Review



rabbit polyclonal anti mtor  (Cell Signaling Technology Inc)


Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 97

    Structured Review

    Cell Signaling Technology Inc rabbit polyclonal anti mtor
    Rabbit Polyclonal Anti Mtor, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 4791 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti mtor/product/Cell Signaling Technology Inc
    Average 97 stars, based on 4791 article reviews
    rabbit polyclonal anti mtor - by Bioz Stars, 2026-04
    97/100 stars

    Images



    Similar Products

    96
    Proteintech rabbit polyclonal anti mtor
    Rabbit Polyclonal Anti Mtor, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti mtor/product/Proteintech
    Average 96 stars, based on 1 article reviews
    rabbit polyclonal anti mtor - by Bioz Stars, 2026-04
    96/100 stars
      Buy from Supplier

    93
    Cusabio technology
    Technology, supplied by Cusabio, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/technology/product/Cusabio
    Average 93 stars, based on 1 article reviews
    technology - by Bioz Stars, 2026-04
    93/100 stars
      Buy from Supplier

    90
    ImmunoWay Biotechnology Company rabbit polyclonal anti-human phosphorylated mtor (ser 2448 ) antibody
    Dose-dependent stimulation of β-casein, <t>mTOR</t> phosphorylation, SREBP1 and cyclin D1 by exogenous Met and Leu. Confluent cultures of bovine mammary epithelial cells were treated by adding either Met (0, 0.2, 0.4, 0.6 and 0.8 mM) (Upper panel) or Leu (0, 0.2, 0.4, 0.6 and 0.8 mM) (Lower panel) to the Opti-MEM medium (37 °C). After 24 h, cells were lysed and subjected to Western blot analysis. Protein levels of β-casein, mTOR, SREBP1, cyclin D1, β-actin and <t>p-mTOR</t> were established by densitometric analysis of the immunopositive bands enabling calculation of p-mTOR/mTOR. Protein levels presented were first normalized to β-actin and then to its corresponding no-AA control group. Values are presented as mean ± SEM for three independent experiments. Statistical effects compared with no-AA control group, ∗ P < 0.05, ∗∗ P < 0.01. mTOR = mechanistic target of rapamycin; SREBP1 = sterol regulatory element-binding protein 1.
    Rabbit Polyclonal Anti Human Phosphorylated Mtor (Ser 2448 ) Antibody, supplied by ImmunoWay Biotechnology Company, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti-human phosphorylated mtor (ser 2448 ) antibody/product/ImmunoWay Biotechnology Company
    Average 90 stars, based on 1 article reviews
    rabbit polyclonal anti-human phosphorylated mtor (ser 2448 ) antibody - by Bioz Stars, 2026-04
    90/100 stars
      Buy from Supplier

    90
    ImmunoWay Biotechnology Company rabbit polyclonal anti-human mtor antibody
    Dose-dependent stimulation of β-casein, <t>mTOR</t> phosphorylation, SREBP1 and cyclin D1 by exogenous Met and Leu. Confluent cultures of bovine mammary epithelial cells were treated by adding either Met (0, 0.2, 0.4, 0.6 and 0.8 mM) (Upper panel) or Leu (0, 0.2, 0.4, 0.6 and 0.8 mM) (Lower panel) to the Opti-MEM medium (37 °C). After 24 h, cells were lysed and subjected to Western blot analysis. Protein levels of β-casein, mTOR, SREBP1, cyclin D1, β-actin and p-mTOR were established by densitometric analysis of the immunopositive bands enabling calculation of p-mTOR/mTOR. Protein levels presented were first normalized to β-actin and then to its corresponding no-AA control group. Values are presented as mean ± SEM for three independent experiments. Statistical effects compared with no-AA control group, ∗ P < 0.05, ∗∗ P < 0.01. mTOR = mechanistic target of rapamycin; SREBP1 = sterol regulatory element-binding protein 1.
    Rabbit Polyclonal Anti Human Mtor Antibody, supplied by ImmunoWay Biotechnology Company, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti-human mtor antibody/product/ImmunoWay Biotechnology Company
    Average 90 stars, based on 1 article reviews
    rabbit polyclonal anti-human mtor antibody - by Bioz Stars, 2026-04
    90/100 stars
      Buy from Supplier

    97
    Cell Signaling Technology Inc rabbit polyclonal anti mtor
    Dose-dependent stimulation of β-casein, <t>mTOR</t> phosphorylation, SREBP1 and cyclin D1 by exogenous Met and Leu. Confluent cultures of bovine mammary epithelial cells were treated by adding either Met (0, 0.2, 0.4, 0.6 and 0.8 mM) (Upper panel) or Leu (0, 0.2, 0.4, 0.6 and 0.8 mM) (Lower panel) to the Opti-MEM medium (37 °C). After 24 h, cells were lysed and subjected to Western blot analysis. Protein levels of β-casein, mTOR, SREBP1, cyclin D1, β-actin and p-mTOR were established by densitometric analysis of the immunopositive bands enabling calculation of p-mTOR/mTOR. Protein levels presented were first normalized to β-actin and then to its corresponding no-AA control group. Values are presented as mean ± SEM for three independent experiments. Statistical effects compared with no-AA control group, ∗ P < 0.05, ∗∗ P < 0.01. mTOR = mechanistic target of rapamycin; SREBP1 = sterol regulatory element-binding protein 1.
    Rabbit Polyclonal Anti Mtor, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti mtor/product/Cell Signaling Technology Inc
    Average 97 stars, based on 1 article reviews
    rabbit polyclonal anti mtor - by Bioz Stars, 2026-04
    97/100 stars
      Buy from Supplier

