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antibodies recombinant human adiponectin (R&D Systems)

Name: antibodies recombinant human adiponectin
Brand: R&D Systems
Rating: 94 (34 reviews)

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R&D Systems antibodies recombinant human adiponectin

<t>Adiponectin</t> induces bovine mammary alveolar (MAC-T) cell proliferation. (A) Dose-dependent (0, 1, 5, 10, 20, 50, 100, or 150 ng/mL) effects of adiponectin on MAC-T cell proliferation determined using a BrdU cell proliferation assay. Adiponectin-induced cell proliferation rates are presented as relative percentage (%) changes relative to untreated (0 ng/mL) MAC-T cells (100%). Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. (B) Relative abundance and localization of proliferating cell nuclear antigen (PCNA) protein in adiponectin-treated (20 ng/mL) or untreated MAC-T cells analyzed using immunofluorescence microscopy. Nuclei were counterstained with 4',6-diamidino-2-phenylindole (DAPI; blue; second horizontal panels). Scale bars represent 40 μm (first and third vertical panels) or 20 μm (second and fourth vertical panels). The relative intensity of the immunoreactive PCNA protein is presented in a graph. Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. Asterisks indicate significant effect of treatment (***P < 0.001, **P < 0.01, and *P < 0.05).

Antibodies Recombinant Human Adiponectin, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 34 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Adiponectin: A prosurvival and proproliferation signal that increases bovine mammary epithelial cell numbers and protects them from endoplasmic reticulum stress responses ¹ "

Article Title: Adiponectin: A prosurvival and proproliferation signal that increases bovine mammary epithelial cell numbers and protects them from endoplasmic reticulum stress responses ¹

Journal: Journal of Animal Science

doi: 10.2527/jas2017.1885

Adiponectin induces bovine mammary alveolar (MAC-T) cell proliferation. (A) Dose-dependent (0, 1, 5, 10, 20, 50, 100, or 150 ng/mL) effects of adiponectin on MAC-T cell proliferation determined using a BrdU cell proliferation assay. Adiponectin-induced cell proliferation rates are presented as relative percentage (%) changes relative to untreated (0 ng/mL) MAC-T cells (100%). Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. (B) Relative abundance and localization of proliferating cell nuclear antigen (PCNA) protein in adiponectin-treated (20 ng/mL) or untreated MAC-T cells analyzed using immunofluorescence microscopy. Nuclei were counterstained with 4',6-diamidino-2-phenylindole (DAPI; blue; second horizontal panels). Scale bars represent 40 μm (first and third vertical panels) or 20 μm (second and fourth vertical panels). The relative intensity of the immunoreactive PCNA protein is presented in a graph. Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. Asterisks indicate significant effect of treatment (***P < 0.001, **P < 0.01, and *P < 0.05).

Figure Legend Snippet: Adiponectin induces bovine mammary alveolar (MAC-T) cell proliferation. (A) Dose-dependent (0, 1, 5, 10, 20, 50, 100, or 150 ng/mL) effects of adiponectin on MAC-T cell proliferation determined using a BrdU cell proliferation assay. Adiponectin-induced cell proliferation rates are presented as relative percentage (%) changes relative to untreated (0 ng/mL) MAC-T cells (100%). Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. (B) Relative abundance and localization of proliferating cell nuclear antigen (PCNA) protein in adiponectin-treated (20 ng/mL) or untreated MAC-T cells analyzed using immunofluorescence microscopy. Nuclei were counterstained with 4',6-diamidino-2-phenylindole (DAPI; blue; second horizontal panels). Scale bars represent 40 μm (first and third vertical panels) or 20 μm (second and fourth vertical panels). The relative intensity of the immunoreactive PCNA protein is presented in a graph. Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. Asterisks indicate significant effect of treatment (***P < 0.001, **P < 0.01, and *P < 0.05).

