anti glut2 slc2a2 antibody  (Alomone Labs)


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    Alomone Labs anti glut2 slc2a2 antibody
    <t>Glut2</t> expression in GFAP-expressing tanycytes is required for stimulating feeding in response to fasting. ( A ) Body weight (g), ( B ) cumulative meal events (events/24 h), ( C ) cumulative food intake (g/24 h), ( D ) cumulative food intake (g/12 h) in the dark and light phase of feeding and ( E ) cumulative food intake (g/1 h) during the 12 h of the dark phase of feeding in <t>Slc2a2</t> loxP/loxP mice transduced with AAV- Gfap -GFP or AAV- Gfap -Cre-GFP. The parameters were analyzed in basal conditions. ( F ) Experimental approach. ( G ) cumulative meal events (events/24 h), ( H ) food intake (g/1 h), ( I ) cumulative food intake (g/12 h) during the dark and light cycle, ( J ) cumulative food intake (g/1 h) after 24 h of fasting, ( K ) cumulative food intake at 1 h and 6 h of refeeding, ( L ) cumulative food intake (g/1 h), ( M ) feeding rate (mg/min), and ( J ) first meal duration (min) by mice with ad libitum access to food as well as those undergoing a fasting-refeeding period. All the experiments were performed in Slc2a2 loxP/loxP mice transduced for 4-weeks with the viral vector AAV- Gfap -GFP or AAV 5 - Gfap -Cre-GFP. Error bars represent SEM. Comparisons between two groups were performed using a student’s t -test. Multiple comparisons were performed using a two-way ANOVA (Bonferonni’s post-hoc test). n.s not significant.
    Anti Glut2 Slc2a2 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti glut2 slc2a2 antibody/product/Alomone Labs
    Average 94 stars, based on 5 article reviews
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    anti glut2 slc2a2 antibody - by Bioz Stars, 2022-11
    94/100 stars

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    1) Product Images from "GLUT2 expression by glial fibrillary acidic protein-positive tanycytes is required for promoting feeding-response to fasting"

    Article Title: GLUT2 expression by glial fibrillary acidic protein-positive tanycytes is required for promoting feeding-response to fasting

    Journal: Scientific Reports

    doi: 10.1038/s41598-022-22489-2

    Glut2 expression in GFAP-expressing tanycytes is required for stimulating feeding in response to fasting. ( A ) Body weight (g), ( B ) cumulative meal events (events/24 h), ( C ) cumulative food intake (g/24 h), ( D ) cumulative food intake (g/12 h) in the dark and light phase of feeding and ( E ) cumulative food intake (g/1 h) during the 12 h of the dark phase of feeding in Slc2a2 loxP/loxP mice transduced with AAV- Gfap -GFP or AAV- Gfap -Cre-GFP. The parameters were analyzed in basal conditions. ( F ) Experimental approach. ( G ) cumulative meal events (events/24 h), ( H ) food intake (g/1 h), ( I ) cumulative food intake (g/12 h) during the dark and light cycle, ( J ) cumulative food intake (g/1 h) after 24 h of fasting, ( K ) cumulative food intake at 1 h and 6 h of refeeding, ( L ) cumulative food intake (g/1 h), ( M ) feeding rate (mg/min), and ( J ) first meal duration (min) by mice with ad libitum access to food as well as those undergoing a fasting-refeeding period. All the experiments were performed in Slc2a2 loxP/loxP mice transduced for 4-weeks with the viral vector AAV- Gfap -GFP or AAV 5 - Gfap -Cre-GFP. Error bars represent SEM. Comparisons between two groups were performed using a student’s t -test. Multiple comparisons were performed using a two-way ANOVA (Bonferonni’s post-hoc test). n.s not significant.
    Figure Legend Snippet: Glut2 expression in GFAP-expressing tanycytes is required for stimulating feeding in response to fasting. ( A ) Body weight (g), ( B ) cumulative meal events (events/24 h), ( C ) cumulative food intake (g/24 h), ( D ) cumulative food intake (g/12 h) in the dark and light phase of feeding and ( E ) cumulative food intake (g/1 h) during the 12 h of the dark phase of feeding in Slc2a2 loxP/loxP mice transduced with AAV- Gfap -GFP or AAV- Gfap -Cre-GFP. The parameters were analyzed in basal conditions. ( F ) Experimental approach. ( G ) cumulative meal events (events/24 h), ( H ) food intake (g/1 h), ( I ) cumulative food intake (g/12 h) during the dark and light cycle, ( J ) cumulative food intake (g/1 h) after 24 h of fasting, ( K ) cumulative food intake at 1 h and 6 h of refeeding, ( L ) cumulative food intake (g/1 h), ( M ) feeding rate (mg/min), and ( J ) first meal duration (min) by mice with ad libitum access to food as well as those undergoing a fasting-refeeding period. All the experiments were performed in Slc2a2 loxP/loxP mice transduced for 4-weeks with the viral vector AAV- Gfap -GFP or AAV 5 - Gfap -Cre-GFP. Error bars represent SEM. Comparisons between two groups were performed using a student’s t -test. Multiple comparisons were performed using a two-way ANOVA (Bonferonni’s post-hoc test). n.s not significant.

    Techniques Used: Expressing, Mouse Assay, Transduction, Plasmid Preparation

    Loss of regulated Pomc expression in response to Glut2 inactivation during the fasting-to-refeeding transition. ( A ) Experimental approach. Slc2a2 loxP/loxP mice transduced for 6-weeks with the viral vector AAV- Gfap -GFP or AAV- Gfap -Cre-GFP. Total RNA was obtained after 24 h of fasted (grey bars) and 6 h of refed (purpure bars). Analysis of Npy ( B ), Cart ( C ), and Pomc ( D ) mRNA expression using qRT‐PCR. Error bars represent SEM. Multiple comparisons were performed using a two-way ANOVA. n.s not significant.
    Figure Legend Snippet: Loss of regulated Pomc expression in response to Glut2 inactivation during the fasting-to-refeeding transition. ( A ) Experimental approach. Slc2a2 loxP/loxP mice transduced for 6-weeks with the viral vector AAV- Gfap -GFP or AAV- Gfap -Cre-GFP. Total RNA was obtained after 24 h of fasted (grey bars) and 6 h of refed (purpure bars). Analysis of Npy ( B ), Cart ( C ), and Pomc ( D ) mRNA expression using qRT‐PCR. Error bars represent SEM. Multiple comparisons were performed using a two-way ANOVA. n.s not significant.