    97
    Cell Signaling Technology Inc rabbit polyclonal anti mtor antibody
    Signaling pathways involved in the genesis of mood cycling (A) Schematic showing comparative analysis of hippocampal gene expression profiles between manic and depressive Syt7 KO mice. GeneM, comparison between the WT mice and the manic Syt7 KO mice. GeneD, comparison between the WT mice and the depressive Syt7 KO mice. (B and C) Heatmap (B) and distribution (C) of genes differentially expressed between GeneM and GeneD. (D) Expression of representative BD-related genes in manic and depressive Syt7 KO mice. (E) Representative significantly enriched KEGG pathways showing bi-directional alterations in the manic and depressive episodes in Syt7 KO mice. (F and G) Schematic (F) and heatmap (G) showing the comparative analysis of transcripts bi-directionally regulated in drug-induced/Syt7 deficiency-induced manic and depressive mice. GeneR, comparison between the WT mice with and without the Ro25 treatment in the dark phase. GeneB, comparison between the WT mice with and without the BMS-536924 treatment in the light phase. (H) Representative significantly enriched KEGG pathways showing bi-directional alterations between the drug-induced/Syt7-deficiency-induced manic and depressive mice. (I) Mapping of representative KEGG pathways for network analysis. (J) Bi-directional regulation of representative genes within featured KEGG pathways in mice with drug-induced/Syt7-deficiency-induced mania or depression. (K and L) Immunoblots (left) and quantitative analysis (right) of mammalian targets of rapamycin <t>(mTOR)</t> (K) and eukaryotic elongation factor 2 (eEF2) (L) phosphorylation in the hippocampus of WT and Syt7 KO mice. n = 3. Student’s t test; ∗ p < 0.05; ∗∗ p < 0.001; error bars, SEM.
    Rabbit Polyclonal Anti Mtor Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti mtor antibody/product/Cell Signaling Technology Inc
    Average 97 stars, based on 1 article reviews
    rabbit polyclonal anti mtor antibody - by Bioz Stars, 2026-04
    97/100 stars
      Buy from Supplier

    97
    Cell Signaling Technology Inc rabbit polyclonal anti p mtor antibody
    Signaling pathways involved in the genesis of mood cycling (A) Schematic showing comparative analysis of hippocampal gene expression profiles between manic and depressive Syt7 KO mice. GeneM, comparison between the WT mice and the manic Syt7 KO mice. GeneD, comparison between the WT mice and the depressive Syt7 KO mice. (B and C) Heatmap (B) and distribution (C) of genes differentially expressed between GeneM and GeneD. (D) Expression of representative BD-related genes in manic and depressive Syt7 KO mice. (E) Representative significantly enriched KEGG pathways showing bi-directional alterations in the manic and depressive episodes in Syt7 KO mice. (F and G) Schematic (F) and heatmap (G) showing the comparative analysis of transcripts bi-directionally regulated in drug-induced/Syt7 deficiency-induced manic and depressive mice. GeneR, comparison between the WT mice with and without the Ro25 treatment in the dark phase. GeneB, comparison between the WT mice with and without the BMS-536924 treatment in the light phase. (H) Representative significantly enriched KEGG pathways showing bi-directional alterations between the drug-induced/Syt7-deficiency-induced manic and depressive mice. (I) Mapping of representative KEGG pathways for network analysis. (J) Bi-directional regulation of representative genes within featured KEGG pathways in mice with drug-induced/Syt7-deficiency-induced mania or depression. (K and L) Immunoblots (left) and quantitative analysis (right) of mammalian targets of rapamycin <t>(mTOR)</t> (K) and eukaryotic elongation factor 2 (eEF2) (L) phosphorylation in the hippocampus of WT and Syt7 KO mice. n = 3. Student’s t test; ∗ p < 0.05; ∗∗ p < 0.001; error bars, SEM.
    Rabbit Polyclonal Anti P Mtor Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti p mtor antibody/product/Cell Signaling Technology Inc
    Average 97 stars, based on 1 article reviews
    rabbit polyclonal anti p mtor antibody - by Bioz Stars, 2026-04
    97/100 stars
      Buy from Supplier

    97
    Cell Signaling Technology Inc rabbit polyclonal anti p mtor
    Signaling pathways involved in the genesis of mood cycling (A) Schematic showing comparative analysis of hippocampal gene expression profiles between manic and depressive Syt7 KO mice. GeneM, comparison between the WT mice and the manic Syt7 KO mice. GeneD, comparison between the WT mice and the depressive Syt7 KO mice. (B and C) Heatmap (B) and distribution (C) of genes differentially expressed between GeneM and GeneD. (D) Expression of representative BD-related genes in manic and depressive Syt7 KO mice. (E) Representative significantly enriched KEGG pathways showing bi-directional alterations in the manic and depressive episodes in Syt7 KO mice. (F and G) Schematic (F) and heatmap (G) showing the comparative analysis of transcripts bi-directionally regulated in drug-induced/Syt7 deficiency-induced manic and depressive mice. GeneR, comparison between the WT mice with and without the Ro25 treatment in the dark phase. GeneB, comparison between the WT mice with and without the BMS-536924 treatment in the light phase. (H) Representative significantly enriched KEGG pathways showing bi-directional alterations between the drug-induced/Syt7-deficiency-induced manic and depressive mice. (I) Mapping of representative KEGG pathways for network analysis. (J) Bi-directional regulation of representative genes within featured KEGG pathways in mice with drug-induced/Syt7-deficiency-induced mania or depression. (K and L) Immunoblots (left) and quantitative analysis (right) of mammalian targets of rapamycin <t>(mTOR)</t> (K) and eukaryotic elongation factor 2 (eEF2) (L) phosphorylation in the hippocampus of WT and Syt7 KO mice. n = 3. Student’s t test; ∗ p < 0.05; ∗∗ p < 0.001; error bars, SEM.
    Rabbit Polyclonal Anti P Mtor, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti p mtor/product/Cell Signaling Technology Inc
    Average 97 stars, based on 1 article reviews
    rabbit polyclonal anti p mtor - by Bioz Stars, 2026-04
    97/100 stars
      Buy from Supplier

    Image Search Results


    Dose-dependent stimulation of β-casein, mTOR phosphorylation, SREBP1 and cyclin D1 by exogenous Met and Leu. Confluent cultures of bovine mammary epithelial cells were treated by adding either Met (0, 0.2, 0.4, 0.6 and 0.8 mM) (Upper panel) or Leu (0, 0.2, 0.4, 0.6 and 0.8 mM) (Lower panel) to the Opti-MEM medium (37 °C). After 24 h, cells were lysed and subjected to Western blot analysis. Protein levels of β-casein, mTOR, SREBP1, cyclin D1, β-actin and p-mTOR were established by densitometric analysis of the immunopositive bands enabling calculation of p-mTOR/mTOR. Protein levels presented were first normalized to β-actin and then to its corresponding no-AA control group. Values are presented as mean ± SEM for three independent experiments. Statistical effects compared with no-AA control group, ∗ P < 0.05, ∗∗ P < 0.01. mTOR = mechanistic target of rapamycin; SREBP1 = sterol regulatory element-binding protein 1.

