aqp7  (Alomone Labs)


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    Structured Review

    Alomone Labs aqp7
    Relative contributions of <t>AQP7</t> and AQP3 to glycerol permeability in plasma membrane vesicles from UDCs, CTL-DCs and LPS-DCs. Ki values were determined by stopped-flow light scattering analysis of plasma membrane vesicles prepared from UDCs, untreated DCs (CTL) and LPS-treated DCs (LPS) in the absence or presence of 0.3 mM HgCl 2 or 1.0 mM CuSO 4 as described in Materials and Methods. The results are the mean ± S.E.M. of the Ki values from 7 to 12 independent vesicles preparations. Data were analyzed using One-way ANOVA and Bonferroni post-hoc t -test. For HgCl 2 : °° p
    Aqp7, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 91/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/aqp7/product/Alomone Labs
    Average 91 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    aqp7 - by Bioz Stars, 2022-09
    91/100 stars

    Images

    1) Product Images from "Lipopolysaccharide Modifies Glycerol Permeability and Metabolism in 3T3-L1 Adipocytes"

    Article Title: Lipopolysaccharide Modifies Glycerol Permeability and Metabolism in 3T3-L1 Adipocytes

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms18122566

    Relative contributions of AQP7 and AQP3 to glycerol permeability in plasma membrane vesicles from UDCs, CTL-DCs and LPS-DCs. Ki values were determined by stopped-flow light scattering analysis of plasma membrane vesicles prepared from UDCs, untreated DCs (CTL) and LPS-treated DCs (LPS) in the absence or presence of 0.3 mM HgCl 2 or 1.0 mM CuSO 4 as described in Materials and Methods. The results are the mean ± S.E.M. of the Ki values from 7 to 12 independent vesicles preparations. Data were analyzed using One-way ANOVA and Bonferroni post-hoc t -test. For HgCl 2 : °° p
    Figure Legend Snippet: Relative contributions of AQP7 and AQP3 to glycerol permeability in plasma membrane vesicles from UDCs, CTL-DCs and LPS-DCs. Ki values were determined by stopped-flow light scattering analysis of plasma membrane vesicles prepared from UDCs, untreated DCs (CTL) and LPS-treated DCs (LPS) in the absence or presence of 0.3 mM HgCl 2 or 1.0 mM CuSO 4 as described in Materials and Methods. The results are the mean ± S.E.M. of the Ki values from 7 to 12 independent vesicles preparations. Data were analyzed using One-way ANOVA and Bonferroni post-hoc t -test. For HgCl 2 : °° p