    Techniques Used: Expressing, Mouse Assay, Plasmid Preparation, Quantitative RT-PCR

    Glut2 gene inactivation in GFAP-expressing tanycytes and its in situ evaluation. ( A ) Experimental approach. Slc2a2 loxP/loxP mice were injected into the 3V with a control viral vector AAV- Gfap -GFP or a viral vector that expresses the CRE recombinase under the control of GFAP promoter (AAV- Gfap -Cre-GFP). ( B ) Structure of the Glut2 floxed construction and genomic PCR of mice injected with AAV- Gfap -GFP (lane 1) or AAV- Gfap -Cre-GFP (lane 2). ( C ) GFP fluorescence (green) in coronal sections (20 µm) of mice transduced for two weeks. DAPI was used as a nuclear marker (magenta). ( D ) GFP fluorescence in GFAP-expressing tanycytes was analyzed through vimentin (purple) and GFAP immunoreactivity (yellow). DAPI was used as a nuclear marker (blue). ( E ) Percentage of GFAP-expressing tanycytes positives for the GFP fluorescence. ( F ) GFP fluorescence in GFAP-expressing tanycytes analyzed through the GFAP immunoreactivity (red). DAPI was used as a nuclear marker (blue). ( G – L ) Percentage of GFAP-expressing tanycytes transduced in the hypothalamic anteroposterior and dorsoventral axis (n = 3 mice). P1 primer 1, P2 primer 2, P3 primer 3, 3V third ventricle, ME median eminence, DMN dorsomedial nucleus, VMN ventromedial nucleus, ARC arcuate nucleus, PVN paraventricular nucleus, DTM dorsal tuberomammillary nucleus.
    Figure Legend Snippet: Glut2 gene inactivation in GFAP-expressing tanycytes and its in situ evaluation. ( A ) Experimental approach. Slc2a2 loxP/loxP mice were injected into the 3V with a control viral vector AAV- Gfap -GFP or a viral vector that expresses the CRE recombinase under the control of GFAP promoter (AAV- Gfap -Cre-GFP). ( B ) Structure of the Glut2 floxed construction and genomic PCR of mice injected with AAV- Gfap -GFP (lane 1) or AAV- Gfap -Cre-GFP (lane 2). ( C ) GFP fluorescence (green) in coronal sections (20 µm) of mice transduced for two weeks. DAPI was used as a nuclear marker (magenta). ( D ) GFP fluorescence in GFAP-expressing tanycytes was analyzed through vimentin (purple) and GFAP immunoreactivity (yellow). DAPI was used as a nuclear marker (blue). ( E ) Percentage of GFAP-expressing tanycytes positives for the GFP fluorescence. ( F ) GFP fluorescence in GFAP-expressing tanycytes analyzed through the GFAP immunoreactivity (red). DAPI was used as a nuclear marker (blue). ( G – L ) Percentage of GFAP-expressing tanycytes transduced in the hypothalamic anteroposterior and dorsoventral axis (n = 3 mice). P1 primer 1, P2 primer 2, P3 primer 3, 3V third ventricle, ME median eminence, DMN dorsomedial nucleus, VMN ventromedial nucleus, ARC arcuate nucleus, PVN paraventricular nucleus, DTM dorsal tuberomammillary nucleus.

    Techniques Used: Expressing, In Situ, Mouse Assay, Injection, Plasmid Preparation, Polymerase Chain Reaction, Fluorescence, Marker

    Glut2 inactivation enhances the ghrelin secretion in fasting. ( A ) Blood glucose concentration (mmol/L), ( B ) plasma insulin concentration (ng/mL) and ( C ) plasma glucagon concentration (pg/mL). ( D ) Mice show a normal i.p GTT (2 g/kg). ( E ) Plasma leptin (ng/mL), ( F ) plasma GLP-1 (pM) and ( G ) plasma total ghrelin (ng/mL) concentrations. All the measurements were performed on mice transduced for 4-weeks with the viral vector AAV- Gfap -GFP (grey bars) or AAV- Gfap -Cre-GFP (purpure bars). Plasma samples were obtained after 24 h of fasting and 6 h of refeeding. ( H ) Ghrelin response. Total food intake (g) was measured 1 h post i.p treatment of mouse acyl-ghrelin (10 µg/kg) or vehicle (NaCl 0.9% w/v). Error bars represent SEM. Multiple comparisons were performed using a two-way ANOVA (Bonferonni’s post-hoc test). n.s not significant.
    Figure Legend Snippet: Glut2 inactivation enhances the ghrelin secretion in fasting. ( A ) Blood glucose concentration (mmol/L), ( B ) plasma insulin concentration (ng/mL) and ( C ) plasma glucagon concentration (pg/mL). ( D ) Mice show a normal i.p GTT (2 g/kg). ( E ) Plasma leptin (ng/mL), ( F ) plasma GLP-1 (pM) and ( G ) plasma total ghrelin (ng/mL) concentrations. All the measurements were performed on mice transduced for 4-weeks with the viral vector AAV- Gfap -GFP (grey bars) or AAV- Gfap -Cre-GFP (purpure bars). Plasma samples were obtained after 24 h of fasting and 6 h of refeeding. ( H ) Ghrelin response. Total food intake (g) was measured 1 h post i.p treatment of mouse acyl-ghrelin (10 µg/kg) or vehicle (NaCl 0.9% w/v). Error bars represent SEM. Multiple comparisons were performed using a two-way ANOVA (Bonferonni’s post-hoc test). n.s not significant.

    Techniques Used: Concentration Assay, Mouse Assay, Plasmid Preparation

    GLUT2 is expressed in hypothalamic tanycytes. Low and high magnification images of tanycytes facing the VMN ( A ) and ARC ( B ) using the anti-GLUT2 (red) and anti-vimentin (green) antibodies. DAPI was used as a nuclear marker. 3V third ventricle, ME median eminence, VMN ventromedial nucleus, ARC arcuate nucleus.
    Figure Legend Snippet: GLUT2 is expressed in hypothalamic tanycytes. Low and high magnification images of tanycytes facing the VMN ( A ) and ARC ( B ) using the anti-GLUT2 (red) and anti-vimentin (green) antibodies. DAPI was used as a nuclear marker. 3V third ventricle, ME median eminence, VMN ventromedial nucleus, ARC arcuate nucleus.