    Journal: Animal Nutrition

    Article Title: Myotonic dystrophy-related CDC42-binding kinase alpha (MRCKα) mediates methionine- and leucine-stimulated β-casein synthesis in bovine mammary epithelial cells via targeting mTOR

    doi: 10.1016/j.aninu.2025.01.003

    Figure Lengend Snippet: Dose-dependent stimulation of β-casein, mTOR phosphorylation, SREBP1 and cyclin D1 by exogenous Met and Leu. Confluent cultures of bovine mammary epithelial cells were treated by adding either Met (0, 0.2, 0.4, 0.6 and 0.8 mM) (Upper panel) or Leu (0, 0.2, 0.4, 0.6 and 0.8 mM) (Lower panel) to the Opti-MEM medium (37 °C). After 24 h, cells were lysed and subjected to Western blot analysis. Protein levels of β-casein, mTOR, SREBP1, cyclin D1, β-actin and p-mTOR were established by densitometric analysis of the immunopositive bands enabling calculation of p-mTOR/mTOR. Protein levels presented were first normalized to β-actin and then to its corresponding no-AA control group. Values are presented as mean ± SEM for three independent experiments. Statistical effects compared with no-AA control group, ∗ P < 0.05, ∗∗ P < 0.01. mTOR = mechanistic target of rapamycin; SREBP1 = sterol regulatory element-binding protein 1.

    Article Snippet: Rabbit polyclonal anti-human mTOR antibody and rabbit polyclonal anti-human phosphorylated mTOR (Ser 2448 ) antibody were obtained from ImmunoWay Biotechnology Company (Plano, TX, USA).

    Techniques: Phospho-proteomics, Western Blot, Control, Binding Assay

    Silencing of MRCKα inhibits the stimulatory effects of Met and Leu on MRCKα, β-casein, PKB phosphorylation, and mTOR phosphorylation, but not PI3K phosphorylation in bovine mammary epithelial cells. Cells were transfected with scrambled siRNA (small interfering RNA; control, SC) or MRCKα siRNA (SI) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were lysed, and protein levels were detected by immunoblotting followed by densitometric analysis. All protein levels were first normalized to β-actin and then to SC + B group. Values are presented as mean ± SEM for three independent experiments. Different low case letters above columns indicate significant statistical differences ( P < 0.05). P AA , P -value of amino acid addition (AA); P SI , P -value of silencing of MRCKα (SI); P AA×SI , P -value of AA × SI interaction. MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; PI3K = phosphatidylinositol 3-kinase; PKB = protein kinase B; mTOR = mechanistic target of rapamycin.

    Journal: Animal Nutrition

    Article Title: Myotonic dystrophy-related CDC42-binding kinase alpha (MRCKα) mediates methionine- and leucine-stimulated β-casein synthesis in bovine mammary epithelial cells via targeting mTOR

    doi: 10.1016/j.aninu.2025.01.003

    Figure Lengend Snippet: Silencing of MRCKα inhibits the stimulatory effects of Met and Leu on MRCKα, β-casein, PKB phosphorylation, and mTOR phosphorylation, but not PI3K phosphorylation in bovine mammary epithelial cells. Cells were transfected with scrambled siRNA (small interfering RNA; control, SC) or MRCKα siRNA (SI) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were lysed, and protein levels were detected by immunoblotting followed by densitometric analysis. All protein levels were first normalized to β-actin and then to SC + B group. Values are presented as mean ± SEM for three independent experiments. Different low case letters above columns indicate significant statistical differences ( P < 0.05). P AA , P -value of amino acid addition (AA); P SI , P -value of silencing of MRCKα (SI); P AA×SI , P -value of AA × SI interaction. MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; PI3K = phosphatidylinositol 3-kinase; PKB = protein kinase B; mTOR = mechanistic target of rapamycin.

    Article Snippet: Rabbit polyclonal anti-human mTOR antibody and rabbit polyclonal anti-human phosphorylated mTOR (Ser 2448 ) antibody were obtained from ImmunoWay Biotechnology Company (Plano, TX, USA).

    Techniques: Phospho-proteomics, Transfection, Small Interfering RNA, Control, Western Blot, Binding Assay

    Inhibition of PI3K blocks the stimulatory action of Met and Leu on MRCKα, β-casein, PI3K phosphorylation and mTOR phosphorylation in bovine mammary epithelial cells. Cells were treated with blank (untreated control) or PI3K inhibitor (LY294002, 43 μM) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were lysed, and protein levels were detected by immunoblotting followed by densitometric analysis. All protein levels were first normalized to β-actin and then to Blank + B group. Values are presented as mean ± SEM for three independent experiments. Different low case letters above columns indicate significant statistical differences ( P < 0.05). P AA , P -value of amino acid addition (AA); P LY , P -value of inhibition of PI3K (LY); P AA×LY , P -value of AA × LY interaction. MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; PI3K = phosphatidylinositol 3-kinase; PKB = protein kinase B; mTOR = mechanistic target of rapamycin.

    Journal: Animal Nutrition

    Article Title: Myotonic dystrophy-related CDC42-binding kinase alpha (MRCKα) mediates methionine- and leucine-stimulated β-casein synthesis in bovine mammary epithelial cells via targeting mTOR

    doi: 10.1016/j.aninu.2025.01.003

    Figure Lengend Snippet: Inhibition of PI3K blocks the stimulatory action of Met and Leu on MRCKα, β-casein, PI3K phosphorylation and mTOR phosphorylation in bovine mammary epithelial cells. Cells were treated with blank (untreated control) or PI3K inhibitor (LY294002, 43 μM) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were lysed, and protein levels were detected by immunoblotting followed by densitometric analysis. All protein levels were first normalized to β-actin and then to Blank + B group. Values are presented as mean ± SEM for three independent experiments. Different low case letters above columns indicate significant statistical differences ( P < 0.05). P AA , P -value of amino acid addition (AA); P LY , P -value of inhibition of PI3K (LY); P AA×LY , P -value of AA × LY interaction. MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; PI3K = phosphatidylinositol 3-kinase; PKB = protein kinase B; mTOR = mechanistic target of rapamycin.

    Article Snippet: Rabbit polyclonal anti-human mTOR antibody and rabbit polyclonal anti-human phosphorylated mTOR (Ser 2448 ) antibody were obtained from ImmunoWay Biotechnology Company (Plano, TX, USA).

