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αvβ3 blocking antibody (Santa Cruz Biotechnology)

Name: αvβ3 blocking antibody
Brand: Santa Cruz Biotechnology
Rating: 93 (117 reviews)

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Santa Cruz Biotechnology αvβ3 blocking antibody

JAK/STAT pathway’s protein phosphorylation in differentiated PC-12 cells in hypoxia. Densitometric analysis (arbitrary units of spot signal densities normalized to the positive control signals) showing the effect of 10 nM T3 and <t>αvβ3-Ab</t> integrin (µg/ml). Results represent the mean ± SEM of duplicate samples from two independent experiments. A significant level is defined as * p < 0.05 vs control and # p < 0.05 to T3.

αvβ3 Blocking Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 117 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/αvβ3 blocking antibody/product/Santa Cruz Biotechnology
Average 93 stars, based on 117 article reviews

αvβ3 blocking antibody - by Bioz Stars, 2026-02

93/100 stars

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1) Product Images from "Thyroid hormone T3 induces Fyn modification and modulates palmitoyltransferase gene expression through αvβ3 integrin receptor in PC12 cells during hypoxia"

Article Title: Thyroid hormone T3 induces Fyn modification and modulates palmitoyltransferase gene expression through αvβ3 integrin receptor in PC12 cells during hypoxia

Journal: Translational Neuroscience

doi: 10.1515/tnsci-2022-0347

Figure Legend Snippet: JAK/STAT pathway’s protein phosphorylation in differentiated PC-12 cells in hypoxia. Densitometric analysis (arbitrary units of spot signal densities normalized to the positive control signals) showing the effect of 10 nM T3 and αvβ3-Ab integrin (µg/ml). Results represent the mean ± SEM of duplicate samples from two independent experiments. A significant level is defined as * p < 0.05 vs control and # p < 0.05 to T3.

Techniques Used: Phospho-proteomics, Positive Control, Control

The action of T3 on the phosphorylation and palmitoylation of Fyn A. The ratio of palmitoylated and non-palmitoylated Fyn and p-Fyn forms. The palm-Fyn/Fyn ratio in differentiated PC-12 cells exposed to 10 nM T3 and µg/ml αvβ3-Ab integrin during 1 h of hypoxia. (a) Immunoblotting image of palm-Fyn and total Fyn; the palm-p-Fyn/p-Fyn ratio in differentiated PC-12 cells exposed to 10 nM T3 and αvβ3-Ab integrin (µg/ml) during 1 h of hypoxia. (b) Immunoblotting image of palm-p-Fyn and total p-Fyn; plot of the ratio of palm-p-Fyn to total p-Fyn. Plot of the ratio of palm-Fyn to total Fyn. Results represent the mean ± SEM of duplicate samples from two independent experiments. A significant level was defined as * p < 0.05 vs control and # p < 0.05 to T3.

Figure Legend Snippet: The action of T3 on the phosphorylation and palmitoylation of Fyn A. The ratio of palmitoylated and non-palmitoylated Fyn and p-Fyn forms. The palm-Fyn/Fyn ratio in differentiated PC-12 cells exposed to 10 nM T3 and µg/ml αvβ3-Ab integrin during 1 h of hypoxia. (a) Immunoblotting image of palm-Fyn and total Fyn; the palm-p-Fyn/p-Fyn ratio in differentiated PC-12 cells exposed to 10 nM T3 and αvβ3-Ab integrin (µg/ml) during 1 h of hypoxia. (b) Immunoblotting image of palm-p-Fyn and total p-Fyn; plot of the ratio of palm-p-Fyn to total p-Fyn. Plot of the ratio of palm-Fyn to total Fyn. Results represent the mean ± SEM of duplicate samples from two independent experiments. A significant level was defined as * p < 0.05 vs control and # p < 0.05 to T3.

Techniques Used: Phospho-proteomics, Western Blot, Control

TH supplementation of hypoxic cells increases the proportion of phosphorylated to non-phosphorylated forms of palmitoylated Fyn kinase in differentiated PC-12 cells exposed to 10 nM T3 and αvβ3-Ab (µg/ml) integrin during 1 h hypoxia. Results represent the mean ± SEM of duplicate samples from two independent experiments. A significant level was defined as * p < 0.05. vs control and # p < 0.05. to T3.