    Techniques Used: Marker

    Glut2 inactivation increases c-Fos expression in the VMN response to fasting. ( A – E ) Representative images and quantification of c-Fos-immunoreactive cells (white) in the hypothalamus of Slc2a2 loxP/loxP mice transduced for 4-weeks with the viral vector AAV- Gfap -GFP (grey bars) or AAV- Gfap -Cre-GFP (purpure bars). Antero-posterior c-Fos quantification was performed from the bregma AP-1.54 mm ( A ) to bregma AP − 2.54 mm ( E ) in 24 h fasted mice. Error bars represent SEM. Multiple comparisons were performed using a two-way ANOVA (Bonferonni’s post-hoc test). DMN Dorsomedial nucleus, VMN ventromedial nucleus, ARC arcuate nucleus, DTM dorsal tuberomammillary nucleus, PVN paraventricular nucleus, 3V third ventricle. n.s not significant.
    Figure Legend Snippet: Glut2 inactivation increases c-Fos expression in the VMN response to fasting. ( A – E ) Representative images and quantification of c-Fos-immunoreactive cells (white) in the hypothalamus of Slc2a2 loxP/loxP mice transduced for 4-weeks with the viral vector AAV- Gfap -GFP (grey bars) or AAV- Gfap -Cre-GFP (purpure bars). Antero-posterior c-Fos quantification was performed from the bregma AP-1.54 mm ( A ) to bregma AP − 2.54 mm ( E ) in 24 h fasted mice. Error bars represent SEM. Multiple comparisons were performed using a two-way ANOVA (Bonferonni’s post-hoc test). DMN Dorsomedial nucleus, VMN ventromedial nucleus, ARC arcuate nucleus, DTM dorsal tuberomammillary nucleus, PVN paraventricular nucleus, 3V third ventricle. n.s not significant.

    Techniques Used: Expressing, Mouse Assay, Plasmid Preparation

    2) Product Images from "Opposite physiological and pathological mTORC1-mediated roles of the CB1 receptor in regulating renal tubular function"

    Article Title: Opposite physiological and pathological mTORC1-mediated roles of the CB1 receptor in regulating renal tubular function

    Journal: Nature Communications

    doi: 10.1038/s41467-022-29124-8

    CB 1 R regulates mTORC1 activation under normoglycemic conditions. a , c Immunoblotting analysis and quantification of pS6 in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 5 mice per group (* P = 0.0166). b , d Immunoblotting analysis and quantification of pAKT in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 4 mice per group (* P = 0.0275). e – g Immunoblotting analysis and quantification of SREBP1c and GLUT2 in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 6 mice per group (* P
    Figure Legend Snippet: CB 1 R regulates mTORC1 activation under normoglycemic conditions. a , c Immunoblotting analysis and quantification of pS6 in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 5 mice per group (* P = 0.0166). b , d Immunoblotting analysis and quantification of pAKT in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 4 mice per group (* P = 0.0275). e – g Immunoblotting analysis and quantification of SREBP1c and GLUT2 in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 6 mice per group (* P

    Techniques Used: Activation Assay, Mouse Assay

    A proposed mechanism by which renal proximal tubule CB 1 R regulates mTORC1 activity in health and disease. In normoglycemia CB 1 R is responsible to maintain mTORC1 normal activation by preventing excess of amino acids uptake (left). In hyperglycemia, CB 1 R-mediated mTORC1 over-activation results in upregulating GLUT2 transcription, consequently enhancing glucose absorption and tubular damage (right).
    Figure Legend Snippet: A proposed mechanism by which renal proximal tubule CB 1 R regulates mTORC1 activity in health and disease. In normoglycemia CB 1 R is responsible to maintain mTORC1 normal activation by preventing excess of amino acids uptake (left). In hyperglycemia, CB 1 R-mediated mTORC1 over-activation results in upregulating GLUT2 transcription, consequently enhancing glucose absorption and tubular damage (right).

    Techniques Used: Activity Assay, Activation Assay

    Genetic reduction of GLUT2 in RPTCs protects mice from developing DKD. All the following measurements were done in Akita diabetic mice and their littermate WT controls with or without reduced expression of GLUT2 in RPTCs: a Body weight surveillance for a period of 16 weeks. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− . b Blood glucose surveillance for a period of 16 weeks. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− . c Serum glucose. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− (* P
    Figure Legend Snippet: Genetic reduction of GLUT2 in RPTCs protects mice from developing DKD. All the following measurements were done in Akita diabetic mice and their littermate WT controls with or without reduced expression of GLUT2 in RPTCs: a Body weight surveillance for a period of 16 weeks. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− . b Blood glucose surveillance for a period of 16 weeks. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− . c Serum glucose. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− (* P

    Techniques Used: Mouse Assay, Expressing

    RPTC CB 1 R regulates mTORC1 and GLUT2. a , d Immunoblotting analysis and quantification of pS6 (S235/236) in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 4 mice for Akita-RPTC CB1R+/+ , n = 5 mice for Akita-RPTC CB1R−/− (* P = 0.0032). b , e Immunoblotting analysis and quantification of pAKT (S473) in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 4 mice for Akita-RPTC CB1R+/+ , n = 5 mice for Akita-RPTC CB1R−/− (* P = 0.0056). c , f Immunoblotting analysis and quantification of GLUT2 in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 5 mice per group (* P
    Figure Legend Snippet: RPTC CB 1 R regulates mTORC1 and GLUT2. a , d Immunoblotting analysis and quantification of pS6 (S235/236) in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 4 mice for Akita-RPTC CB1R+/+ , n = 5 mice for Akita-RPTC CB1R−/− (* P = 0.0032). b , e Immunoblotting analysis and quantification of pAKT (S473) in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 4 mice for Akita-RPTC CB1R+/+ , n = 5 mice for Akita-RPTC CB1R−/− (* P = 0.0056). c , f Immunoblotting analysis and quantification of GLUT2 in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 5 mice per group (* P