    Techniques: Inhibition, Phospho-proteomics, Control, Western Blot, Binding Assay

    Inhibition of protein kinase B (PKB) inhibits the stimulatory effects of MRCKα overexpression on β-casein and mTOR phosphorylation in bovine mammary epithelial cells. Cells were treated with blank (untreated control) or PKB inhibitor (MK2206, 1 μM) and transfected simultaneously with empty vector (control, EV) or MRCKα (OE). After 24 h, cells were lysed, and protein levels were detected by immunoblotting followed by densitometric analysis. All protein levels were first normalized to β-actin and then to Blank + EV group. Values are presented as mean ± SEM for three independent experiments. Different low case letters above columns indicate significant statistical differences ( P < 0.05). P OE , P -value of MRCKα overexpression (OE); P MK , P -value of inhibition of PKB (MK); P OE×MK , P -value of OE × MK interaction. MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; mTOR = mechanistic target of rapamycin.

    Journal: Animal Nutrition

    Article Title: Myotonic dystrophy-related CDC42-binding kinase alpha (MRCKα) mediates methionine- and leucine-stimulated β-casein synthesis in bovine mammary epithelial cells via targeting mTOR

    doi: 10.1016/j.aninu.2025.01.003

    Figure Lengend Snippet: Inhibition of protein kinase B (PKB) inhibits the stimulatory effects of MRCKα overexpression on β-casein and mTOR phosphorylation in bovine mammary epithelial cells. Cells were treated with blank (untreated control) or PKB inhibitor (MK2206, 1 μM) and transfected simultaneously with empty vector (control, EV) or MRCKα (OE). After 24 h, cells were lysed, and protein levels were detected by immunoblotting followed by densitometric analysis. All protein levels were first normalized to β-actin and then to Blank + EV group. Values are presented as mean ± SEM for three independent experiments. Different low case letters above columns indicate significant statistical differences ( P < 0.05). P OE , P -value of MRCKα overexpression (OE); P MK , P -value of inhibition of PKB (MK); P OE×MK , P -value of OE × MK interaction. MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; mTOR = mechanistic target of rapamycin.

    Article Snippet: Rabbit polyclonal anti-human mTOR antibody and rabbit polyclonal anti-human phosphorylated mTOR (Ser 2448 ) antibody were obtained from ImmunoWay Biotechnology Company (Plano, TX, USA).

    Techniques: Inhibition, Over Expression, Phospho-proteomics, Control, Transfection, Plasmid Preparation, Western Blot, Binding Assay

    Silencing of MRCKα inhibits the stimulatory effects of Met and Leu on mRNA abundance of genes related to milk protein synthesis in bovine mammary epithelial cells. Cells were transfected with scrambled siRNA (control, SC) or MRCKα siRNA (SI) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were collected and isolated for RT-qPCR analysis. Values are presented as mean ± SEM for three independent experiments. P AA , P -value of amino acid addition (AA); P SI , P -value of silencing of MRCKα (SI); P AA×SI , P -value of AA × SI interaction. CSN2 = β-casein; CSN1S1 = αS1-casein; CSN3 = κ-casein; LALBA = lactalbumin α; MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; mTOR = mechanistic target of rapamycin; JAK2 = Janus kinase 2; STAT5 = signal transducers and activators of transcription 5.

    Journal: Animal Nutrition

    Article Title: Myotonic dystrophy-related CDC42-binding kinase alpha (MRCKα) mediates methionine- and leucine-stimulated β-casein synthesis in bovine mammary epithelial cells via targeting mTOR

    doi: 10.1016/j.aninu.2025.01.003

    Figure Lengend Snippet: Silencing of MRCKα inhibits the stimulatory effects of Met and Leu on mRNA abundance of genes related to milk protein synthesis in bovine mammary epithelial cells. Cells were transfected with scrambled siRNA (control, SC) or MRCKα siRNA (SI) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were collected and isolated for RT-qPCR analysis. Values are presented as mean ± SEM for three independent experiments. P AA , P -value of amino acid addition (AA); P SI , P -value of silencing of MRCKα (SI); P AA×SI , P -value of AA × SI interaction. CSN2 = β-casein; CSN1S1 = αS1-casein; CSN3 = κ-casein; LALBA = lactalbumin α; MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; mTOR = mechanistic target of rapamycin; JAK2 = Janus kinase 2; STAT5 = signal transducers and activators of transcription 5.

    Article Snippet: Rabbit polyclonal anti-human mTOR antibody and rabbit polyclonal anti-human phosphorylated mTOR (Ser 2448 ) antibody were obtained from ImmunoWay Biotechnology Company (Plano, TX, USA).

    Techniques: Transfection, Control, Isolation, Quantitative RT-PCR, Binding Assay

    Amino acids are sensed by PI3K-MRCKα-PKB signaling pathways to activate mTOR and its downstream signaling, which leads to promotion of β-casein synthesis, SREBP1 and Cyclin D1 expression in BMEC. Besides, the mRNA abundance of CSN1S1 , CSN2 and JAK2 are decreased when MRCKα expression is inhibited. PI3K = phosphatidylinositol 3-kinase; MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; PKB = protein kinase B; mTOR = mechanistic target of rapamycin; CSN1S1 = αS1-casein; CSN2 = β-casein; JAK2 = Janus kinase 2.

    Journal: Animal Nutrition

    Article Title: Myotonic dystrophy-related CDC42-binding kinase alpha (MRCKα) mediates methionine- and leucine-stimulated β-casein synthesis in bovine mammary epithelial cells via targeting mTOR

    doi: 10.1016/j.aninu.2025.01.003

    Figure Lengend Snippet: Amino acids are sensed by PI3K-MRCKα-PKB signaling pathways to activate mTOR and its downstream signaling, which leads to promotion of β-casein synthesis, SREBP1 and Cyclin D1 expression in BMEC. Besides, the mRNA abundance of CSN1S1 , CSN2 and JAK2 are decreased when MRCKα expression is inhibited. PI3K = phosphatidylinositol 3-kinase; MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; PKB = protein kinase B; mTOR = mechanistic target of rapamycin; CSN1S1 = αS1-casein; CSN2 = β-casein; JAK2 = Janus kinase 2.

    Article Snippet: Rabbit polyclonal anti-human mTOR antibody and rabbit polyclonal anti-human phosphorylated mTOR (Ser 2448 ) antibody were obtained from ImmunoWay Biotechnology Company (Plano, TX, USA).

