 mg kg –1 ) and TRPM8 antagonist AMTB (10 mg kg –1 ), or vehicle control (Veh - 10 % <t>DMSO,</t> 10 % Tween in saline) i.p. 30 min before cold treatment. ( a–c ) % change in hindpaw blood flow from baseline to 0–2 min following cold treatment (maximum vasoconstriction) in mice treated with combined antagonist ( a ) A967079+ AMTB, ( b ) A967079, and ( c ) AMTB. ( d-f ) Maximum vasoconstriction caused by cold water treatment in mice treated with combined antagonist ( d ) A967079+ AMTB, ( e ) A967079, and ( f ) AMTB normalised against vehicle treated mice. (n = 5–10) ( g–h ) RT-PCR CT analysis shows fold change of ( g ) Trpa1 and ( h ) Trpm8 normalised to three housekeeping genes in DRG. (n = 14–15) ( i ) Representative western blot of TRPM8 in DRG of young and aged mice and densitometric analysis normalised to Tubulin (Y = young, A = aged) (n = 9). All results are shown as mean ± s.e.m. *p
    Dmso, 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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    93
    Alomone Labs k252a
    A–C . Conventional protein kinase C isoforms (PKCα,β,γ) effectively phosphorylate p75NTR and this phosphorylation is abolished by the kinase inhibitor <t>K252a.</t> A . Human p75NTR is phosphorylated in vitro by several kinases,
    K252a, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TRPA1 and TRPM8 are involved in cold-induced vascular response. Vascular responses with cold (4 °C) water treatment in mice pre-treated with combined TRPA1 antagonist A967079 (100 mg kg –1 ) and TRPM8 antagonist AMTB (10 mg kg –1 ), or vehicle control (Veh - 10 % DMSO, 10 % Tween in saline) i.p. 30 min before cold treatment. ( a–c ) % change in hindpaw blood flow from baseline to 0–2 min following cold treatment (maximum vasoconstriction) in mice treated with combined antagonist ( a ) A967079+ AMTB, ( b ) A967079, and ( c ) AMTB. ( d-f ) Maximum vasoconstriction caused by cold water treatment in mice treated with combined antagonist ( d ) A967079+ AMTB, ( e ) A967079, and ( f ) AMTB normalised against vehicle treated mice. (n = 5–10) ( g–h ) RT-PCR CT analysis shows fold change of ( g ) Trpa1 and ( h ) Trpm8 normalised to three housekeeping genes in DRG. (n = 14–15) ( i ) Representative western blot of TRPM8 in DRG of young and aged mice and densitometric analysis normalised to Tubulin (Y = young, A = aged) (n = 9). All results are shown as mean ± s.e.m. *p

    Journal: eLife

    Article Title: Dysfunctional TRPM8 signalling in the vascular response to environmental cold in ageing

    doi: 10.7554/eLife.70153

    Figure Lengend Snippet: TRPA1 and TRPM8 are involved in cold-induced vascular response. Vascular responses with cold (4 °C) water treatment in mice pre-treated with combined TRPA1 antagonist A967079 (100 mg kg –1 ) and TRPM8 antagonist AMTB (10 mg kg –1 ), or vehicle control (Veh - 10 % DMSO, 10 % Tween in saline) i.p. 30 min before cold treatment. ( a–c ) % change in hindpaw blood flow from baseline to 0–2 min following cold treatment (maximum vasoconstriction) in mice treated with combined antagonist ( a ) A967079+ AMTB, ( b ) A967079, and ( c ) AMTB. ( d-f ) Maximum vasoconstriction caused by cold water treatment in mice treated with combined antagonist ( d ) A967079+ AMTB, ( e ) A967079, and ( f ) AMTB normalised against vehicle treated mice. (n = 5–10) ( g–h ) RT-PCR CT analysis shows fold change of ( g ) Trpa1 and ( h ) Trpm8 normalised to three housekeeping genes in DRG. (n = 14–15) ( i ) Representative western blot of TRPM8 in DRG of young and aged mice and densitometric analysis normalised to Tubulin (Y = young, A = aged) (n = 9). All results are shown as mean ± s.e.m. *p

    Article Snippet: The TRPA1 antagonist A967079 ((1E,3E)–1-(4-Fluorophenyl)–2-methyl-1-pentene-3-one oxime); (Alomone Labs, # A-225) was dissolved in 10 % DMSO (Dimethyl sulfoxide) with 10 % Tween-80 in saline.