Figure Legend Snippet: TH supplementation of hypoxic cells increases the proportion of phosphorylated to non-phosphorylated forms of palmitoylated Fyn kinase in differentiated PC-12 cells exposed to 10 nM T3 and αvβ3-Ab (µg/ml) integrin during 1 h hypoxia. Results represent the mean ± SEM of duplicate samples from two independent experiments. A significant level was defined as * p < 0.05. vs control and # p < 0.05. to T3.

Techniques Used: Control

RT-qPCR analysis of genes ZDHHC2, ZDHHC3, ZDHHC8, ZDHHC9, and ZDHHC16 showing the effect of 10 nM T3 and αvβ3-Ab integrin (µg/ml) in differentiated PC-12 cells exposed to 1 h hypoxia

Figure Legend Snippet: RT-qPCR analysis of genes ZDHHC2, ZDHHC3, ZDHHC8, ZDHHC9, and ZDHHC16 showing the effect of 10 nM T3 and αvβ3-Ab integrin (µg/ml) in differentiated PC-12 cells exposed to 1 h hypoxia

Techniques Used: Control

The palmitoyltransferase gene expression levels of (a) ZDHHC2 and (b) ZDHHC9It were determined using the RT-PCR method in differentiated PC-12 cells exposed to 10 nM T3 and αvβ3-Ab integrin (µg/ml) during 1 h hypoxia. Results represent the mean ± SEM of duplicate samples from three independent experiments. A significant level was defined as * p < 0.05 vs control and # p < 0.05 to T3.

Figure Legend Snippet: The palmitoyltransferase gene expression levels of (a) ZDHHC2 and (b) ZDHHC9It were determined using the RT-PCR method in differentiated PC-12 cells exposed to 10 nM T3 and αvβ3-Ab integrin (µg/ml) during 1 h hypoxia. Results represent the mean ± SEM of duplicate samples from three independent experiments. A significant level was defined as * p < 0.05 vs control and # p < 0.05 to T3.

Techniques Used: Gene Expression, Reverse Transcription Polymerase Chain Reaction, Control

Image Search Results

Journal: Translational Neuroscience

Article Title: Thyroid hormone T3 induces Fyn modification and modulates palmitoyltransferase gene expression through αvβ3 integrin receptor in PC12 cells during hypoxia

doi: 10.1515/tnsci-2022-0347

Figure Lengend Snippet: JAK/STAT pathway’s protein phosphorylation in differentiated PC-12 cells in hypoxia. Densitometric analysis (arbitrary units of spot signal densities normalized to the positive control signals) showing the effect of 10 nM T3 and αvβ3-Ab integrin (µg/ml). Results represent the mean ± SEM of duplicate samples from two independent experiments. A significant level is defined as * p < 0.05 vs control and # p < 0.05 to T3.

Article Snippet: Differentiated cells were incubated with 10 nM T3 and αvβ3 blocking antibody (αvβ3-Ab, 1 μg/ml; sc-7312, Santa Cruz Biotechnology).

Techniques: Phospho-proteomics, Positive Control, Control

Journal: Translational Neuroscience

Article Title: Thyroid hormone T3 induces Fyn modification and modulates palmitoyltransferase gene expression through αvβ3 integrin receptor in PC12 cells during hypoxia

doi: 10.1515/tnsci-2022-0347

Figure Lengend Snippet: The action of T3 on the phosphorylation and palmitoylation of Fyn A. The ratio of palmitoylated and non-palmitoylated Fyn and p-Fyn forms. The palm-Fyn/Fyn ratio in differentiated PC-12 cells exposed to 10 nM T3 and µg/ml αvβ3-Ab integrin during 1 h of hypoxia. (a) Immunoblotting image of palm-Fyn and total Fyn; the palm-p-Fyn/p-Fyn ratio in differentiated PC-12 cells exposed to 10 nM T3 and αvβ3-Ab integrin (µg/ml) during 1 h of hypoxia. (b) Immunoblotting image of palm-p-Fyn and total p-Fyn; plot of the ratio of palm-p-Fyn to total p-Fyn. Plot of the ratio of palm-Fyn to total Fyn. Results represent the mean ± SEM of duplicate samples from two independent experiments. A significant level was defined as * p < 0.05 vs control and # p < 0.05 to T3.