Techniques Used: BrdU Cell Proliferation Assay, Immunofluorescence, Microscopy

Adiponectin regulates bovine mammary alveolar (MAC-T) cell cycle progression. (A) Changes in cell cycle progression of MAC-T cells with increasing doses (0, 1, 5, 10, or 20 ng/mL) of adiponectin investigated using flow cytometry. Each independent experiment was replicated 3 times, and percentages of cell populations in G1, S, and G2/M phases are presented in a bar chart. (B) Histograms showing changes in DNA content of MAC-T cells positive for propidium iodide (PI). Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. (C) Abundance and localization of cyclin D1 protein in adiponectin-treated (20 ng/mL) or untreated MAC-T cells analyzed using immunofluorescence microscopy. Nuclei were counterstained with 4',6-diamidino-2-phenylindole (DAPI; blue; second horizontal panels). Scale bars represent 40 μm (first and third vertical panels) or 20 μm (second and fourth vertical panels). The relative intensity of the immunoreactive cyclin D1 protein is presented in a graph. Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. Asterisks indicate significant effect of treatment (*P < 0.05).

Figure Legend Snippet: Adiponectin regulates bovine mammary alveolar (MAC-T) cell cycle progression. (A) Changes in cell cycle progression of MAC-T cells with increasing doses (0, 1, 5, 10, or 20 ng/mL) of adiponectin investigated using flow cytometry. Each independent experiment was replicated 3 times, and percentages of cell populations in G1, S, and G2/M phases are presented in a bar chart. (B) Histograms showing changes in DNA content of MAC-T cells positive for propidium iodide (PI). Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. (C) Abundance and localization of cyclin D1 protein in adiponectin-treated (20 ng/mL) or untreated MAC-T cells analyzed using immunofluorescence microscopy. Nuclei were counterstained with 4',6-diamidino-2-phenylindole (DAPI; blue; second horizontal panels). Scale bars represent 40 μm (first and third vertical panels) or 20 μm (second and fourth vertical panels). The relative intensity of the immunoreactive cyclin D1 protein is presented in a graph. Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. Asterisks indicate significant effect of treatment (*P < 0.05).

Techniques Used: Flow Cytometry, Immunofluorescence, Microscopy

Adiponectin activates phosphoinositide 3-kinase (PI3K) and extracellular signal-regulated kinases 1 and 2 (ERK1/2) mitogen-activated protein kinase (MAPK) ERK1/2 MAPK signaling proteins in MAC-T cells. (A) Phosphorylation of serine/threonine protein kinase (AKT), (B) 70 kDa ribosomal S6 kinase (P70S6K), (C) ribosomal protein S6 (S6), (D) ERK1/2, (E) 90 kDa ribosomal S6 kinase (P90S6K), and (F) cyclin D1 in response to increasing concentrations of adiponectin (0, 1, 5, 10, or 20 ng/mL) determined using Western blot. Images were captured to calculate normalized values for p-proteins relative to t-proteins. Bar graphs above blot images show abundance of p-proteins normalized to the abundance of t-proteins; values are presented as fold change relative to untreated (0 ng/mL) control MAC-T cells. Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM of relative band intensities. Asterisks indicate significant differences compared to control cells (***P < 0.001, **P < 0.01, and *P < 0.05).

Figure Legend Snippet: Adiponectin activates phosphoinositide 3-kinase (PI3K) and extracellular signal-regulated kinases 1 and 2 (ERK1/2) mitogen-activated protein kinase (MAPK) ERK1/2 MAPK signaling proteins in MAC-T cells. (A) Phosphorylation of serine/threonine protein kinase (AKT), (B) 70 kDa ribosomal S6 kinase (P70S6K), (C) ribosomal protein S6 (S6), (D) ERK1/2, (E) 90 kDa ribosomal S6 kinase (P90S6K), and (F) cyclin D1 in response to increasing concentrations of adiponectin (0, 1, 5, 10, or 20 ng/mL) determined using Western blot. Images were captured to calculate normalized values for p-proteins relative to t-proteins. Bar graphs above blot images show abundance of p-proteins normalized to the abundance of t-proteins; values are presented as fold change relative to untreated (0 ng/mL) control MAC-T cells. Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM of relative band intensities. Asterisks indicate significant differences compared to control cells (***P < 0.001, **P < 0.01, and *P < 0.05).