    Techniques: Mouse Assay, Reverse Transcription Polymerase Chain Reaction, Western Blot

    A–C . Conventional protein kinase C isoforms (PKCα,β,γ) effectively phosphorylate p75NTR and this phosphorylation is abolished by the kinase inhibitor K252a. A . Human p75NTR is phosphorylated in vitro by several kinases,

    Journal:

    Article Title: Fates of Neurotrophins after Retrograde Axonal Transport: Phosphorylation of p75NTR Is a Sorting Signal for Delayed Degradation

    doi: 10.1523/JNEUROSCI.2512-09.2009

    Figure Lengend Snippet: A–C . Conventional protein kinase C isoforms (PKCα,β,γ) effectively phosphorylate p75NTR and this phosphorylation is abolished by the kinase inhibitor K252a. A . Human p75NTR is phosphorylated in vitro by several kinases,

    Article Snippet: Embryos at ages E13-14 received intraocular injections of NGF alone (1 µg in PBS), NGF (1 µg) plus Gö6976 (1 µl of 250 µM in DMSO), Gö6976 alone (1 µl of 250 µM in DMSO), K252a alone (1 µl of 250 µM in DMSO), or NGF (1 µg in PBS) plus K252a (1 µl of 250 µM in DMSO), and were allowed to survive for 24 hrs.

    Techniques: In Vitro

    A – D , Effect of K252a and trkC activity on the distribution of internalized neurotrophins in retinal ganglion cells ( RGC ) ( A – C ) and SDS-PAGE analysis of internalized neurotrophins in purified RGCs ( D ). A , Labeling densities of internalized BDNF and NT-3 in the Golgi system of RGCs with and without K252a. The analysis was done in triplicate; significance was determined by unpaired t test. B , Labeling densities of internalized BDNF and NT-3 in lysosomes and endosomes of RGCs with and without K252a. The analysis was done in triplicate; significance was determined by unpaired t test. C , Quantification of anterograde transport of 50–80 ng radiolabeled NGF when coinjected in the eye with 50–60 ng cold NT-3 or BDNF. The number of experiments is indicated. Significance was determined by unpaired t test. Error bars indicate SEM. D , SDS-PAGE (15%) of internalized neurotrophins NGF, BDNF, and NT-3 recovered from purified immunopanned RGCs after 10 hr. Each sample was run with an adjacent sample of native same factor ( Na ). The molecular weight is indicated. Arrow indicates the dye front. Note that much of the BDNF recovered from RGCs is cleaved, whereas virtually all the NGF and NT-3 is intact protein by this analysis.

    Journal: The Journal of Neuroscience

    Article Title: Sorting of Internalized Neurotrophins into an Endocytic Transcytosis Pathway via the Golgi System: Ultrastructural Analysis in Retinal Ganglion Cells

    doi: 10.1523/JNEUROSCI.21-22-08915.2001

    Figure Lengend Snippet: A – D , Effect of K252a and trkC activity on the distribution of internalized neurotrophins in retinal ganglion cells ( RGC ) ( A – C ) and SDS-PAGE analysis of internalized neurotrophins in purified RGCs ( D ). A , Labeling densities of internalized BDNF and NT-3 in the Golgi system of RGCs with and without K252a. The analysis was done in triplicate; significance was determined by unpaired t test. B , Labeling densities of internalized BDNF and NT-3 in lysosomes and endosomes of RGCs with and without K252a. The analysis was done in triplicate; significance was determined by unpaired t test. C , Quantification of anterograde transport of 50–80 ng radiolabeled NGF when coinjected in the eye with 50–60 ng cold NT-3 or BDNF. The number of experiments is indicated. Significance was determined by unpaired t test. Error bars indicate SEM. D , SDS-PAGE (15%) of internalized neurotrophins NGF, BDNF, and NT-3 recovered from purified immunopanned RGCs after 10 hr. Each sample was run with an adjacent sample of native same factor ( Na ). The molecular weight is indicated. Arrow indicates the dye front. Note that much of the BDNF recovered from RGCs is cleaved, whereas virtually all the NGF and NT-3 is intact protein by this analysis.

    Article Snippet: Because coinjection of K252a (but not DMSO vehicle alone) substantially reduced the anterograde transport of exogenous NT-3 (Fig. B ), but not its internalization (Fig. ), we tested the hypothesis that blockade of trk activity may alter the pattern of NT-3 accumulation and specifically that K252a may reduce the accumulation of NT-3 in the Golgi system, which is known to be required for anterograde axonal transport of newly synthesized proteins ( ).