    Techniques: Protein-Protein interactions, Expressing, Binding Assay

    Dose-dependent stimulation of β-casein, mTOR phosphorylation, SREBP1 and cyclin D1 by exogenous Met and Leu. Confluent cultures of bovine mammary epithelial cells were treated by adding either Met (0, 0.2, 0.4, 0.6 and 0.8 mM) (Upper panel) or Leu (0, 0.2, 0.4, 0.6 and 0.8 mM) (Lower panel) to the Opti-MEM medium (37 °C). After 24 h, cells were lysed and subjected to Western blot analysis. Protein levels of β-casein, mTOR, SREBP1, cyclin D1, β-actin and p-mTOR were established by densitometric analysis of the immunopositive bands enabling calculation of p-mTOR/mTOR. Protein levels presented were first normalized to β-actin and then to its corresponding no-AA control group. Values are presented as mean ± SEM for three independent experiments. Statistical effects compared with no-AA control group, ∗ P < 0.05, ∗∗ P < 0.01. mTOR = mechanistic target of rapamycin; SREBP1 = sterol regulatory element-binding protein 1.

    Journal: Animal Nutrition

    Article Title: Myotonic dystrophy-related CDC42-binding kinase alpha (MRCKα) mediates methionine- and leucine-stimulated β-casein synthesis in bovine mammary epithelial cells via targeting mTOR

    doi: 10.1016/j.aninu.2025.01.003

    Figure Lengend Snippet: Dose-dependent stimulation of β-casein, mTOR phosphorylation, SREBP1 and cyclin D1 by exogenous Met and Leu. Confluent cultures of bovine mammary epithelial cells were treated by adding either Met (0, 0.2, 0.4, 0.6 and 0.8 mM) (Upper panel) or Leu (0, 0.2, 0.4, 0.6 and 0.8 mM) (Lower panel) to the Opti-MEM medium (37 °C). After 24 h, cells were lysed and subjected to Western blot analysis. Protein levels of β-casein, mTOR, SREBP1, cyclin D1, β-actin and p-mTOR were established by densitometric analysis of the immunopositive bands enabling calculation of p-mTOR/mTOR. Protein levels presented were first normalized to β-actin and then to its corresponding no-AA control group. Values are presented as mean ± SEM for three independent experiments. Statistical effects compared with no-AA control group, ∗ P < 0.05, ∗∗ P < 0.01. mTOR = mechanistic target of rapamycin; SREBP1 = sterol regulatory element-binding protein 1.

    Article Snippet: Rabbit polyclonal anti-human mTOR antibody and rabbit polyclonal anti-human phosphorylated mTOR (Ser 2448 ) antibody were obtained from ImmunoWay Biotechnology Company (Plano, TX, USA).

    Techniques: Phospho-proteomics, Western Blot, Control, Binding Assay

    Silencing of MRCKα inhibits the stimulatory effects of Met and Leu on MRCKα, β-casein, PKB phosphorylation, and mTOR phosphorylation, but not PI3K phosphorylation in bovine mammary epithelial cells. Cells were transfected with scrambled siRNA (small interfering RNA; control, SC) or MRCKα siRNA (SI) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were lysed, and protein levels were detected by immunoblotting followed by densitometric analysis. All protein levels were first normalized to β-actin and then to SC + B group. Values are presented as mean ± SEM for three independent experiments. Different low case letters above columns indicate significant statistical differences ( P < 0.05). P AA , P -value of amino acid addition (AA); P SI , P -value of silencing of MRCKα (SI); P AA×SI , P -value of AA × SI interaction. MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; PI3K = phosphatidylinositol 3-kinase; PKB = protein kinase B; mTOR = mechanistic target of rapamycin.

    Journal: Animal Nutrition

    Article Title: Myotonic dystrophy-related CDC42-binding kinase alpha (MRCKα) mediates methionine- and leucine-stimulated β-casein synthesis in bovine mammary epithelial cells via targeting mTOR

    doi: 10.1016/j.aninu.2025.01.003

    Figure Lengend Snippet: Silencing of MRCKα inhibits the stimulatory effects of Met and Leu on MRCKα, β-casein, PKB phosphorylation, and mTOR phosphorylation, but not PI3K phosphorylation in bovine mammary epithelial cells. Cells were transfected with scrambled siRNA (small interfering RNA; control, SC) or MRCKα siRNA (SI) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were lysed, and protein levels were detected by immunoblotting followed by densitometric analysis. All protein levels were first normalized to β-actin and then to SC + B group. Values are presented as mean ± SEM for three independent experiments. Different low case letters above columns indicate significant statistical differences ( P < 0.05). P AA , P -value of amino acid addition (AA); P SI , P -value of silencing of MRCKα (SI); P AA×SI , P -value of AA × SI interaction. MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; PI3K = phosphatidylinositol 3-kinase; PKB = protein kinase B; mTOR = mechanistic target of rapamycin.

    Article Snippet: Rabbit polyclonal anti-human mTOR antibody and rabbit polyclonal anti-human phosphorylated mTOR (Ser 2448 ) antibody were obtained from ImmunoWay Biotechnology Company (Plano, TX, USA).

    Techniques: Phospho-proteomics, Transfection, Small Interfering RNA, Control, Western Blot, Binding Assay

    Inhibition of PI3K blocks the stimulatory action of Met and Leu on MRCKα, β-casein, PI3K phosphorylation and mTOR phosphorylation in bovine mammary epithelial cells. Cells were treated with blank (untreated control) or PI3K inhibitor (LY294002, 43 μM) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were lysed, and protein levels were detected by immunoblotting followed by densitometric analysis. All protein levels were first normalized to β-actin and then to Blank + B group. Values are presented as mean ± SEM for three independent experiments. Different low case letters above columns indicate significant statistical differences ( P < 0.05). P AA , P -value of amino acid addition (AA); P LY , P -value of inhibition of PI3K (LY); P AA×LY , P -value of AA × LY interaction. MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; PI3K = phosphatidylinositol 3-kinase; PKB = protein kinase B; mTOR = mechanistic target of rapamycin.

    Journal: Animal Nutrition

    Article Title: Myotonic dystrophy-related CDC42-binding kinase alpha (MRCKα) mediates methionine- and leucine-stimulated β-casein synthesis in bovine mammary epithelial cells via targeting mTOR

    doi: 10.1016/j.aninu.2025.01.003

    Figure Lengend Snippet: Inhibition of PI3K blocks the stimulatory action of Met and Leu on MRCKα, β-casein, PI3K phosphorylation and mTOR phosphorylation in bovine mammary epithelial cells. Cells were treated with blank (untreated control) or PI3K inhibitor (LY294002, 43 μM) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were lysed, and protein levels were detected by immunoblotting followed by densitometric analysis. All protein levels were first normalized to β-actin and then to Blank + B group. Values are presented as mean ± SEM for three independent experiments. Different low case letters above columns indicate significant statistical differences ( P < 0.05). P AA , P -value of amino acid addition (AA); P LY , P -value of inhibition of PI3K (LY); P AA×LY , P -value of AA × LY interaction. MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; PI3K = phosphatidylinositol 3-kinase; PKB = protein kinase B; mTOR = mechanistic target of rapamycin.