Techniques Used: Phospho-proteomics, Western Blot, Control

Adiponectin-induced signaling pathways activate common downstream molecules. Effects of inhibition of phosphoinositide 3-kinase (PI3K) and extracellular signal-regulated kinases 1 and 2 (ERK1/2) on activation of their downstream signaling proteins by adiponectin were determined using Western blot. Abundance of phosphorylated (A) AKTserine/threonine protein kinase (AKT) (B) 70 kDa ribosomal S6 kinase (P70S6K), (C) ribosomal protein S6 (S6), (D) ERK1/2, (E) 90 kDa ribosomal S6 kinase (P90S6K), and (F) cyclin D1 analyzed in MAC-T cells treated with adiponectin (20 ng/mL) plus wortmannin (1 μM, PI3K inhibitor) or U0126 (20 μM, ERK1/2 inhibitor). After preincubation with each pharmacological inhibitor for 2 h, cells were treated with 20 ng/mL adiponectin. Bar graphs above blot images show abundance of p-proteins normalized to abundance of t-proteins; values are presented as fold change relative to control (no adiponectin and no inhibitor), which was given a value of 1. Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. Asterisks indicate significant differences between 2 groups (**P < 0.01, and *P < 0.05).

Figure Legend Snippet: Adiponectin-induced signaling pathways activate common downstream molecules. Effects of inhibition of phosphoinositide 3-kinase (PI3K) and extracellular signal-regulated kinases 1 and 2 (ERK1/2) on activation of their downstream signaling proteins by adiponectin were determined using Western blot. Abundance of phosphorylated (A) AKTserine/threonine protein kinase (AKT) (B) 70 kDa ribosomal S6 kinase (P70S6K), (C) ribosomal protein S6 (S6), (D) ERK1/2, (E) 90 kDa ribosomal S6 kinase (P90S6K), and (F) cyclin D1 analyzed in MAC-T cells treated with adiponectin (20 ng/mL) plus wortmannin (1 μM, PI3K inhibitor) or U0126 (20 μM, ERK1/2 inhibitor). After preincubation with each pharmacological inhibitor for 2 h, cells were treated with 20 ng/mL adiponectin. Bar graphs above blot images show abundance of p-proteins normalized to abundance of t-proteins; values are presented as fold change relative to control (no adiponectin and no inhibitor), which was given a value of 1. Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. Asterisks indicate significant differences between 2 groups (**P < 0.01, and *P < 0.05).

Techniques Used: Protein-Protein interactions, Inhibition, Activation Assay, Western Blot, Control

Adiponectin-induced signaling pathways control the functional effects of adiponectin to induce cell proliferation. Effect of phosphoinositide 3-kinase (PI3K) and extracellular signal-regulated kinases 1 and 2 (ERK1/2) inhibition on adiponectin-induced MAC-T cell proliferation determined using a bromodeoxyuridine (BrdU) cell proliferation assay. Serum-starved MAC-T cells were incubated with adiponectin and either wortmannin or U0126 for 48 h. Cell proliferation rates are presented as relative percentage changes relative to untreated control cells (100%). Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. Asterisks indicate significant differences between 2 groups (***P < 0.001 and **P < 0.01).

Figure Legend Snippet: Adiponectin-induced signaling pathways control the functional effects of adiponectin to induce cell proliferation. Effect of phosphoinositide 3-kinase (PI3K) and extracellular signal-regulated kinases 1 and 2 (ERK1/2) inhibition on adiponectin-induced MAC-T cell proliferation determined using a bromodeoxyuridine (BrdU) cell proliferation assay. Serum-starved MAC-T cells were incubated with adiponectin and either wortmannin or U0126 for 48 h. Cell proliferation rates are presented as relative percentage changes relative to untreated control cells (100%). Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. Asterisks indicate significant differences between 2 groups (***P < 0.001 and **P < 0.01).