    Techniques: Activity Assay, SDS Page, Purification, Labeling, Molecular Weight

    Internalization of 125 I-NT-3 (10–20 ng/ml) in purified retinal ganglion cells from E18–21 chick embryos does not require tyrosine kinase activity. The amount of internalization in the presence of 1 μg/ml K252a (tyrosine kinase inhibitor) is plotted as the percentage relative to the values for vehicle (1 μg/ml DMSO), which were averaged to 100% internalization (∼40,000 cpm per plate). Nonspecific association of NT-3 (at 4°C) is indicated ( dotted line ). Error bars indicate SEM. The number of independent experiments (each in duplicate) is indicated. The p level for confidence ( t test) is indicated, showing no significant effect of K252a on NT-3 internalization.

    Journal: The Journal of Neuroscience

    Article Title: Sorting of Internalized Neurotrophins into an Endocytic Transcytosis Pathway via the Golgi System: Ultrastructural Analysis in Retinal Ganglion Cells

    doi: 10.1523/JNEUROSCI.21-22-08915.2001

    Figure Lengend Snippet: Internalization of 125 I-NT-3 (10–20 ng/ml) in purified retinal ganglion cells from E18–21 chick embryos does not require tyrosine kinase activity. The amount of internalization in the presence of 1 μg/ml K252a (tyrosine kinase inhibitor) is plotted as the percentage relative to the values for vehicle (1 μg/ml DMSO), which were averaged to 100% internalization (∼40,000 cpm per plate). Nonspecific association of NT-3 (at 4°C) is indicated ( dotted line ). Error bars indicate SEM. The number of independent experiments (each in duplicate) is indicated. The p level for confidence ( t test) is indicated, showing no significant effect of K252a on NT-3 internalization.

    Article Snippet: Because coinjection of K252a (but not DMSO vehicle alone) substantially reduced the anterograde transport of exogenous NT-3 (Fig. B ), but not its internalization (Fig. ), we tested the hypothesis that blockade of trk activity may alter the pattern of NT-3 accumulation and specifically that K252a may reduce the accumulation of NT-3 in the Golgi system, which is known to be required for anterograde axonal transport of newly synthesized proteins ( ).

    Techniques: Purification, Activity Assay

    Diagram summarizing proposed subcellular pathways of internalized NT-3 ( black dots ) in a retinal ganglion cell. At least two pathways of internalized NT-3 can be distinguished. A lysosomal pathway of NT-3 may be common to all neurotrophins and may involve binding to the p75 receptor ( U ) or binding of NT-3 to trkC receptor ( Y ) in the presence of the tyrosine kinase inhibitor K252a. The neurotrophin is degraded in lysosomes ( LYS ). Alternatively, a novel pathway of NT-3 internalized in endosomes fuses with membranes of the Golgi apparatus: Golgi Pathway . This sorting requires tyrosine kinase activity (presumably trkC , Y ), and this pathway may join that of newly synthesized neurotrophins as well as p75 receptor ( U ) from the endoplasmic reticulum ( ER ). After passage through the Golgi system, internalized NT-3 is packaged in presumptive large dense-core vesicles ( LDCV ) for anterograde axonal transport. In this pathway, internalized NT-3 binds preferentially to p75. Anterogradely transported NT-3 is released from RGC axon terminals in the tectum, and after release it binds predominantly to trkC in tectal cells where it accumulates in multivesicular bodies ( MVB ).

    Journal: The Journal of Neuroscience

    Article Title: Sorting of Internalized Neurotrophins into an Endocytic Transcytosis Pathway via the Golgi System: Ultrastructural Analysis in Retinal Ganglion Cells

    doi: 10.1523/JNEUROSCI.21-22-08915.2001

    Figure Lengend Snippet: Diagram summarizing proposed subcellular pathways of internalized NT-3 ( black dots ) in a retinal ganglion cell. At least two pathways of internalized NT-3 can be distinguished. A lysosomal pathway of NT-3 may be common to all neurotrophins and may involve binding to the p75 receptor ( U ) or binding of NT-3 to trkC receptor ( Y ) in the presence of the tyrosine kinase inhibitor K252a. The neurotrophin is degraded in lysosomes ( LYS ). Alternatively, a novel pathway of NT-3 internalized in endosomes fuses with membranes of the Golgi apparatus: Golgi Pathway . This sorting requires tyrosine kinase activity (presumably trkC , Y ), and this pathway may join that of newly synthesized neurotrophins as well as p75 receptor ( U ) from the endoplasmic reticulum ( ER ). After passage through the Golgi system, internalized NT-3 is packaged in presumptive large dense-core vesicles ( LDCV ) for anterograde axonal transport. In this pathway, internalized NT-3 binds preferentially to p75. Anterogradely transported NT-3 is released from RGC axon terminals in the tectum, and after release it binds predominantly to trkC in tectal cells where it accumulates in multivesicular bodies ( MVB ).