    Techniques Used: Mouse Assay

    GLUT2 transcription is directly regulated by CB 1 R and mTORC1. a – e Luminescence relative response ratio (RRR) analyses of HEK293 cells co-transfected transiently with pGL3-GLUT and Renilla luciferase plasmids (T2) or with pGL3-GLUT, Renilla luciferase, and CB 1 R-TK-d64 plasmids (T3), treated with or without ACEA (10 μM; b , c ) or with HG (30 mM; a , d , e ) for 3 h, in the presence or absence of JD5037 (100 nM) or rapamycin (100 nM). For a , n = 6 for T2, n = 8 for T2+HG (* P = 0.0034). For b , n = 16 per group (* P
    Figure Legend Snippet: GLUT2 transcription is directly regulated by CB 1 R and mTORC1. a – e Luminescence relative response ratio (RRR) analyses of HEK293 cells co-transfected transiently with pGL3-GLUT and Renilla luciferase plasmids (T2) or with pGL3-GLUT, Renilla luciferase, and CB 1 R-TK-d64 plasmids (T3), treated with or without ACEA (10 μM; b , c ) or with HG (30 mM; a , d , e ) for 3 h, in the presence or absence of JD5037 (100 nM) or rapamycin (100 nM). For a , n = 6 for T2, n = 8 for T2+HG (* P = 0.0034). For b , n = 16 per group (* P

    Techniques Used: Transfection, Luciferase

    3) Product Images from "Opposite physiological and pathological mTORC1-mediated roles of the CB1 receptor in regulating renal tubular function"

    Article Title: Opposite physiological and pathological mTORC1-mediated roles of the CB1 receptor in regulating renal tubular function

    Journal: Nature Communications

    doi: 10.1038/s41467-022-29124-8

    CB 1 R regulates mTORC1 activation under normoglycemic conditions. a , c Immunoblotting analysis and quantification of pS6 in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 5 mice per group (* P = 0.0166). b , d Immunoblotting analysis and quantification of pAKT in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 4 mice per group (* P = 0.0275). e – g Immunoblotting analysis and quantification of SREBP1c and GLUT2 in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 6 mice per group (* P
    Figure Legend Snippet: CB 1 R regulates mTORC1 activation under normoglycemic conditions. a , c Immunoblotting analysis and quantification of pS6 in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 5 mice per group (* P = 0.0166). b , d Immunoblotting analysis and quantification of pAKT in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 4 mice per group (* P = 0.0275). e – g Immunoblotting analysis and quantification of SREBP1c and GLUT2 in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 6 mice per group (* P

    Techniques Used: Activation Assay, Mouse Assay

    A proposed mechanism by which renal proximal tubule CB 1 R regulates mTORC1 activity in health and disease. In normoglycemia CB 1 R is responsible to maintain mTORC1 normal activation by preventing excess of amino acids uptake (left). In hyperglycemia, CB 1 R-mediated mTORC1 over-activation results in upregulating GLUT2 transcription, consequently enhancing glucose absorption and tubular damage (right).
    Figure Legend Snippet: A proposed mechanism by which renal proximal tubule CB 1 R regulates mTORC1 activity in health and disease. In normoglycemia CB 1 R is responsible to maintain mTORC1 normal activation by preventing excess of amino acids uptake (left). In hyperglycemia, CB 1 R-mediated mTORC1 over-activation results in upregulating GLUT2 transcription, consequently enhancing glucose absorption and tubular damage (right).

    Techniques Used: Activity Assay, Activation Assay

    Genetic reduction of GLUT2 in RPTCs protects mice from developing DKD. All the following measurements were done in Akita diabetic mice and their littermate WT controls with or without reduced expression of GLUT2 in RPTCs: a Body weight surveillance for a period of 16 weeks. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− . b Blood glucose surveillance for a period of 16 weeks. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− . c Serum glucose. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− (* P
    Figure Legend Snippet: Genetic reduction of GLUT2 in RPTCs protects mice from developing DKD. All the following measurements were done in Akita diabetic mice and their littermate WT controls with or without reduced expression of GLUT2 in RPTCs: a Body weight surveillance for a period of 16 weeks. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− . b Blood glucose surveillance for a period of 16 weeks. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− . c Serum glucose. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− (* P

    Techniques Used: Mouse Assay, Expressing

    RPTC CB 1 R regulates mTORC1 and GLUT2. a , d Immunoblotting analysis and quantification of pS6 (S235/236) in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 4 mice for Akita-RPTC CB1R+/+ , n = 5 mice for Akita-RPTC CB1R−/− (* P = 0.0032). b , e Immunoblotting analysis and quantification of pAKT (S473) in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 4 mice for Akita-RPTC CB1R+/+ , n = 5 mice for Akita-RPTC CB1R−/− (* P = 0.0056). c , f Immunoblotting analysis and quantification of GLUT2 in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 5 mice per group (* P
    Figure Legend Snippet: RPTC CB 1 R regulates mTORC1 and GLUT2. a , d Immunoblotting analysis and quantification of pS6 (S235/236) in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 4 mice for Akita-RPTC CB1R+/+ , n = 5 mice for Akita-RPTC CB1R−/− (* P = 0.0032). b , e Immunoblotting analysis and quantification of pAKT (S473) in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 4 mice for Akita-RPTC CB1R+/+ , n = 5 mice for Akita-RPTC CB1R−/− (* P = 0.0056). c , f Immunoblotting analysis and quantification of GLUT2 in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 5 mice per group (* P

    Techniques Used: Mouse Assay

    GLUT2 transcription is directly regulated by CB 1 R and mTORC1. a – e Luminescence relative response ratio (RRR) analyses of HEK293 cells co-transfected transiently with pGL3-GLUT and Renilla luciferase plasmids (T2) or with pGL3-GLUT, Renilla luciferase, and CB 1 R-TK-d64 plasmids (T3), treated with or without ACEA (10 μM; b , c ) or with HG (30 mM; a , d , e ) for 3 h, in the presence or absence of JD5037 (100 nM) or rapamycin (100 nM). For a , n = 6 for T2, n = 8 for T2+HG (* P = 0.0034). For b , n = 16 per group (* P
    Figure Legend Snippet: GLUT2 transcription is directly regulated by CB 1 R and mTORC1. a – e Luminescence relative response ratio (RRR) analyses of HEK293 cells co-transfected transiently with pGL3-GLUT and Renilla luciferase plasmids (T2) or with pGL3-GLUT, Renilla luciferase, and CB 1 R-TK-d64 plasmids (T3), treated with or without ACEA (10 μM; b , c ) or with HG (30 mM; a , d , e ) for 3 h, in the presence or absence of JD5037 (100 nM) or rapamycin (100 nM). For a , n = 6 for T2, n = 8 for T2+HG (* P = 0.0034). For b , n = 16 per group (* P