    Techniques Used: Permeability

    Model for the role of aquaglyceroporins in the regulation of lipogenesis and lipolysis in mouse adipocytes. ( A ) Lipogenesis: insulin is secreted in response to an increase of glycaemia consecutive to feeding. Glucose metabolites, glycerol-3 phosphate (G-3-P) and free fatty acids are used to produce TAGs that will be stored. Both AQP3 and AQP7 are internalized. AQP9 is constitutively expressed at the plasma membrane; ( B ) Lipolysis: upon glucagon secretion in response to fasting or cAMP-mediated response (exercise, catecholamine secretion), TAGs are hydrolyzed to glycerol and free fatty acids, both AQP7 and AQP3 traffic to the plasma membrane enabling increased glycerol efflux. AQP9 may also participate to glycerol efflux during lipolysis. Arrows inside AQP channels represent the direction of glycerol flow; ( C ) Under inflammatory conditions mimicking obesity, LPS is hypothesized to induce AQP3 and AQP9 internalization, thereby reducing plasma membrane glycerol permeability and intracellular TAGs accumulation. Abbreviations: TAGs, triacylglycerols; G-3-P, glycerol-3-phosphate; FFA, free fatty acids; H, catecholamine or glucagon; AC, adenylyl cyclase; ATP, adenosine triphosphate; cAMP, cyclic adenosine monophosphate; PKA, protein kinase A; HSL, hormone sensitive lipase; LPS, lipopolysaccharide; TLR4, Toll-like receptor 4; AQP, aquaporin.
    Figure Legend Snippet: Model for the role of aquaglyceroporins in the regulation of lipogenesis and lipolysis in mouse adipocytes. ( A ) Lipogenesis: insulin is secreted in response to an increase of glycaemia consecutive to feeding. Glucose metabolites, glycerol-3 phosphate (G-3-P) and free fatty acids are used to produce TAGs that will be stored. Both AQP3 and AQP7 are internalized. AQP9 is constitutively expressed at the plasma membrane; ( B ) Lipolysis: upon glucagon secretion in response to fasting or cAMP-mediated response (exercise, catecholamine secretion), TAGs are hydrolyzed to glycerol and free fatty acids, both AQP7 and AQP3 traffic to the plasma membrane enabling increased glycerol efflux. AQP9 may also participate to glycerol efflux during lipolysis. Arrows inside AQP channels represent the direction of glycerol flow; ( C ) Under inflammatory conditions mimicking obesity, LPS is hypothesized to induce AQP3 and AQP9 internalization, thereby reducing plasma membrane glycerol permeability and intracellular TAGs accumulation. Abbreviations: TAGs, triacylglycerols; G-3-P, glycerol-3-phosphate; FFA, free fatty acids; H, catecholamine or glucagon; AC, adenylyl cyclase; ATP, adenosine triphosphate; cAMP, cyclic adenosine monophosphate; PKA, protein kinase A; HSL, hormone sensitive lipase; LPS, lipopolysaccharide; TLR4, Toll-like receptor 4; AQP, aquaporin.

    Techniques Used: Permeability

    AQP3, AQP7 and AQP9 protein expression in UDCs, CTL-DCs and LPS-DCs. AQP3, AQP7 and AQP9 protein expression levels were determined in UDCs, untreated DCs (CTL-DCs) or LPS-treated DCs (1 μg LPS/mL) by Western blotting analysis. ( A ) AQP7 (30 kDa), AQP3 (30 kDa), AQP9 (30 kDa) and β-actin (42 kDa) were detected using specific antibodies as described in Materials and Methods. Western blot was representative of 3 independent experiments; ( B ) The relative expression of each AQP was determined by densitometry analysis of the Western blots as described in Materials and Methods. Ratio between AQP band volume and β-actin band volume were calculated, the relative expression of each AQP in LPS-DCs is expressed in fold of the ratio calculated for CTL-DCs (set to 1) and is the mean ± standard error of the mean (S.E.M.) of 3 independents experiments. Statistical analysis was performed using the t -test for the unique sample.
    Figure Legend Snippet: AQP3, AQP7 and AQP9 protein expression in UDCs, CTL-DCs and LPS-DCs. AQP3, AQP7 and AQP9 protein expression levels were determined in UDCs, untreated DCs (CTL-DCs) or LPS-treated DCs (1 μg LPS/mL) by Western blotting analysis. ( A ) AQP7 (30 kDa), AQP3 (30 kDa), AQP9 (30 kDa) and β-actin (42 kDa) were detected using specific antibodies as described in Materials and Methods. Western blot was representative of 3 independent experiments; ( B ) The relative expression of each AQP was determined by densitometry analysis of the Western blots as described in Materials and Methods. Ratio between AQP band volume and β-actin band volume were calculated, the relative expression of each AQP in LPS-DCs is expressed in fold of the ratio calculated for CTL-DCs (set to 1) and is the mean ± standard error of the mean (S.E.M.) of 3 independents experiments. Statistical analysis was performed using the t -test for the unique sample.