    Article Snippet: Rabbit polyclonal anti-human mTOR antibody and rabbit polyclonal anti-human phosphorylated mTOR (Ser 2448 ) antibody were obtained from ImmunoWay Biotechnology Company (Plano, TX, USA).

    Techniques: Inhibition, Phospho-proteomics, Control, Western Blot, Binding Assay

    Inhibition of protein kinase B (PKB) inhibits the stimulatory effects of MRCKα overexpression on β-casein and mTOR phosphorylation in bovine mammary epithelial cells. Cells were treated with blank (untreated control) or PKB inhibitor (MK2206, 1 μM) and transfected simultaneously with empty vector (control, EV) or MRCKα (OE). After 24 h, cells were lysed, and protein levels were detected by immunoblotting followed by densitometric analysis. All protein levels were first normalized to β-actin and then to Blank + EV group. Values are presented as mean ± SEM for three independent experiments. Different low case letters above columns indicate significant statistical differences ( P < 0.05). P OE , P -value of MRCKα overexpression (OE); P MK , P -value of inhibition of PKB (MK); P OE×MK , P -value of OE × MK interaction. MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; mTOR = mechanistic target of rapamycin.

    Journal: Animal Nutrition

    Article Title: Myotonic dystrophy-related CDC42-binding kinase alpha (MRCKα) mediates methionine- and leucine-stimulated β-casein synthesis in bovine mammary epithelial cells via targeting mTOR

    doi: 10.1016/j.aninu.2025.01.003

    Figure Lengend Snippet: Inhibition of protein kinase B (PKB) inhibits the stimulatory effects of MRCKα overexpression on β-casein and mTOR phosphorylation in bovine mammary epithelial cells. Cells were treated with blank (untreated control) or PKB inhibitor (MK2206, 1 μM) and transfected simultaneously with empty vector (control, EV) or MRCKα (OE). After 24 h, cells were lysed, and protein levels were detected by immunoblotting followed by densitometric analysis. All protein levels were first normalized to β-actin and then to Blank + EV group. Values are presented as mean ± SEM for three independent experiments. Different low case letters above columns indicate significant statistical differences ( P < 0.05). P OE , P -value of MRCKα overexpression (OE); P MK , P -value of inhibition of PKB (MK); P OE×MK , P -value of OE × MK interaction. MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; mTOR = mechanistic target of rapamycin.

    Article Snippet: Rabbit polyclonal anti-human mTOR antibody and rabbit polyclonal anti-human phosphorylated mTOR (Ser 2448 ) antibody were obtained from ImmunoWay Biotechnology Company (Plano, TX, USA).

    Techniques: Inhibition, Over Expression, Phospho-proteomics, Control, Transfection, Plasmid Preparation, Western Blot, Binding Assay

    Silencing of MRCKα inhibits the stimulatory effects of Met and Leu on mRNA abundance of genes related to milk protein synthesis in bovine mammary epithelial cells. Cells were transfected with scrambled siRNA (control, SC) or MRCKα siRNA (SI) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were collected and isolated for RT-qPCR analysis. Values are presented as mean ± SEM for three independent experiments. P AA , P -value of amino acid addition (AA); P SI , P -value of silencing of MRCKα (SI); P AA×SI , P -value of AA × SI interaction. CSN2 = β-casein; CSN1S1 = αS1-casein; CSN3 = κ-casein; LALBA = lactalbumin α; MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; mTOR = mechanistic target of rapamycin; JAK2 = Janus kinase 2; STAT5 = signal transducers and activators of transcription 5.

    Journal: Animal Nutrition

    Article Title: Myotonic dystrophy-related CDC42-binding kinase alpha (MRCKα) mediates methionine- and leucine-stimulated β-casein synthesis in bovine mammary epithelial cells via targeting mTOR

    doi: 10.1016/j.aninu.2025.01.003

    Figure Lengend Snippet: Silencing of MRCKα inhibits the stimulatory effects of Met and Leu on mRNA abundance of genes related to milk protein synthesis in bovine mammary epithelial cells. Cells were transfected with scrambled siRNA (control, SC) or MRCKα siRNA (SI) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were collected and isolated for RT-qPCR analysis. Values are presented as mean ± SEM for three independent experiments. P AA , P -value of amino acid addition (AA); P SI , P -value of silencing of MRCKα (SI); P AA×SI , P -value of AA × SI interaction. CSN2 = β-casein; CSN1S1 = αS1-casein; CSN3 = κ-casein; LALBA = lactalbumin α; MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; mTOR = mechanistic target of rapamycin; JAK2 = Janus kinase 2; STAT5 = signal transducers and activators of transcription 5.

    Article Snippet: Rabbit polyclonal anti-human mTOR antibody and rabbit polyclonal anti-human phosphorylated mTOR (Ser 2448 ) antibody were obtained from ImmunoWay Biotechnology Company (Plano, TX, USA).

    Techniques: Transfection, Control, Isolation, Quantitative RT-PCR, Binding Assay

    Amino acids are sensed by PI3K-MRCKα-PKB signaling pathways to activate mTOR and its downstream signaling, which leads to promotion of β-casein synthesis, SREBP1 and Cyclin D1 expression in BMEC. Besides, the mRNA abundance of CSN1S1 , CSN2 and JAK2 are decreased when MRCKα expression is inhibited. PI3K = phosphatidylinositol 3-kinase; MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; PKB = protein kinase B; mTOR = mechanistic target of rapamycin; CSN1S1 = αS1-casein; CSN2 = β-casein; JAK2 = Janus kinase 2.