    Article Snippet: Because coinjection of K252a (but not DMSO vehicle alone) substantially reduced the anterograde transport of exogenous NT-3 (Fig. B ), but not its internalization (Fig. ), we tested the hypothesis that blockade of trk activity may alter the pattern of NT-3 accumulation and specifically that K252a may reduce the accumulation of NT-3 in the Golgi system, which is known to be required for anterograde axonal transport of newly synthesized proteins ( ).

    Techniques: Binding Assay, Activity Assay, Synthesized

    A – C , Anterograde axonal transport of neurotrophic factors and cytochrome c in chick RGCs. A , B , The relative amount of anterograde transport of radiolabeled NT-3 was plotted by dividing the amount measured by gamma counting in the tectum (counts per minute per specific activity in picograms) by the amount measured in the eye (counts per minute per specific activity in nanograms) at the time chick embryos were killed (20 hr after injection in the eye). A , The effects of coinjection of monensin ( MON ), excess cold NT-3 ( cold NT-3 ), excess cold NGF ( cold NGF ), or excess cold BDNF ( cold BDNF ), blocking p75 antibody ( aP75 ), blocking trkC antibody ( atrkC ), and normal rabbit IgG ( IgG ). B , The effects of coinjection of monensin ( MON ), tyrosine kinase inhibitor K252a ( K252a ), vehicle ( DMSO ), wortmannin ( WOR ), LY294,002 ( LY ), and brefeldin A ( BFA ) are indicated. C , The relative amount of anterograde transport of radiolabeled glial cell line-derived neurotrophic factor ( GDNF ), cardiotrophin-1 ( CT1 ), and cytochrome c ( CytC ) was plotted by dividing the amount measured by gamma counting in the midbrain (picograms) by the amount measured in the eye (nanograms) at the time chick embryos were killed (20 hr after injection in the eye). The effects of coinjection of monensin ( MON ), excess cold GDNF, or CytC, and K252a are indicated. Error bars indicate SEM. The number of independent experiments is indicated. *** p ≤ 0.005; ** p ≤ 0.01; * p ≤ 0.05.

    Journal: The Journal of Neuroscience

    Article Title: Sorting of Internalized Neurotrophins into an Endocytic Transcytosis Pathway via the Golgi System: Ultrastructural Analysis in Retinal Ganglion Cells

    doi: 10.1523/JNEUROSCI.21-22-08915.2001

    Figure Lengend Snippet: A – C , Anterograde axonal transport of neurotrophic factors and cytochrome c in chick RGCs. A , B , The relative amount of anterograde transport of radiolabeled NT-3 was plotted by dividing the amount measured by gamma counting in the tectum (counts per minute per specific activity in picograms) by the amount measured in the eye (counts per minute per specific activity in nanograms) at the time chick embryos were killed (20 hr after injection in the eye). A , The effects of coinjection of monensin ( MON ), excess cold NT-3 ( cold NT-3 ), excess cold NGF ( cold NGF ), or excess cold BDNF ( cold BDNF ), blocking p75 antibody ( aP75 ), blocking trkC antibody ( atrkC ), and normal rabbit IgG ( IgG ). B , The effects of coinjection of monensin ( MON ), tyrosine kinase inhibitor K252a ( K252a ), vehicle ( DMSO ), wortmannin ( WOR ), LY294,002 ( LY ), and brefeldin A ( BFA ) are indicated. C , The relative amount of anterograde transport of radiolabeled glial cell line-derived neurotrophic factor ( GDNF ), cardiotrophin-1 ( CT1 ), and cytochrome c ( CytC ) was plotted by dividing the amount measured by gamma counting in the midbrain (picograms) by the amount measured in the eye (nanograms) at the time chick embryos were killed (20 hr after injection in the eye). The effects of coinjection of monensin ( MON ), excess cold GDNF, or CytC, and K252a are indicated. Error bars indicate SEM. The number of independent experiments is indicated. *** p ≤ 0.005; ** p ≤ 0.01; * p ≤ 0.05.

    Article Snippet: Because coinjection of K252a (but not DMSO vehicle alone) substantially reduced the anterograde transport of exogenous NT-3 (Fig. B ), but not its internalization (Fig. ), we tested the hypothesis that blockade of trk activity may alter the pattern of NT-3 accumulation and specifically that K252a may reduce the accumulation of NT-3 in the Golgi system, which is known to be required for anterograde axonal transport of newly synthesized proteins ( ).

    Techniques: Activity Assay, Injection, Blocking Assay, Derivative Assay