    Techniques Used: Expressing, Western Blot

    2) Product Images from "Empagliflozin Contributes to Polyuria via Regulation of Sodium Transporters and Water Channels in Diabetic Rat Kidneys"

    Article Title: Empagliflozin Contributes to Polyuria via Regulation of Sodium Transporters and Water Channels in Diabetic Rat Kidneys

    Journal: Frontiers in Physiology

    doi: 10.3389/fphys.2019.00271

    Empagliflozin causes no significant changes to AQP3 and AQP1 but tends to increase AQP7 level in diabetic rat kidneys. (A) Representative renal sections immunostained with anti-AQP3. (B) Quantitative analysis of results for AQP3 shows no significant change among groups. Magnification, ×200. (C) Representative immunoblot reacting with anti-NCC, anti-α-ENaC and anti- γ-ENaC. (D) Densitometric analysis shows that the expression of AQP3 protein significantly increased in all OLETF rats. Lixisenatide treatment further increased the expression of AQP3. ∗ P
    Figure Legend Snippet: Empagliflozin causes no significant changes to AQP3 and AQP1 but tends to increase AQP7 level in diabetic rat kidneys. (A) Representative renal sections immunostained with anti-AQP3. (B) Quantitative analysis of results for AQP3 shows no significant change among groups. Magnification, ×200. (C) Representative immunoblot reacting with anti-NCC, anti-α-ENaC and anti- γ-ENaC. (D) Densitometric analysis shows that the expression of AQP3 protein significantly increased in all OLETF rats. Lixisenatide treatment further increased the expression of AQP3. ∗ P

    Techniques Used: Expressing

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    Alomone Labs aqp7
    Relative contributions of <t>AQP7</t> and AQP3 to glycerol permeability in plasma membrane vesicles from UDCs, CTL-DCs and LPS-DCs. Ki values were determined by stopped-flow light scattering analysis of plasma membrane vesicles prepared from UDCs, untreated DCs (CTL) and LPS-treated DCs (LPS) in the absence or presence of 0.3 mM HgCl 2 or 1.0 mM CuSO 4 as described in Materials and Methods. The results are the mean ± S.E.M. of the Ki values from 7 to 12 independent vesicles preparations. Data were analyzed using One-way ANOVA and Bonferroni post-hoc t -test. For HgCl 2 : °° p
    Aqp7, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/aqp7/product/Alomone Labs
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    aqp7 - by Bioz Stars, 2022-09
    91/100 stars
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    Relative contributions of AQP7 and AQP3 to glycerol permeability in plasma membrane vesicles from UDCs, CTL-DCs and LPS-DCs. Ki values were determined by stopped-flow light scattering analysis of plasma membrane vesicles prepared from UDCs, untreated DCs (CTL) and LPS-treated DCs (LPS) in the absence or presence of 0.3 mM HgCl 2 or 1.0 mM CuSO 4 as described in Materials and Methods. The results are the mean ± S.E.M. of the Ki values from 7 to 12 independent vesicles preparations. Data were analyzed using One-way ANOVA and Bonferroni post-hoc t -test. For HgCl 2 : °° p

    Journal: International Journal of Molecular Sciences

    Article Title: Lipopolysaccharide Modifies Glycerol Permeability and Metabolism in 3T3-L1 Adipocytes

    doi: 10.3390/ijms18122566

    Figure Lengend Snippet: Relative contributions of AQP7 and AQP3 to glycerol permeability in plasma membrane vesicles from UDCs, CTL-DCs and LPS-DCs. Ki values were determined by stopped-flow light scattering analysis of plasma membrane vesicles prepared from UDCs, untreated DCs (CTL) and LPS-treated DCs (LPS) in the absence or presence of 0.3 mM HgCl 2 or 1.0 mM CuSO 4 as described in Materials and Methods. The results are the mean ± S.E.M. of the Ki values from 7 to 12 independent vesicles preparations. Data were analyzed using One-way ANOVA and Bonferroni post-hoc t -test. For HgCl 2 : °° p

    Article Snippet: Antibodies directed against AQP7 and AQP9 were purchased from Alomone Labs (Jerusalem, Israel).