    Journal: Animal Nutrition

    Article Title: Myotonic dystrophy-related CDC42-binding kinase alpha (MRCKα) mediates methionine- and leucine-stimulated β-casein synthesis in bovine mammary epithelial cells via targeting mTOR

    doi: 10.1016/j.aninu.2025.01.003

    Figure Lengend Snippet: Amino acids are sensed by PI3K-MRCKα-PKB signaling pathways to activate mTOR and its downstream signaling, which leads to promotion of β-casein synthesis, SREBP1 and Cyclin D1 expression in BMEC. Besides, the mRNA abundance of CSN1S1 , CSN2 and JAK2 are decreased when MRCKα expression is inhibited. PI3K = phosphatidylinositol 3-kinase; MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; PKB = protein kinase B; mTOR = mechanistic target of rapamycin; CSN1S1 = αS1-casein; CSN2 = β-casein; JAK2 = Janus kinase 2.

    Article Snippet: Rabbit polyclonal anti-human mTOR antibody and rabbit polyclonal anti-human phosphorylated mTOR (Ser 2448 ) antibody were obtained from ImmunoWay Biotechnology Company (Plano, TX, USA).

    Techniques: Protein-Protein interactions, Expressing, Binding Assay

    Signaling pathways involved in the genesis of mood cycling (A) Schematic showing comparative analysis of hippocampal gene expression profiles between manic and depressive Syt7 KO mice. GeneM, comparison between the WT mice and the manic Syt7 KO mice. GeneD, comparison between the WT mice and the depressive Syt7 KO mice. (B and C) Heatmap (B) and distribution (C) of genes differentially expressed between GeneM and GeneD. (D) Expression of representative BD-related genes in manic and depressive Syt7 KO mice. (E) Representative significantly enriched KEGG pathways showing bi-directional alterations in the manic and depressive episodes in Syt7 KO mice. (F and G) Schematic (F) and heatmap (G) showing the comparative analysis of transcripts bi-directionally regulated in drug-induced/Syt7 deficiency-induced manic and depressive mice. GeneR, comparison between the WT mice with and without the Ro25 treatment in the dark phase. GeneB, comparison between the WT mice with and without the BMS-536924 treatment in the light phase. (H) Representative significantly enriched KEGG pathways showing bi-directional alterations between the drug-induced/Syt7-deficiency-induced manic and depressive mice. (I) Mapping of representative KEGG pathways for network analysis. (J) Bi-directional regulation of representative genes within featured KEGG pathways in mice with drug-induced/Syt7-deficiency-induced mania or depression. (K and L) Immunoblots (left) and quantitative analysis (right) of mammalian targets of rapamycin (mTOR) (K) and eukaryotic elongation factor 2 (eEF2) (L) phosphorylation in the hippocampus of WT and Syt7 KO mice. n = 3. Student’s t test; ∗ p < 0.05; ∗∗ p < 0.001; error bars, SEM.

    Journal: iScience

    Article Title: Synaptotagmin-7 deficit causes insulin hypoactivity and contributes to behavioral alterations in mice

    doi: 10.1016/j.isci.2025.112354

    Figure Lengend Snippet: Signaling pathways involved in the genesis of mood cycling (A) Schematic showing comparative analysis of hippocampal gene expression profiles between manic and depressive Syt7 KO mice. GeneM, comparison between the WT mice and the manic Syt7 KO mice. GeneD, comparison between the WT mice and the depressive Syt7 KO mice. (B and C) Heatmap (B) and distribution (C) of genes differentially expressed between GeneM and GeneD. (D) Expression of representative BD-related genes in manic and depressive Syt7 KO mice. (E) Representative significantly enriched KEGG pathways showing bi-directional alterations in the manic and depressive episodes in Syt7 KO mice. (F and G) Schematic (F) and heatmap (G) showing the comparative analysis of transcripts bi-directionally regulated in drug-induced/Syt7 deficiency-induced manic and depressive mice. GeneR, comparison between the WT mice with and without the Ro25 treatment in the dark phase. GeneB, comparison between the WT mice with and without the BMS-536924 treatment in the light phase. (H) Representative significantly enriched KEGG pathways showing bi-directional alterations between the drug-induced/Syt7-deficiency-induced manic and depressive mice. (I) Mapping of representative KEGG pathways for network analysis. (J) Bi-directional regulation of representative genes within featured KEGG pathways in mice with drug-induced/Syt7-deficiency-induced mania or depression. (K and L) Immunoblots (left) and quantitative analysis (right) of mammalian targets of rapamycin (mTOR) (K) and eukaryotic elongation factor 2 (eEF2) (L) phosphorylation in the hippocampus of WT and Syt7 KO mice. n = 3. Student’s t test; ∗ p < 0.05; ∗∗ p < 0.001; error bars, SEM.

    Article Snippet: Primary antibodies were as follows: mouse monoclonal anti-Actin antibody (1:5000, Abcam, #ab6276), rabbit polyclonal anti-mTOR antibody (1:500, Cell Signaling, #2972), rabbit polyclonal anti- p -mTOR antibody (1:500, Cell Signaling, #2971), rabbit polyclonal anti-eEF2 antibody (1:1000, Cell Signaling, #2332S), rabbit polyclonal anti- p -eEF2 antibody (1:1000, Cell Signaling, #2331S).

    Techniques: Protein-Protein interactions, Gene Expression, Comparison, Expressing, Western Blot, Phospho-proteomics

    Signaling pathways involved in the genesis of mood cycling (A) Schematic showing comparative analysis of hippocampal gene expression profiles between manic and depressive Syt7 KO mice. GeneM, comparison between the WT mice and the manic Syt7 KO mice. GeneD, comparison between the WT mice and the depressive Syt7 KO mice. (B and C) Heatmap (B) and distribution (C) of genes differentially expressed between GeneM and GeneD. (D) Expression of representative BD-related genes in manic and depressive Syt7 KO mice. (E) Representative significantly enriched KEGG pathways showing bi-directional alterations in the manic and depressive episodes in Syt7 KO mice. (F and G) Schematic (F) and heatmap (G) showing the comparative analysis of transcripts bi-directionally regulated in drug-induced/Syt7 deficiency-induced manic and depressive mice. GeneR, comparison between the WT mice with and without the Ro25 treatment in the dark phase. GeneB, comparison between the WT mice with and without the BMS-536924 treatment in the light phase. (H) Representative significantly enriched KEGG pathways showing bi-directional alterations between the drug-induced/Syt7-deficiency-induced manic and depressive mice. (I) Mapping of representative KEGG pathways for network analysis. (J) Bi-directional regulation of representative genes within featured KEGG pathways in mice with drug-induced/Syt7-deficiency-induced mania or depression. (K and L) Immunoblots (left) and quantitative analysis (right) of mammalian targets of rapamycin (mTOR) (K) and eukaryotic elongation factor 2 (eEF2) (L) phosphorylation in the hippocampus of WT and Syt7 KO mice. n = 3. Student’s t test; ∗ p < 0.05; ∗∗ p < 0.001; error bars, SEM.