    Techniques Used: Transfection, Luciferase

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    Alomone Labs anti glut2 slc2a2 antibody
    <t>Glut2</t> expression in GFAP-expressing tanycytes is required for stimulating feeding in response to fasting. ( A ) Body weight (g), ( B ) cumulative meal events (events/24 h), ( C ) cumulative food intake (g/24 h), ( D ) cumulative food intake (g/12 h) in the dark and light phase of feeding and ( E ) cumulative food intake (g/1 h) during the 12 h of the dark phase of feeding in <t>Slc2a2</t> loxP/loxP mice transduced with AAV- Gfap -GFP or AAV- Gfap -Cre-GFP. The parameters were analyzed in basal conditions. ( F ) Experimental approach. ( G ) cumulative meal events (events/24 h), ( H ) food intake (g/1 h), ( I ) cumulative food intake (g/12 h) during the dark and light cycle, ( J ) cumulative food intake (g/1 h) after 24 h of fasting, ( K ) cumulative food intake at 1 h and 6 h of refeeding, ( L ) cumulative food intake (g/1 h), ( M ) feeding rate (mg/min), and ( J ) first meal duration (min) by mice with ad libitum access to food as well as those undergoing a fasting-refeeding period. All the experiments were performed in Slc2a2 loxP/loxP mice transduced for 4-weeks with the viral vector AAV- Gfap -GFP or AAV 5 - Gfap -Cre-GFP. Error bars represent SEM. Comparisons between two groups were performed using a student’s t -test. Multiple comparisons were performed using a two-way ANOVA (Bonferonni’s post-hoc test). n.s not significant.
    Anti Glut2 Slc2a2 Antibody, 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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    Glut2 expression in GFAP-expressing tanycytes is required for stimulating feeding in response to fasting. ( A ) Body weight (g), ( B ) cumulative meal events (events/24 h), ( C ) cumulative food intake (g/24 h), ( D ) cumulative food intake (g/12 h) in the dark and light phase of feeding and ( E ) cumulative food intake (g/1 h) during the 12 h of the dark phase of feeding in Slc2a2 loxP/loxP mice transduced with AAV- Gfap -GFP or AAV- Gfap -Cre-GFP. The parameters were analyzed in basal conditions. ( F ) Experimental approach. ( G ) cumulative meal events (events/24 h), ( H ) food intake (g/1 h), ( I ) cumulative food intake (g/12 h) during the dark and light cycle, ( J ) cumulative food intake (g/1 h) after 24 h of fasting, ( K ) cumulative food intake at 1 h and 6 h of refeeding, ( L ) cumulative food intake (g/1 h), ( M ) feeding rate (mg/min), and ( J ) first meal duration (min) by mice with ad libitum access to food as well as those undergoing a fasting-refeeding period. All the experiments were performed in Slc2a2 loxP/loxP mice transduced for 4-weeks with the viral vector AAV- Gfap -GFP or AAV 5 - Gfap -Cre-GFP. Error bars represent SEM. Comparisons between two groups were performed using a student’s t -test. Multiple comparisons were performed using a two-way ANOVA (Bonferonni’s post-hoc test). n.s not significant.

    Journal: Scientific Reports

    Article Title: GLUT2 expression by glial fibrillary acidic protein-positive tanycytes is required for promoting feeding-response to fasting

    doi: 10.1038/s41598-022-22489-2

    Figure Lengend Snippet: Glut2 expression in GFAP-expressing tanycytes is required for stimulating feeding in response to fasting. ( A ) Body weight (g), ( B ) cumulative meal events (events/24 h), ( C ) cumulative food intake (g/24 h), ( D ) cumulative food intake (g/12 h) in the dark and light phase of feeding and ( E ) cumulative food intake (g/1 h) during the 12 h of the dark phase of feeding in Slc2a2 loxP/loxP mice transduced with AAV- Gfap -GFP or AAV- Gfap -Cre-GFP. The parameters were analyzed in basal conditions. ( F ) Experimental approach. ( G ) cumulative meal events (events/24 h), ( H ) food intake (g/1 h), ( I ) cumulative food intake (g/12 h) during the dark and light cycle, ( J ) cumulative food intake (g/1 h) after 24 h of fasting, ( K ) cumulative food intake at 1 h and 6 h of refeeding, ( L ) cumulative food intake (g/1 h), ( M ) feeding rate (mg/min), and ( J ) first meal duration (min) by mice with ad libitum access to food as well as those undergoing a fasting-refeeding period. All the experiments were performed in Slc2a2 loxP/loxP mice transduced for 4-weeks with the viral vector AAV- Gfap -GFP or AAV 5 - Gfap -Cre-GFP. Error bars represent SEM. Comparisons between two groups were performed using a student’s t -test. Multiple comparisons were performed using a two-way ANOVA (Bonferonni’s post-hoc test). n.s not significant.

    Article Snippet: Rabbit anti-GLUT2 (1:200; Alomone, AGT-022, Jerusalem BioPark, Jerusalem, Israel), chicken anti-vimentin (1:400; Millipore, AB5733, Billerica, MA, USA), and mouse anti-GFAP (1:500; Millipore, MAB360) were used as primary antibodies after dilution in PBS and 1% bovine serum albumin.

    Techniques: Expressing, Mouse Assay, Transduction, Plasmid Preparation

    Loss of regulated Pomc expression in response to Glut2 inactivation during the fasting-to-refeeding transition. ( A ) Experimental approach. Slc2a2 loxP/loxP mice transduced for 6-weeks with the viral vector AAV- Gfap -GFP or AAV- Gfap -Cre-GFP. Total RNA was obtained after 24 h of fasted (grey bars) and 6 h of refed (purpure bars). Analysis of Npy ( B ), Cart ( C ), and Pomc ( D ) mRNA expression using qRT‐PCR. Error bars represent SEM. Multiple comparisons were performed using a two-way ANOVA. n.s not significant.

    Journal: Scientific Reports

    Article Title: GLUT2 expression by glial fibrillary acidic protein-positive tanycytes is required for promoting feeding-response to fasting

    doi: 10.1038/s41598-022-22489-2

    Figure Lengend Snippet: Loss of regulated Pomc expression in response to Glut2 inactivation during the fasting-to-refeeding transition. ( A ) Experimental approach. Slc2a2 loxP/loxP mice transduced for 6-weeks with the viral vector AAV- Gfap -GFP or AAV- Gfap -Cre-GFP. Total RNA was obtained after 24 h of fasted (grey bars) and 6 h of refed (purpure bars). Analysis of Npy ( B ), Cart ( C ), and Pomc ( D ) mRNA expression using qRT‐PCR. Error bars represent SEM. Multiple comparisons were performed using a two-way ANOVA. n.s not significant.