    Techniques: Permeability

    Model for the role of aquaglyceroporins in the regulation of lipogenesis and lipolysis in mouse adipocytes. ( A ) Lipogenesis: insulin is secreted in response to an increase of glycaemia consecutive to feeding. Glucose metabolites, glycerol-3 phosphate (G-3-P) and free fatty acids are used to produce TAGs that will be stored. Both AQP3 and AQP7 are internalized. AQP9 is constitutively expressed at the plasma membrane; ( B ) Lipolysis: upon glucagon secretion in response to fasting or cAMP-mediated response (exercise, catecholamine secretion), TAGs are hydrolyzed to glycerol and free fatty acids, both AQP7 and AQP3 traffic to the plasma membrane enabling increased glycerol efflux. AQP9 may also participate to glycerol efflux during lipolysis. Arrows inside AQP channels represent the direction of glycerol flow; ( C ) Under inflammatory conditions mimicking obesity, LPS is hypothesized to induce AQP3 and AQP9 internalization, thereby reducing plasma membrane glycerol permeability and intracellular TAGs accumulation. Abbreviations: TAGs, triacylglycerols; G-3-P, glycerol-3-phosphate; FFA, free fatty acids; H, catecholamine or glucagon; AC, adenylyl cyclase; ATP, adenosine triphosphate; cAMP, cyclic adenosine monophosphate; PKA, protein kinase A; HSL, hormone sensitive lipase; LPS, lipopolysaccharide; TLR4, Toll-like receptor 4; AQP, aquaporin.

    Journal: International Journal of Molecular Sciences

    Article Title: Lipopolysaccharide Modifies Glycerol Permeability and Metabolism in 3T3-L1 Adipocytes

    doi: 10.3390/ijms18122566

    Figure Lengend Snippet: Model for the role of aquaglyceroporins in the regulation of lipogenesis and lipolysis in mouse adipocytes. ( A ) Lipogenesis: insulin is secreted in response to an increase of glycaemia consecutive to feeding. Glucose metabolites, glycerol-3 phosphate (G-3-P) and free fatty acids are used to produce TAGs that will be stored. Both AQP3 and AQP7 are internalized. AQP9 is constitutively expressed at the plasma membrane; ( B ) Lipolysis: upon glucagon secretion in response to fasting or cAMP-mediated response (exercise, catecholamine secretion), TAGs are hydrolyzed to glycerol and free fatty acids, both AQP7 and AQP3 traffic to the plasma membrane enabling increased glycerol efflux. AQP9 may also participate to glycerol efflux during lipolysis. Arrows inside AQP channels represent the direction of glycerol flow; ( C ) Under inflammatory conditions mimicking obesity, LPS is hypothesized to induce AQP3 and AQP9 internalization, thereby reducing plasma membrane glycerol permeability and intracellular TAGs accumulation. Abbreviations: TAGs, triacylglycerols; G-3-P, glycerol-3-phosphate; FFA, free fatty acids; H, catecholamine or glucagon; AC, adenylyl cyclase; ATP, adenosine triphosphate; cAMP, cyclic adenosine monophosphate; PKA, protein kinase A; HSL, hormone sensitive lipase; LPS, lipopolysaccharide; TLR4, Toll-like receptor 4; AQP, aquaporin.

    Article Snippet: Antibodies directed against AQP7 and AQP9 were purchased from Alomone Labs (Jerusalem, Israel).

    Techniques: Permeability

    AQP3, AQP7 and AQP9 protein expression in UDCs, CTL-DCs and LPS-DCs. AQP3, AQP7 and AQP9 protein expression levels were determined in UDCs, untreated DCs (CTL-DCs) or LPS-treated DCs (1 μg LPS/mL) by Western blotting analysis. ( A ) AQP7 (30 kDa), AQP3 (30 kDa), AQP9 (30 kDa) and β-actin (42 kDa) were detected using specific antibodies as described in Materials and Methods. Western blot was representative of 3 independent experiments; ( B ) The relative expression of each AQP was determined by densitometry analysis of the Western blots as described in Materials and Methods. Ratio between AQP band volume and β-actin band volume were calculated, the relative expression of each AQP in LPS-DCs is expressed in fold of the ratio calculated for CTL-DCs (set to 1) and is the mean ± standard error of the mean (S.E.M.) of 3 independents experiments. Statistical analysis was performed using the t -test for the unique sample.