    Journal: iScience

    Article Title: Synaptotagmin-7 deficit causes insulin hypoactivity and contributes to behavioral alterations in mice

    doi: 10.1016/j.isci.2025.112354

    Figure Lengend Snippet: Signaling pathways involved in the genesis of mood cycling (A) Schematic showing comparative analysis of hippocampal gene expression profiles between manic and depressive Syt7 KO mice. GeneM, comparison between the WT mice and the manic Syt7 KO mice. GeneD, comparison between the WT mice and the depressive Syt7 KO mice. (B and C) Heatmap (B) and distribution (C) of genes differentially expressed between GeneM and GeneD. (D) Expression of representative BD-related genes in manic and depressive Syt7 KO mice. (E) Representative significantly enriched KEGG pathways showing bi-directional alterations in the manic and depressive episodes in Syt7 KO mice. (F and G) Schematic (F) and heatmap (G) showing the comparative analysis of transcripts bi-directionally regulated in drug-induced/Syt7 deficiency-induced manic and depressive mice. GeneR, comparison between the WT mice with and without the Ro25 treatment in the dark phase. GeneB, comparison between the WT mice with and without the BMS-536924 treatment in the light phase. (H) Representative significantly enriched KEGG pathways showing bi-directional alterations between the drug-induced/Syt7-deficiency-induced manic and depressive mice. (I) Mapping of representative KEGG pathways for network analysis. (J) Bi-directional regulation of representative genes within featured KEGG pathways in mice with drug-induced/Syt7-deficiency-induced mania or depression. (K and L) Immunoblots (left) and quantitative analysis (right) of mammalian targets of rapamycin (mTOR) (K) and eukaryotic elongation factor 2 (eEF2) (L) phosphorylation in the hippocampus of WT and Syt7 KO mice. n = 3. Student’s t test; ∗ p < 0.05; ∗∗ p < 0.001; error bars, SEM.

    Article Snippet: Primary antibodies were as follows: mouse monoclonal anti-Actin antibody (1:5000, Abcam, #ab6276), rabbit polyclonal anti-mTOR antibody (1:500, Cell Signaling, #2972), rabbit polyclonal anti- p -mTOR antibody (1:500, Cell Signaling, #2971), rabbit polyclonal anti-eEF2 antibody (1:1000, Cell Signaling, #2332S), rabbit polyclonal anti- p -eEF2 antibody (1:1000, Cell Signaling, #2331S).

    Techniques: Protein-Protein interactions, Gene Expression, Comparison, Expressing, Western Blot, Phospho-proteomics

    Signaling pathways involved in the genesis of mood cycling (A) Schematic showing comparative analysis of hippocampal gene expression profiles between manic and depressive Syt7 KO mice. GeneM, comparison between the WT mice and the manic Syt7 KO mice. GeneD, comparison between the WT mice and the depressive Syt7 KO mice. (B and C) Heatmap (B) and distribution (C) of genes differentially expressed between GeneM and GeneD. (D) Expression of representative BD-related genes in manic and depressive Syt7 KO mice. (E) Representative significantly enriched KEGG pathways showing bi-directional alterations in the manic and depressive episodes in Syt7 KO mice. (F and G) Schematic (F) and heatmap (G) showing the comparative analysis of transcripts bi-directionally regulated in drug-induced/Syt7 deficiency-induced manic and depressive mice. GeneR, comparison between the WT mice with and without the Ro25 treatment in the dark phase. GeneB, comparison between the WT mice with and without the BMS-536924 treatment in the light phase. (H) Representative significantly enriched KEGG pathways showing bi-directional alterations between the drug-induced/Syt7-deficiency-induced manic and depressive mice. (I) Mapping of representative KEGG pathways for network analysis. (J) Bi-directional regulation of representative genes within featured KEGG pathways in mice with drug-induced/Syt7-deficiency-induced mania or depression. (K and L) Immunoblots (left) and quantitative analysis (right) of mammalian targets of rapamycin (mTOR) (K) and eukaryotic elongation factor 2 (eEF2) (L) phosphorylation in the hippocampus of WT and Syt7 KO mice. n = 3. Student’s t test; ∗ p < 0.05; ∗∗ p < 0.001; error bars, SEM.

    Journal: iScience

    Article Title: Synaptotagmin-7 deficit causes insulin hypoactivity and contributes to behavioral alterations in mice

    doi: 10.1016/j.isci.2025.112354

    Figure Lengend Snippet: Signaling pathways involved in the genesis of mood cycling (A) Schematic showing comparative analysis of hippocampal gene expression profiles between manic and depressive Syt7 KO mice. GeneM, comparison between the WT mice and the manic Syt7 KO mice. GeneD, comparison between the WT mice and the depressive Syt7 KO mice. (B and C) Heatmap (B) and distribution (C) of genes differentially expressed between GeneM and GeneD. (D) Expression of representative BD-related genes in manic and depressive Syt7 KO mice. (E) Representative significantly enriched KEGG pathways showing bi-directional alterations in the manic and depressive episodes in Syt7 KO mice. (F and G) Schematic (F) and heatmap (G) showing the comparative analysis of transcripts bi-directionally regulated in drug-induced/Syt7 deficiency-induced manic and depressive mice. GeneR, comparison between the WT mice with and without the Ro25 treatment in the dark phase. GeneB, comparison between the WT mice with and without the BMS-536924 treatment in the light phase. (H) Representative significantly enriched KEGG pathways showing bi-directional alterations between the drug-induced/Syt7-deficiency-induced manic and depressive mice. (I) Mapping of representative KEGG pathways for network analysis. (J) Bi-directional regulation of representative genes within featured KEGG pathways in mice with drug-induced/Syt7-deficiency-induced mania or depression. (K and L) Immunoblots (left) and quantitative analysis (right) of mammalian targets of rapamycin (mTOR) (K) and eukaryotic elongation factor 2 (eEF2) (L) phosphorylation in the hippocampus of WT and Syt7 KO mice. n = 3. Student’s t test; ∗ p < 0.05; ∗∗ p < 0.001; error bars, SEM.

    Article Snippet: Rabbit polyclonal anti- p -mTOR , Cell Signaling , Cat# 2971; RRID: AB_330970.

    Techniques: Protein-Protein interactions, Gene Expression, Comparison, Expressing, Western Blot, Phospho-proteomics