    Article Snippet: Rabbit anti-GLUT2 (1:200; Alomone, AGT-022, Jerusalem BioPark, Jerusalem, Israel), chicken anti-vimentin (1:400; Millipore, AB5733, Billerica, MA, USA), and mouse anti-GFAP (1:500; Millipore, MAB360) were used as primary antibodies after dilution in PBS and 1% bovine serum albumin.

    Techniques: Expressing, Mouse Assay, Plasmid Preparation, Quantitative RT-PCR

    Glut2 gene inactivation in GFAP-expressing tanycytes and its in situ evaluation. ( A ) Experimental approach. Slc2a2 loxP/loxP mice were injected into the 3V with a control viral vector AAV- Gfap -GFP or a viral vector that expresses the CRE recombinase under the control of GFAP promoter (AAV- Gfap -Cre-GFP). ( B ) Structure of the Glut2 floxed construction and genomic PCR of mice injected with AAV- Gfap -GFP (lane 1) or AAV- Gfap -Cre-GFP (lane 2). ( C ) GFP fluorescence (green) in coronal sections (20 µm) of mice transduced for two weeks. DAPI was used as a nuclear marker (magenta). ( D ) GFP fluorescence in GFAP-expressing tanycytes was analyzed through vimentin (purple) and GFAP immunoreactivity (yellow). DAPI was used as a nuclear marker (blue). ( E ) Percentage of GFAP-expressing tanycytes positives for the GFP fluorescence. ( F ) GFP fluorescence in GFAP-expressing tanycytes analyzed through the GFAP immunoreactivity (red). DAPI was used as a nuclear marker (blue). ( G – L ) Percentage of GFAP-expressing tanycytes transduced in the hypothalamic anteroposterior and dorsoventral axis (n = 3 mice). P1 primer 1, P2 primer 2, P3 primer 3, 3V third ventricle, ME median eminence, DMN dorsomedial nucleus, VMN ventromedial nucleus, ARC arcuate nucleus, PVN paraventricular nucleus, DTM dorsal tuberomammillary nucleus.

    Journal: Scientific Reports

    Article Title: GLUT2 expression by glial fibrillary acidic protein-positive tanycytes is required for promoting feeding-response to fasting

    doi: 10.1038/s41598-022-22489-2

    Figure Lengend Snippet: Glut2 gene inactivation in GFAP-expressing tanycytes and its in situ evaluation. ( A ) Experimental approach. Slc2a2 loxP/loxP mice were injected into the 3V with a control viral vector AAV- Gfap -GFP or a viral vector that expresses the CRE recombinase under the control of GFAP promoter (AAV- Gfap -Cre-GFP). ( B ) Structure of the Glut2 floxed construction and genomic PCR of mice injected with AAV- Gfap -GFP (lane 1) or AAV- Gfap -Cre-GFP (lane 2). ( C ) GFP fluorescence (green) in coronal sections (20 µm) of mice transduced for two weeks. DAPI was used as a nuclear marker (magenta). ( D ) GFP fluorescence in GFAP-expressing tanycytes was analyzed through vimentin (purple) and GFAP immunoreactivity (yellow). DAPI was used as a nuclear marker (blue). ( E ) Percentage of GFAP-expressing tanycytes positives for the GFP fluorescence. ( F ) GFP fluorescence in GFAP-expressing tanycytes analyzed through the GFAP immunoreactivity (red). DAPI was used as a nuclear marker (blue). ( G – L ) Percentage of GFAP-expressing tanycytes transduced in the hypothalamic anteroposterior and dorsoventral axis (n = 3 mice). P1 primer 1, P2 primer 2, P3 primer 3, 3V third ventricle, ME median eminence, DMN dorsomedial nucleus, VMN ventromedial nucleus, ARC arcuate nucleus, PVN paraventricular nucleus, DTM dorsal tuberomammillary nucleus.

    Article Snippet: Rabbit anti-GLUT2 (1:200; Alomone, AGT-022, Jerusalem BioPark, Jerusalem, Israel), chicken anti-vimentin (1:400; Millipore, AB5733, Billerica, MA, USA), and mouse anti-GFAP (1:500; Millipore, MAB360) were used as primary antibodies after dilution in PBS and 1% bovine serum albumin.

    Techniques: Expressing, In Situ, Mouse Assay, Injection, Plasmid Preparation, Polymerase Chain Reaction, Fluorescence, Marker

    Glut2 inactivation enhances the ghrelin secretion in fasting. ( A ) Blood glucose concentration (mmol/L), ( B ) plasma insulin concentration (ng/mL) and ( C ) plasma glucagon concentration (pg/mL). ( D ) Mice show a normal i.p GTT (2 g/kg). ( E ) Plasma leptin (ng/mL), ( F ) plasma GLP-1 (pM) and ( G ) plasma total ghrelin (ng/mL) concentrations. All the measurements were performed on mice transduced for 4-weeks with the viral vector AAV- Gfap -GFP (grey bars) or AAV- Gfap -Cre-GFP (purpure bars). Plasma samples were obtained after 24 h of fasting and 6 h of refeeding. ( H ) Ghrelin response. Total food intake (g) was measured 1 h post i.p treatment of mouse acyl-ghrelin (10 µg/kg) or vehicle (NaCl 0.9% w/v). Error bars represent SEM. Multiple comparisons were performed using a two-way ANOVA (Bonferonni’s post-hoc test). n.s not significant.