Article Snippet: Differentiated cells were incubated with 10 nM T3 and αvβ3 blocking antibody (αvβ3-Ab, 1 μg/ml; sc-7312, Santa Cruz Biotechnology).

Techniques: Phospho-proteomics, Western Blot, Control

Journal: Translational Neuroscience

Article Title: Thyroid hormone T3 induces Fyn modification and modulates palmitoyltransferase gene expression through αvβ3 integrin receptor in PC12 cells during hypoxia

doi: 10.1515/tnsci-2022-0347

Figure Lengend Snippet: TH supplementation of hypoxic cells increases the proportion of phosphorylated to non-phosphorylated forms of palmitoylated Fyn kinase in differentiated PC-12 cells exposed to 10 nM T3 and αvβ3-Ab (µg/ml) integrin during 1 h hypoxia. Results represent the mean ± SEM of duplicate samples from two independent experiments. A significant level was defined as * p < 0.05. vs control and # p < 0.05. to T3.

Article Snippet: Differentiated cells were incubated with 10 nM T3 and αvβ3 blocking antibody (αvβ3-Ab, 1 μg/ml; sc-7312, Santa Cruz Biotechnology).

Techniques: Control

Journal: Translational Neuroscience

Article Title: Thyroid hormone T3 induces Fyn modification and modulates palmitoyltransferase gene expression through αvβ3 integrin receptor in PC12 cells during hypoxia

doi: 10.1515/tnsci-2022-0347

Figure Lengend Snippet: RT-qPCR analysis of genes ZDHHC2, ZDHHC3, ZDHHC8, ZDHHC9, and ZDHHC16 showing the effect of 10 nM T3 and αvβ3-Ab integrin (µg/ml) in differentiated PC-12 cells exposed to 1 h hypoxia

Article Snippet: Differentiated cells were incubated with 10 nM T3 and αvβ3 blocking antibody (αvβ3-Ab, 1 μg/ml; sc-7312, Santa Cruz Biotechnology).

Techniques: Control

Journal: Translational Neuroscience

Article Title: Thyroid hormone T3 induces Fyn modification and modulates palmitoyltransferase gene expression through αvβ3 integrin receptor in PC12 cells during hypoxia

doi: 10.1515/tnsci-2022-0347

Figure Lengend Snippet: The palmitoyltransferase gene expression levels of (a) ZDHHC2 and (b) ZDHHC9It were determined using the RT-PCR method in differentiated PC-12 cells exposed to 10 nM T3 and αvβ3-Ab integrin (µg/ml) during 1 h hypoxia. Results represent the mean ± SEM of duplicate samples from three independent experiments. A significant level was defined as * p < 0.05 vs control and # p < 0.05 to T3.

Article Snippet: Differentiated cells were incubated with 10 nM T3 and αvβ3 blocking antibody (αvβ3-Ab, 1 μg/ml; sc-7312, Santa Cruz Biotechnology).

Techniques: Gene Expression, Reverse Transcription Polymerase Chain Reaction, Control

Immunoblotting analysis. A. Ratio of cofilin1/p-cofilin1 in the differentiated PC-12 cells with/without 10 nM T3 and αvβ3 antibody (αvβ3-Ab, 1 µg/ ml) during 1 hour hypoxia. Results of triplicate experiments are shown as mean ± SEM. Error-bars denote one standard error of the mean and asterisk and hash indicate a statistically significant difference. *; P=0.0045 vs. control and #; P=0.0058 vs. T3 treatment. B. Western blots of cofilin1 p-cofilin1, and beta-actin (loading control) in differentiated PC-12 cells with/without 10 nM T3 hormone and αvβ3 antibody (αvβ3-Ab, 1 µg/ml) during one-hour hypoxia. Bands were quantified by Image J.

Journal: Cell Journal (Yakhteh)

Article Title: 3,5,3'-Triiodo-L-Thyronine Regulates Actin Cytoskeleton Dynamic in The Differentiated PC-12 Cells during Hypoxia through An αvβ3 Integrin

doi: 10.22074/CELLJ.2022.557501.1059.