Techniques Used: Protein-Protein interactions, Control, Functional Assay, Inhibition, BrdU Cell Proliferation Assay, Incubation

Adiponectin attenuates tunicamycin-induced endoplasmic reticulum (ER) stress and cell proliferation inhibition. (A) MAC-T cells were treated with tunicamycin (0.25 µg/mL) to induce ER stress. Inhibitory effects of tunicamycin and adiponectin alone or in combination on MAC-T cell proliferation analyzed using a bromodeoxyuridine (BrdU) cell proliferation assay. Cell proliferation rates are presented as relative percentage changes relative to control cells (100%). Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. (B)–(G) Expression and activation of ER stress-related proteins in response to tunicamycin and adiponectin alone or in combination were analyzed by Western blot. The tunicamycin-induced increase in inositol-requiring protein 1α (IRE1α), activating transcription factor 6α (ATF6α), p-posphorylated (p)-protein kinase RNA-like ER kinase (PERK), p-p-eukaryotic translation initiator factor 2α (eIF2α) glucose-regulated protein 78 (GRP78), and growth arrest- and DNA damage-inducible gene 153 (GADD153) was reduced in the presence of adiponectin. Bar graphs above blot images show the abundance of proteins of interest normalized to t-proteins or α-tubulin (TUBA); values are presented as fold change relative to control MAC-T cells, which were given a value of 1. Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM of relative band intensities. Asterisks indicate significant differences between 2 groups (***P < 0.001, **P < 0.01, and *P < 0.05).

Figure Legend Snippet: Adiponectin attenuates tunicamycin-induced endoplasmic reticulum (ER) stress and cell proliferation inhibition. (A) MAC-T cells were treated with tunicamycin (0.25 µg/mL) to induce ER stress. Inhibitory effects of tunicamycin and adiponectin alone or in combination on MAC-T cell proliferation analyzed using a bromodeoxyuridine (BrdU) cell proliferation assay. Cell proliferation rates are presented as relative percentage changes relative to control cells (100%). Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. (B)–(G) Expression and activation of ER stress-related proteins in response to tunicamycin and adiponectin alone or in combination were analyzed by Western blot. The tunicamycin-induced increase in inositol-requiring protein 1α (IRE1α), activating transcription factor 6α (ATF6α), p-posphorylated (p)-protein kinase RNA-like ER kinase (PERK), p-p-eukaryotic translation initiator factor 2α (eIF2α) glucose-regulated protein 78 (GRP78), and growth arrest- and DNA damage-inducible gene 153 (GADD153) was reduced in the presence of adiponectin. Bar graphs above blot images show the abundance of proteins of interest normalized to t-proteins or α-tubulin (TUBA); values are presented as fold change relative to control MAC-T cells, which were given a value of 1. Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM of relative band intensities. Asterisks indicate significant differences between 2 groups (***P < 0.001, **P < 0.01, and *P < 0.05).

Techniques Used: Inhibition, BrdU Cell Proliferation Assay, Control, Expressing, Activation Assay, Western Blot

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Journal: Journal of Animal Science

Article Title: Adiponectin: A prosurvival and proproliferation signal that increases bovine mammary epithelial cell numbers and protects them from endoplasmic reticulum stress responses ¹

doi: 10.2527/jas2017.1885

Figure Lengend Snippet: Adiponectin induces bovine mammary alveolar (MAC-T) cell proliferation. (A) Dose-dependent (0, 1, 5, 10, 20, 50, 100, or 150 ng/mL) effects of adiponectin on MAC-T cell proliferation determined using a BrdU cell proliferation assay. Adiponectin-induced cell proliferation rates are presented as relative percentage (%) changes relative to untreated (0 ng/mL) MAC-T cells (100%). Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. (B) Relative abundance and localization of proliferating cell nuclear antigen (PCNA) protein in adiponectin-treated (20 ng/mL) or untreated MAC-T cells analyzed using immunofluorescence microscopy. Nuclei were counterstained with 4',6-diamidino-2-phenylindole (DAPI; blue; second horizontal panels). Scale bars represent 40 μm (first and third vertical panels) or 20 μm (second and fourth vertical panels). The relative intensity of the immunoreactive PCNA protein is presented in a graph. Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. Asterisks indicate significant effect of treatment (***P < 0.001, **P < 0.01, and *P < 0.05).