    Journal: Scientific Reports

    Article Title: GLUT2 expression by glial fibrillary acidic protein-positive tanycytes is required for promoting feeding-response to fasting

    doi: 10.1038/s41598-022-22489-2

    Figure Lengend Snippet: Glut2 inactivation enhances the ghrelin secretion in fasting. ( A ) Blood glucose concentration (mmol/L), ( B ) plasma insulin concentration (ng/mL) and ( C ) plasma glucagon concentration (pg/mL). ( D ) Mice show a normal i.p GTT (2 g/kg). ( E ) Plasma leptin (ng/mL), ( F ) plasma GLP-1 (pM) and ( G ) plasma total ghrelin (ng/mL) concentrations. All the measurements were performed on mice transduced for 4-weeks with the viral vector AAV- Gfap -GFP (grey bars) or AAV- Gfap -Cre-GFP (purpure bars). Plasma samples were obtained after 24 h of fasting and 6 h of refeeding. ( H ) Ghrelin response. Total food intake (g) was measured 1 h post i.p treatment of mouse acyl-ghrelin (10 µg/kg) or vehicle (NaCl 0.9% w/v). Error bars represent SEM. Multiple comparisons were performed using a two-way ANOVA (Bonferonni’s post-hoc test). n.s not significant.

    Article Snippet: Rabbit anti-GLUT2 (1:200; Alomone, AGT-022, Jerusalem BioPark, Jerusalem, Israel), chicken anti-vimentin (1:400; Millipore, AB5733, Billerica, MA, USA), and mouse anti-GFAP (1:500; Millipore, MAB360) were used as primary antibodies after dilution in PBS and 1% bovine serum albumin.

    Techniques: Concentration Assay, Mouse Assay, Plasmid Preparation

    GLUT2 is expressed in hypothalamic tanycytes. Low and high magnification images of tanycytes facing the VMN ( A ) and ARC ( B ) using the anti-GLUT2 (red) and anti-vimentin (green) antibodies. DAPI was used as a nuclear marker. 3V third ventricle, ME median eminence, VMN ventromedial nucleus, ARC arcuate nucleus.

    Journal: Scientific Reports

    Article Title: GLUT2 expression by glial fibrillary acidic protein-positive tanycytes is required for promoting feeding-response to fasting

    doi: 10.1038/s41598-022-22489-2

    Figure Lengend Snippet: GLUT2 is expressed in hypothalamic tanycytes. Low and high magnification images of tanycytes facing the VMN ( A ) and ARC ( B ) using the anti-GLUT2 (red) and anti-vimentin (green) antibodies. DAPI was used as a nuclear marker. 3V third ventricle, ME median eminence, VMN ventromedial nucleus, ARC arcuate nucleus.

    Article Snippet: Rabbit anti-GLUT2 (1:200; Alomone, AGT-022, Jerusalem BioPark, Jerusalem, Israel), chicken anti-vimentin (1:400; Millipore, AB5733, Billerica, MA, USA), and mouse anti-GFAP (1:500; Millipore, MAB360) were used as primary antibodies after dilution in PBS and 1% bovine serum albumin.

    Techniques: Marker

    Glut2 inactivation increases c-Fos expression in the VMN response to fasting. ( A – E ) Representative images and quantification of c-Fos-immunoreactive cells (white) in the hypothalamus of Slc2a2 loxP/loxP mice transduced for 4-weeks with the viral vector AAV- Gfap -GFP (grey bars) or AAV- Gfap -Cre-GFP (purpure bars). Antero-posterior c-Fos quantification was performed from the bregma AP-1.54 mm ( A ) to bregma AP − 2.54 mm ( E ) in 24 h fasted mice. Error bars represent SEM. Multiple comparisons were performed using a two-way ANOVA (Bonferonni’s post-hoc test). DMN Dorsomedial nucleus, VMN ventromedial nucleus, ARC arcuate nucleus, DTM dorsal tuberomammillary nucleus, PVN paraventricular nucleus, 3V third ventricle. n.s not significant.

    Journal: Scientific Reports

    Article Title: GLUT2 expression by glial fibrillary acidic protein-positive tanycytes is required for promoting feeding-response to fasting

    doi: 10.1038/s41598-022-22489-2

    Figure Lengend Snippet: Glut2 inactivation increases c-Fos expression in the VMN response to fasting. ( A – E ) Representative images and quantification of c-Fos-immunoreactive cells (white) in the hypothalamus of Slc2a2 loxP/loxP mice transduced for 4-weeks with the viral vector AAV- Gfap -GFP (grey bars) or AAV- Gfap -Cre-GFP (purpure bars). Antero-posterior c-Fos quantification was performed from the bregma AP-1.54 mm ( A ) to bregma AP − 2.54 mm ( E ) in 24 h fasted mice. Error bars represent SEM. Multiple comparisons were performed using a two-way ANOVA (Bonferonni’s post-hoc test). DMN Dorsomedial nucleus, VMN ventromedial nucleus, ARC arcuate nucleus, DTM dorsal tuberomammillary nucleus, PVN paraventricular nucleus, 3V third ventricle. n.s not significant.

    Article Snippet: Rabbit anti-GLUT2 (1:200; Alomone, AGT-022, Jerusalem BioPark, Jerusalem, Israel), chicken anti-vimentin (1:400; Millipore, AB5733, Billerica, MA, USA), and mouse anti-GFAP (1:500; Millipore, MAB360) were used as primary antibodies after dilution in PBS and 1% bovine serum albumin.

    Techniques: Expressing, Mouse Assay, Plasmid Preparation

    CB 1 R regulates mTORC1 activation under normoglycemic conditions. a , c Immunoblotting analysis and quantification of pS6 in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 5 mice per group (* P = 0.0166). b , d Immunoblotting analysis and quantification of pAKT in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 4 mice per group (* P = 0.0275). e – g Immunoblotting analysis and quantification of SREBP1c and GLUT2 in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 6 mice per group (* P

    Journal: Nature Communications

    Article Title: Opposite physiological and pathological mTORC1-mediated roles of the CB1 receptor in regulating renal tubular function

    doi: 10.1038/s41467-022-29124-8

    Figure Lengend Snippet: CB 1 R regulates mTORC1 activation under normoglycemic conditions. a , c Immunoblotting analysis and quantification of pS6 in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 5 mice per group (* P = 0.0166). b , d Immunoblotting analysis and quantification of pAKT in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 4 mice per group (* P = 0.0275). e – g Immunoblotting analysis and quantification of SREBP1c and GLUT2 in kidney lysates from WT-RPTC CB1R+/+ and WT-RPTC CB1R−/− normoglycemic mice. n = 6 mice per group (* P

    Article Snippet: After an additional two hours of blocking in 2% BSA, cells were incubated overnight with Rabbit anti-GLUT2 (#AGT022, Alomone, 1:500) or Rabbit anti-SREBP1 (ab193318, Abcam, 1:500).