Figure Lengend Snippet: Immunoblotting analysis. A. Ratio of cofilin1/p-cofilin1 in the differentiated PC-12 cells with/without 10 nM T3 and αvβ3 antibody (αvβ3-Ab, 1 µg/ ml) during 1 hour hypoxia. Results of triplicate experiments are shown as mean ± SEM. Error-bars denote one standard error of the mean and asterisk and hash indicate a statistically significant difference. *; P=0.0045 vs. control and #; P=0.0058 vs. T3 treatment. B. Western blots of cofilin1 p-cofilin1, and beta-actin (loading control) in differentiated PC-12 cells with/without 10 nM T3 hormone and αvβ3 antibody (αvβ3-Ab, 1 µg/ml) during one-hour hypoxia. Bands were quantified by Image J.

Article Snippet: Differentiated PC-12 cells (5×10 6 cells per sample) were treated with T3 and αvβ3 integrin blocking antibody 1 μg/mL (23C6; sc-7312, Santa Cruz, USA), and incubated for 1 hour under hypoxic condition.

Techniques: Western Blot, Control

Analysis of the cytotoxicity in differentiated PC-12 cells under hypoxia with/without 10 nM T3 hormone and αvβ3 antibody (αvβ3-Ab, 1 µg/ml) during 1 hour hypoxia by the LDH test as described in “Materials and Methods. Results of triplicate experiments are shown as mean ± SEM. Error-bars denote one standard error of the mean and asterisk and hash indicate a statistically significant difference. LDH; Lactate dehydrogenase, *; P=0.0050 vs. control and #; P=0.0153 vs. T3 hormone treatment.

Journal: Cell Journal (Yakhteh)

Article Title: 3,5,3'-Triiodo-L-Thyronine Regulates Actin Cytoskeleton Dynamic in The Differentiated PC-12 Cells during Hypoxia through An αvβ3 Integrin

doi: 10.22074/CELLJ.2022.557501.1059.

Figure Lengend Snippet: Analysis of the cytotoxicity in differentiated PC-12 cells under hypoxia with/without 10 nM T3 hormone and αvβ3 antibody (αvβ3-Ab, 1 µg/ml) during 1 hour hypoxia by the LDH test as described in “Materials and Methods. Results of triplicate experiments are shown as mean ± SEM. Error-bars denote one standard error of the mean and asterisk and hash indicate a statistically significant difference. LDH; Lactate dehydrogenase, *; P=0.0050 vs. control and #; P=0.0153 vs. T3 hormone treatment.

Techniques: Control

Immunoblotting analysis. A. Diagram Analysis of the G- and F-actin content in differentiated PC-12 cells under hypoxia with/without 10 nM T3 hormone and αvβ3 antibody (αvβ3-Ab, 1 µg/ml) during 1 hour hypoxia. Results of triplicate experiments are shown as mean ± SEM. Error-bars denote one standard error of the mean and asterisk and hash indicate a statistically significant difference. *; P=0.0010 vs. control and #; P=0.0020 vs. T3 hormone treatment. B. Western blots of the G and F actins in the differentiated PC-12 cells with/without 10 nM T3 hormone treatment and αvβ3 antibody (αvβ3-Ab, 1 µg/ml) during 1 hour hypoxia. Bands were quantified by Image J.

Journal: Cell Journal (Yakhteh)

Article Title: 3,5,3'-Triiodo-L-Thyronine Regulates Actin Cytoskeleton Dynamic in The Differentiated PC-12 Cells during Hypoxia through An αvβ3 Integrin

doi: 10.22074/CELLJ.2022.557501.1059.

Figure Lengend Snippet: Immunoblotting analysis. A. Diagram Analysis of the G- and F-actin content in differentiated PC-12 cells under hypoxia with/without 10 nM T3 hormone and αvβ3 antibody (αvβ3-Ab, 1 µg/ml) during 1 hour hypoxia. Results of triplicate experiments are shown as mean ± SEM. Error-bars denote one standard error of the mean and asterisk and hash indicate a statistically significant difference. *; P=0.0010 vs. control and #; P=0.0020 vs. T3 hormone treatment. B. Western blots of the G and F actins in the differentiated PC-12 cells with/without 10 nM T3 hormone treatment and αvβ3 antibody (αvβ3-Ab, 1 µg/ml) during 1 hour hypoxia. Bands were quantified by Image J.