    Journal: International Journal of Molecular Sciences

    Article Title: Lipopolysaccharide Modifies Glycerol Permeability and Metabolism in 3T3-L1 Adipocytes

    doi: 10.3390/ijms18122566

    Figure Lengend Snippet: AQP3, AQP7 and AQP9 protein expression in UDCs, CTL-DCs and LPS-DCs. AQP3, AQP7 and AQP9 protein expression levels were determined in UDCs, untreated DCs (CTL-DCs) or LPS-treated DCs (1 μg LPS/mL) by Western blotting analysis. ( A ) AQP7 (30 kDa), AQP3 (30 kDa), AQP9 (30 kDa) and β-actin (42 kDa) were detected using specific antibodies as described in Materials and Methods. Western blot was representative of 3 independent experiments; ( B ) The relative expression of each AQP was determined by densitometry analysis of the Western blots as described in Materials and Methods. Ratio between AQP band volume and β-actin band volume were calculated, the relative expression of each AQP in LPS-DCs is expressed in fold of the ratio calculated for CTL-DCs (set to 1) and is the mean ± standard error of the mean (S.E.M.) of 3 independents experiments. Statistical analysis was performed using the t -test for the unique sample.

    Article Snippet: Antibodies directed against AQP7 and AQP9 were purchased from Alomone Labs (Jerusalem, Israel).

    Techniques: Expressing, Western Blot

    Empagliflozin causes no significant changes to AQP3 and AQP1 but tends to increase AQP7 level in diabetic rat kidneys. (A) Representative renal sections immunostained with anti-AQP3. (B) Quantitative analysis of results for AQP3 shows no significant change among groups. Magnification, ×200. (C) Representative immunoblot reacting with anti-NCC, anti-α-ENaC and anti- γ-ENaC. (D) Densitometric analysis shows that the expression of AQP3 protein significantly increased in all OLETF rats. Lixisenatide treatment further increased the expression of AQP3. ∗ P

    Journal: Frontiers in Physiology

    Article Title: Empagliflozin Contributes to Polyuria via Regulation of Sodium Transporters and Water Channels in Diabetic Rat Kidneys

    doi: 10.3389/fphys.2019.00271

    Figure Lengend Snippet: Empagliflozin causes no significant changes to AQP3 and AQP1 but tends to increase AQP7 level in diabetic rat kidneys. (A) Representative renal sections immunostained with anti-AQP3. (B) Quantitative analysis of results for AQP3 shows no significant change among groups. Magnification, ×200. (C) Representative immunoblot reacting with anti-NCC, anti-α-ENaC and anti- γ-ENaC. (D) Densitometric analysis shows that the expression of AQP3 protein significantly increased in all OLETF rats. Lixisenatide treatment further increased the expression of AQP3. ∗ P

    Article Snippet: Membranes were incubated with the following primary antibodies: AQP1 (Alomone Labs, Jerusalem, Israel), AQP2 (Alomone Labs), p261-AQP2 (Novus Biologicals, Littleton, CO, United States), AQP3 (Alomone Labs), AQP7 (Alomone Labs), cyclin-dependent kinase 1 (cdk1; Santa Cruz Biotechnology, Inc., Santa Cruz, CA, United States), cdk5 (Santa Cruz Biotechnology, Inc.), Na+/H+ exchanger isoform 3 (NHE3; StressMarq Biosciences Inc., Victoria, BC, Canada), extracellular signal–regulated kinase (ERK; Cell Signaling Technology, Danvers, MA, United States), p-Erk (Cell Signaling Technology), p -glycogen synthase kinase 3α (pGSK3α; Santa Cruz Biotechnology, Inc.), Na+-Cl- cotransporter (NCC; StressMarq Biosciences), NKCC2 (StressMarq Biosciences), phosphatase 1β (PP1β; Santa Cruz Biotechnology, Inc.), PP2B (Santa Cruz Biotechnology, Inc.), vasopressin V2 receptor (V2R; Alomone Labs), α-epithelial Na+ channel (ENaC; StressMarq Biosciences); γ-ENaC (StressMarq Biosciences), p38 mitogen-activated protein kinase (p38; Cell Signaling Technology), p-p38 (Cell Signaling Technology) and β-actin (Sigma-Aldrich, St. Louis, MO, United States).

    Techniques: Expressing