Article Snippet: Reagents and Antibodies Recombinant human adiponectin (catalog number 1065-AP) was purchased from R&D Systems (Minneapolis, MN).

Techniques: BrdU Cell Proliferation Assay, Immunofluorescence, Microscopy

Journal: Journal of Animal Science

Article Title: Adiponectin: A prosurvival and proproliferation signal that increases bovine mammary epithelial cell numbers and protects them from endoplasmic reticulum stress responses ¹

doi: 10.2527/jas2017.1885

Figure Lengend Snippet: Adiponectin regulates bovine mammary alveolar (MAC-T) cell cycle progression. (A) Changes in cell cycle progression of MAC-T cells with increasing doses (0, 1, 5, 10, or 20 ng/mL) of adiponectin investigated using flow cytometry. Each independent experiment was replicated 3 times, and percentages of cell populations in G1, S, and G2/M phases are presented in a bar chart. (B) Histograms showing changes in DNA content of MAC-T cells positive for propidium iodide (PI). Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. (C) Abundance and localization of cyclin D1 protein in adiponectin-treated (20 ng/mL) or untreated MAC-T cells analyzed using immunofluorescence microscopy. Nuclei were counterstained with 4',6-diamidino-2-phenylindole (DAPI; blue; second horizontal panels). Scale bars represent 40 μm (first and third vertical panels) or 20 μm (second and fourth vertical panels). The relative intensity of the immunoreactive cyclin D1 protein is presented in a graph. Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. Asterisks indicate significant effect of treatment (*P < 0.05).

Article Snippet: Reagents and Antibodies Recombinant human adiponectin (catalog number 1065-AP) was purchased from R&D Systems (Minneapolis, MN).

Techniques: Flow Cytometry, Immunofluorescence, Microscopy

Journal: Journal of Animal Science

Article Title: Adiponectin: A prosurvival and proproliferation signal that increases bovine mammary epithelial cell numbers and protects them from endoplasmic reticulum stress responses ¹

doi: 10.2527/jas2017.1885

Figure Lengend Snippet: Adiponectin activates phosphoinositide 3-kinase (PI3K) and extracellular signal-regulated kinases 1 and 2 (ERK1/2) mitogen-activated protein kinase (MAPK) ERK1/2 MAPK signaling proteins in MAC-T cells. (A) Phosphorylation of serine/threonine protein kinase (AKT), (B) 70 kDa ribosomal S6 kinase (P70S6K), (C) ribosomal protein S6 (S6), (D) ERK1/2, (E) 90 kDa ribosomal S6 kinase (P90S6K), and (F) cyclin D1 in response to increasing concentrations of adiponectin (0, 1, 5, 10, or 20 ng/mL) determined using Western blot. Images were captured to calculate normalized values for p-proteins relative to t-proteins. Bar graphs above blot images show abundance of p-proteins normalized to the abundance of t-proteins; values are presented as fold change relative to untreated (0 ng/mL) control MAC-T cells. Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM of relative band intensities. Asterisks indicate significant differences compared to control cells (***P < 0.001, **P < 0.01, and *P < 0.05).

Article Snippet: Reagents and Antibodies Recombinant human adiponectin (catalog number 1065-AP) was purchased from R&D Systems (Minneapolis, MN).

Techniques: Phospho-proteomics, Western Blot, Control

Journal: Journal of Animal Science

Article Title: Adiponectin: A prosurvival and proproliferation signal that increases bovine mammary epithelial cell numbers and protects them from endoplasmic reticulum stress responses ¹

doi: 10.2527/jas2017.1885

Figure Lengend Snippet: Adiponectin-induced signaling pathways activate common downstream molecules. Effects of inhibition of phosphoinositide 3-kinase (PI3K) and extracellular signal-regulated kinases 1 and 2 (ERK1/2) on activation of their downstream signaling proteins by adiponectin were determined using Western blot. Abundance of phosphorylated (A) AKTserine/threonine protein kinase (AKT) (B) 70 kDa ribosomal S6 kinase (P70S6K), (C) ribosomal protein S6 (S6), (D) ERK1/2, (E) 90 kDa ribosomal S6 kinase (P90S6K), and (F) cyclin D1 analyzed in MAC-T cells treated with adiponectin (20 ng/mL) plus wortmannin (1 μM, PI3K inhibitor) or U0126 (20 μM, ERK1/2 inhibitor). After preincubation with each pharmacological inhibitor for 2 h, cells were treated with 20 ng/mL adiponectin. Bar graphs above blot images show abundance of p-proteins normalized to abundance of t-proteins; values are presented as fold change relative to control (no adiponectin and no inhibitor), which was given a value of 1. Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. Asterisks indicate significant differences between 2 groups (**P < 0.01, and *P < 0.05).