Techniques: Western Blot, Control

Immunoblotting analysis. A. Diagram of the p-Fyn/Fyn ratio in differentiated PC-12 cells with/without 10 nM T3 and αvβ3 antibody (αvβ3-Ab, one µg/ml) during 1 hour hypoxia. Results of triplicate experiments are shown as mean ± SEM. Error-bars denote one standard error of the mean and asterisk and hash indicate a statistically significant difference. *; P=0.0010 vs. control and #; P=0.0138 vs. T3 treatment. B. Western blots of p-Fyn, Fyn and betaactin (loading control) in the differentiated PC-12 cells with/without 10 nM T3 hormone and αvβ3 antibody (αvβ3-Ab, 1 µg/ml) during one-hour hypoxia. Bands were quantified by Image J.

Journal: Cell Journal (Yakhteh)

Article Title: 3,5,3'-Triiodo-L-Thyronine Regulates Actin Cytoskeleton Dynamic in The Differentiated PC-12 Cells during Hypoxia through An αvβ3 Integrin

doi: 10.22074/CELLJ.2022.557501.1059.

Figure Lengend Snippet: Immunoblotting analysis. A. Diagram of the p-Fyn/Fyn ratio in differentiated PC-12 cells with/without 10 nM T3 and αvβ3 antibody (αvβ3-Ab, one µg/ml) during 1 hour hypoxia. Results of triplicate experiments are shown as mean ± SEM. Error-bars denote one standard error of the mean and asterisk and hash indicate a statistically significant difference. *; P=0.0010 vs. control and #; P=0.0138 vs. T3 treatment. B. Western blots of p-Fyn, Fyn and betaactin (loading control) in the differentiated PC-12 cells with/without 10 nM T3 hormone and αvβ3 antibody (αvβ3-Ab, 1 µg/ml) during one-hour hypoxia. Bands were quantified by Image J.

Techniques: Western Blot, Control

Analysis of the Rac 1 and NADPH oxidase activity in the differentiated PC-12 cells with/without 10 nM T3 hormone and αvβ3 antibody (αvβ3-Ab, 1 µg/ml) during 1 hour hypoxia. A. Level of Rac1 in the differentiated PC-12 cells with/without 10 nM T3 hormone and αvβ3 antibody (αvβ3-Ab,1 µg/ ml) during one h hypoxia. Results of triplicate experiments are shown as mean ± SEM. Error-bars denote one standard error of the mean and the asterisk and hash indicate a statistically significant difference *; P=0.0069 vs. control and #; P=0.0078 vs. T3 hormone treatment. B. NADPH oxidase activity in the differentiated PC-12 cells with/without 10 nM T3 hormone and αvβ3 antibody (αvβ3-Ab, 1 µg/ml) during 1 hour hypoxia. NADPH oxidase activity was measured as Relative Light Unit per minute (RLU/minute). Results of triplicate experiments are shown as mean ± SEM. Error-bars denote one standard error of the mean and asterisk or hash indicates a statistically significant difference. *; P=0.0010 vs. control and #; P=0.0014 vs. T3 hormone treatment.

Journal: Cell Journal (Yakhteh)

Article Title: 3,5,3'-Triiodo-L-Thyronine Regulates Actin Cytoskeleton Dynamic in The Differentiated PC-12 Cells during Hypoxia through An αvβ3 Integrin

doi: 10.22074/CELLJ.2022.557501.1059.

Figure Lengend Snippet: Analysis of the Rac 1 and NADPH oxidase activity in the differentiated PC-12 cells with/without 10 nM T3 hormone and αvβ3 antibody (αvβ3-Ab, 1 µg/ml) during 1 hour hypoxia. A. Level of Rac1 in the differentiated PC-12 cells with/without 10 nM T3 hormone and αvβ3 antibody (αvβ3-Ab,1 µg/ ml) during one h hypoxia. Results of triplicate experiments are shown as mean ± SEM. Error-bars denote one standard error of the mean and the asterisk and hash indicate a statistically significant difference *; P=0.0069 vs. control and #; P=0.0078 vs. T3 hormone treatment. B. NADPH oxidase activity in the differentiated PC-12 cells with/without 10 nM T3 hormone and αvβ3 antibody (αvβ3-Ab, 1 µg/ml) during 1 hour hypoxia. NADPH oxidase activity was measured as Relative Light Unit per minute (RLU/minute). Results of triplicate experiments are shown as mean ± SEM. Error-bars denote one standard error of the mean and asterisk or hash indicates a statistically significant difference. *; P=0.0010 vs. control and #; P=0.0014 vs. T3 hormone treatment.