    Techniques: Activation Assay, Mouse Assay

    A proposed mechanism by which renal proximal tubule CB 1 R regulates mTORC1 activity in health and disease. In normoglycemia CB 1 R is responsible to maintain mTORC1 normal activation by preventing excess of amino acids uptake (left). In hyperglycemia, CB 1 R-mediated mTORC1 over-activation results in upregulating GLUT2 transcription, consequently enhancing glucose absorption and tubular damage (right).

    Journal: Nature Communications

    Article Title: Opposite physiological and pathological mTORC1-mediated roles of the CB1 receptor in regulating renal tubular function

    doi: 10.1038/s41467-022-29124-8

    Figure Lengend Snippet: A proposed mechanism by which renal proximal tubule CB 1 R regulates mTORC1 activity in health and disease. In normoglycemia CB 1 R is responsible to maintain mTORC1 normal activation by preventing excess of amino acids uptake (left). In hyperglycemia, CB 1 R-mediated mTORC1 over-activation results in upregulating GLUT2 transcription, consequently enhancing glucose absorption and tubular damage (right).

    Article Snippet: After an additional two hours of blocking in 2% BSA, cells were incubated overnight with Rabbit anti-GLUT2 (#AGT022, Alomone, 1:500) or Rabbit anti-SREBP1 (ab193318, Abcam, 1:500).

    Techniques: Activity Assay, Activation Assay

    Genetic reduction of GLUT2 in RPTCs protects mice from developing DKD. All the following measurements were done in Akita diabetic mice and their littermate WT controls with or without reduced expression of GLUT2 in RPTCs: a Body weight surveillance for a period of 16 weeks. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− . b Blood glucose surveillance for a period of 16 weeks. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− . c Serum glucose. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− (* P

    Journal: Nature Communications

    Article Title: Opposite physiological and pathological mTORC1-mediated roles of the CB1 receptor in regulating renal tubular function

    doi: 10.1038/s41467-022-29124-8

    Figure Lengend Snippet: Genetic reduction of GLUT2 in RPTCs protects mice from developing DKD. All the following measurements were done in Akita diabetic mice and their littermate WT controls with or without reduced expression of GLUT2 in RPTCs: a Body weight surveillance for a period of 16 weeks. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− . b Blood glucose surveillance for a period of 16 weeks. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− . c Serum glucose. n = 16 mice for WT-RPTC GLUT2+/+ , n = 17 mice for WT-RPTC GLUT2−/− , n = 20 mice for Akita-RPTC GLUT2+/+ , n = 17 mice for Akita-RPTC GLUT2−/− (* P

    Article Snippet: After an additional two hours of blocking in 2% BSA, cells were incubated overnight with Rabbit anti-GLUT2 (#AGT022, Alomone, 1:500) or Rabbit anti-SREBP1 (ab193318, Abcam, 1:500).

    Techniques: Mouse Assay, Expressing

    RPTC CB 1 R regulates mTORC1 and GLUT2. a , d Immunoblotting analysis and quantification of pS6 (S235/236) in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 4 mice for Akita-RPTC CB1R+/+ , n = 5 mice for Akita-RPTC CB1R−/− (* P = 0.0032). b , e Immunoblotting analysis and quantification of pAKT (S473) in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 4 mice for Akita-RPTC CB1R+/+ , n = 5 mice for Akita-RPTC CB1R−/− (* P = 0.0056). c , f Immunoblotting analysis and quantification of GLUT2 in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 5 mice per group (* P

    Journal: Nature Communications

    Article Title: Opposite physiological and pathological mTORC1-mediated roles of the CB1 receptor in regulating renal tubular function

    doi: 10.1038/s41467-022-29124-8

    Figure Lengend Snippet: RPTC CB 1 R regulates mTORC1 and GLUT2. a , d Immunoblotting analysis and quantification of pS6 (S235/236) in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 4 mice for Akita-RPTC CB1R+/+ , n = 5 mice for Akita-RPTC CB1R−/− (* P = 0.0032). b , e Immunoblotting analysis and quantification of pAKT (S473) in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 4 mice for Akita-RPTC CB1R+/+ , n = 5 mice for Akita-RPTC CB1R−/− (* P = 0.0056). c , f Immunoblotting analysis and quantification of GLUT2 in kidney lysates from Akita-RPTC CB1R+/+ and Akita-RPTC CB1R−/− diabetic mice. n = 5 mice per group (* P

    Article Snippet: After an additional two hours of blocking in 2% BSA, cells were incubated overnight with Rabbit anti-GLUT2 (#AGT022, Alomone, 1:500) or Rabbit anti-SREBP1 (ab193318, Abcam, 1:500).

    Techniques: Mouse Assay

    GLUT2 transcription is directly regulated by CB 1 R and mTORC1. a – e Luminescence relative response ratio (RRR) analyses of HEK293 cells co-transfected transiently with pGL3-GLUT and Renilla luciferase plasmids (T2) or with pGL3-GLUT, Renilla luciferase, and CB 1 R-TK-d64 plasmids (T3), treated with or without ACEA (10 μM; b , c ) or with HG (30 mM; a , d , e ) for 3 h, in the presence or absence of JD5037 (100 nM) or rapamycin (100 nM). For a , n = 6 for T2, n = 8 for T2+HG (* P = 0.0034). For b , n = 16 per group (* P

    Journal: Nature Communications

    Article Title: Opposite physiological and pathological mTORC1-mediated roles of the CB1 receptor in regulating renal tubular function

    doi: 10.1038/s41467-022-29124-8

    Figure Lengend Snippet: GLUT2 transcription is directly regulated by CB 1 R and mTORC1. a – e Luminescence relative response ratio (RRR) analyses of HEK293 cells co-transfected transiently with pGL3-GLUT and Renilla luciferase plasmids (T2) or with pGL3-GLUT, Renilla luciferase, and CB 1 R-TK-d64 plasmids (T3), treated with or without ACEA (10 μM; b , c ) or with HG (30 mM; a , d , e ) for 3 h, in the presence or absence of JD5037 (100 nM) or rapamycin (100 nM). For a , n = 6 for T2, n = 8 for T2+HG (* P = 0.0034). For b , n = 16 per group (* P

    Article Snippet: After an additional two hours of blocking in 2% BSA, cells were incubated overnight with Rabbit anti-GLUT2 (#AGT022, Alomone, 1:500) or Rabbit anti-SREBP1 (ab193318, Abcam, 1:500).

    Techniques: Transfection, Luciferase