Article Snippet: Reagents and Antibodies Recombinant human adiponectin (catalog number 1065-AP) was purchased from R&D Systems (Minneapolis, MN).

Techniques: Protein-Protein interactions, Inhibition, Activation Assay, Western Blot, Control

Journal: Journal of Animal Science

Article Title: Adiponectin: A prosurvival and proproliferation signal that increases bovine mammary epithelial cell numbers and protects them from endoplasmic reticulum stress responses ¹

doi: 10.2527/jas2017.1885

Figure Lengend Snippet: Adiponectin-induced signaling pathways control the functional effects of adiponectin to induce cell proliferation. Effect of phosphoinositide 3-kinase (PI3K) and extracellular signal-regulated kinases 1 and 2 (ERK1/2) inhibition on adiponectin-induced MAC-T cell proliferation determined using a bromodeoxyuridine (BrdU) cell proliferation assay. Serum-starved MAC-T cells were incubated with adiponectin and either wortmannin or U0126 for 48 h. Cell proliferation rates are presented as relative percentage changes relative to untreated control cells (100%). Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. Asterisks indicate significant differences between 2 groups (***P < 0.001 and **P < 0.01).

Article Snippet: Reagents and Antibodies Recombinant human adiponectin (catalog number 1065-AP) was purchased from R&D Systems (Minneapolis, MN).

Techniques: Protein-Protein interactions, Control, Functional Assay, Inhibition, BrdU Cell Proliferation Assay, Incubation

Journal: Journal of Animal Science

Article Title: Adiponectin: A prosurvival and proproliferation signal that increases bovine mammary epithelial cell numbers and protects them from endoplasmic reticulum stress responses ¹

doi: 10.2527/jas2017.1885

Figure Lengend Snippet: Adiponectin attenuates tunicamycin-induced endoplasmic reticulum (ER) stress and cell proliferation inhibition. (A) MAC-T cells were treated with tunicamycin (0.25 µg/mL) to induce ER stress. Inhibitory effects of tunicamycin and adiponectin alone or in combination on MAC-T cell proliferation analyzed using a bromodeoxyuridine (BrdU) cell proliferation assay. Cell proliferation rates are presented as relative percentage changes relative to control cells (100%). Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM. (B)–(G) Expression and activation of ER stress-related proteins in response to tunicamycin and adiponectin alone or in combination were analyzed by Western blot. The tunicamycin-induced increase in inositol-requiring protein 1α (IRE1α), activating transcription factor 6α (ATF6α), p-posphorylated (p)-protein kinase RNA-like ER kinase (PERK), p-p-eukaryotic translation initiator factor 2α (eIF2α) glucose-regulated protein 78 (GRP78), and growth arrest- and DNA damage-inducible gene 153 (GADD153) was reduced in the presence of adiponectin. Bar graphs above blot images show the abundance of proteins of interest normalized to t-proteins or α-tubulin (TUBA); values are presented as fold change relative to control MAC-T cells, which were given a value of 1. Pooled data from 3 independent experiments (n = 3) performed in triplicate are shown as mean ± SEM of relative band intensities. Asterisks indicate significant differences between 2 groups (***P < 0.001, **P < 0.01, and *P < 0.05).

Article Snippet: Reagents and Antibodies Recombinant human adiponectin (catalog number 1065-AP) was purchased from R&D Systems (Minneapolis, MN).

Techniques: Inhibition, BrdU Cell Proliferation Assay, Control, Expressing, Activation Assay, Western Blot

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