Techniques: Activity Assay, Control

Network formation of ECFCs in LXW7-modified collagen hydrogel was blocked by an anti-αvβ3 integrin blocking antibody. (A) Network formation of ECFCs cultured in untreated collagen hydrogel (a) , network formation of ECFCs pretreated with an anti-αvβ3 integrin blocking antibody cultured in LXW7-modified collagen hydrogel (b) and network formation of ECFCs cultured in LXW7-modified collagen hydrogel (c) . Scale bar = 200 μm. (B) Quantification of the numbers of vessel network. (C) Quantification of the total vessel network length. Data were expressed as mean ± standard deviation: ∗ p < 0.05 ( n = 5).

Journal: Frontiers in Bioengineering and Biotechnology

Article Title: Developing an Injectable Nanofibrous Extracellular Matrix Hydrogel With an Integrin αvβ3 Ligand to Improve Endothelial Cell Survival, Engraftment and Vascularization

doi: 10.3389/fbioe.2020.00890

Figure Lengend Snippet: Network formation of ECFCs in LXW7-modified collagen hydrogel was blocked by an anti-αvβ3 integrin blocking antibody. (A) Network formation of ECFCs cultured in untreated collagen hydrogel (a) , network formation of ECFCs pretreated with an anti-αvβ3 integrin blocking antibody cultured in LXW7-modified collagen hydrogel (b) and network formation of ECFCs cultured in LXW7-modified collagen hydrogel (c) . Scale bar = 200 μm. (B) Quantification of the numbers of vessel network. (C) Quantification of the total vessel network length. Data were expressed as mean ± standard deviation: ∗ p < 0.05 ( n = 5).

Article Snippet: For capillary network formation, three groups were set up: (1) ECFCs cultured in untreated collagen hydrogel, (2) ECFCs cultured in LXW7-modified collagen hydrogel, (3) ECFCs incubated with a monoclonal anti-αvβ3 integrin blocking antibody (MAB1876, Millipore) first to block the integrin αvβ3 expressed on the ECFCs, then cultured in the LXW7-modified collagen hydrogel.

Techniques: Modification, Blocking Assay, Cell Culture, Standard Deviation

Hypoxia‐driven paracrine OPN signaling promotes EMT and CSC ‐like properties in PCC s. (A) The mRNA expression levels of OPN , the αv subunit of integrin, and the β3 subunit of integrin in 4 pancreatic cancer cell lines and PSC s were analyzed by quantitative real‐time RT ‐ PCR . (B and C) The protein expression levels of OPN , the αv subunit of integrin, and the β3 subunit of integrin in 4 pancreatic cancer cell lines and PSC s were determined by western blot analysis. β‐Actin was used as an internal control. (D) The cell supernatants of 4 pancreatic cancer cell lines and PSC s were collected, and the OPN concentration was measured by ELISA . (E) Representative images from the wound healing assay after rh OPN , PSC ‐ CM , or PSC ‐ CM + OPN Ab treatments in Bx PC ‐3 and CFPAC ‐1 cells. Images were obtained at 0 h and 24 h. The scale bar represents 100 μm. (F and G) Representative images of the Matrigel invasion assay after rh OPN , PSC ‐ CM , or PSC ‐ CM + OPN Ab treatments in Bx PC ‐3 and CFPAC ‐1 cells. The invasive cells were quantified by counting the number of cells in 10 random fields. The scale bar represents 50 μm. (H, I and J) Representative images of the tumorsphere formation assay after rh OPN , PSC ‐ CM , or PSC ‐ CM + OPN Ab treatments in Bx PC ‐3 and CFPAC ‐1 cells. The number of tumorspheres was counted and plotted, and the percentage of tumorspheres with diameters of 50–100 μm, 100–150 μm, or >150 μm was calculated and plotted. The scale bar represents 50 μm. (K) The protein expression levels of EMT and CSC markers after rh OPN , PSC ‐ CM , or PSC ‐ CM + OPN Ab treatments were determined by western blot analysis in Bx PC ‐3 and CFPAC ‐1 cells. β‐Actin was used as an internal control. Q‐ PSC : Quiescent pancreatic stellate cell. A‐ PSC : Activated pancreatic stellate cell. All data are shown as the mean ± SD of at least three independent experiments. One‐way ANOVA and Tukey's multiple comparisons test were performed to determine significance. * P < 0.05, ** P < 0.01, ns: no significance.

Journal: Molecular Oncology

Article Title: Hypoxia‐driven paracrine osteopontin/integrin αvβ3 signaling promotes pancreatic cancer cell epithelial–mesenchymal transition and cancer stem cell‐like properties by modulating forkhead box protein M1

doi: 10.1002/1878-0261.12399

Figure Lengend Snippet: Hypoxia‐driven paracrine OPN signaling promotes EMT and CSC ‐like properties in PCC s. (A) The mRNA expression levels of OPN , the αv subunit of integrin, and the β3 subunit of integrin in 4 pancreatic cancer cell lines and PSC s were analyzed by quantitative real‐time RT ‐ PCR . (B and C) The protein expression levels of OPN , the αv subunit of integrin, and the β3 subunit of integrin in 4 pancreatic cancer cell lines and PSC s were determined by western blot analysis. β‐Actin was used as an internal control. (D) The cell supernatants of 4 pancreatic cancer cell lines and PSC s were collected, and the OPN concentration was measured by ELISA . (E) Representative images from the wound healing assay after rh OPN , PSC ‐ CM , or PSC ‐ CM + OPN Ab treatments in Bx PC ‐3 and CFPAC ‐1 cells. Images were obtained at 0 h and 24 h. The scale bar represents 100 μm. (F and G) Representative images of the Matrigel invasion assay after rh OPN , PSC ‐ CM , or PSC ‐ CM + OPN Ab treatments in Bx PC ‐3 and CFPAC ‐1 cells. The invasive cells were quantified by counting the number of cells in 10 random fields. The scale bar represents 50 μm. (H, I and J) Representative images of the tumorsphere formation assay after rh OPN , PSC ‐ CM , or PSC ‐ CM + OPN Ab treatments in Bx PC ‐3 and CFPAC ‐1 cells. The number of tumorspheres was counted and plotted, and the percentage of tumorspheres with diameters of 50–100 μm, 100–150 μm, or >150 μm was calculated and plotted. The scale bar represents 50 μm. (K) The protein expression levels of EMT and CSC markers after rh OPN , PSC ‐ CM , or PSC ‐ CM + OPN Ab treatments were determined by western blot analysis in Bx PC ‐3 and CFPAC ‐1 cells. β‐Actin was used as an internal control. Q‐ PSC : Quiescent pancreatic stellate cell. A‐ PSC : Activated pancreatic stellate cell. All data are shown as the mean ± SD of at least three independent experiments. One‐way ANOVA and Tukey's multiple comparisons test were performed to determine significance. * P < 0.05, ** P < 0.01, ns: no significance.

Article Snippet: Integrin αvβ3 blocking antibody was obtained from Millipore (Darmstadt, Germany).

Techniques: Expressing, Quantitative RT-PCR, Western Blot, Control, Concentration Assay, Enzyme-linked Immunosorbent Assay, Wound Healing Assay, Invasion Assay, Tube Formation Assay

Integrin αvβ3 mediates the effects of paracrine OPN signaling on EMT and CSC ‐like properties in PCC s. (A) Representative images from the wound healing assay after αvβ3 Ab, rh OPN , or rh OPN + αvβ3 Ab treatments in Bx PC ‐3 and CFPAC ‐1 cells. Images were obtained at 0 h and 24 h. The scale bar represents 100 μm. (B and C) Representative images of the Matrigel invasion assay after αvβ3 Ab, rh OPN , or rh OPN + αvβ3 Ab treatments in Bx PC ‐3 and CFPAC ‐1 cells. The invasive cells were quantified by counting the number of cells in 10 random fields. The scale bar represents 50 μm. (D, E, and F) Representative images from the tumorsphere formation assay after αvβ3 Ab, rh OPN , or rh OPN + αvβ3 Ab treatments in Bx PC ‐3 and CFPAC ‐1 cells. The number of tumorspheres was counted and plotted, and the percentage of tumorspheres with diameters of 50–100 μm, 100–150 μm, or >150 μm was calculated and plotted. The scale bar represents 50 μm. (G) The protein expression levels of EMT and CSC markers after αvβ3 Ab, rh OPN , or rh OPN + αvβ3 Ab treatments were determined by western blot analysis in Bx PC ‐3 and CFPAC ‐1 cells. β‐Actin was used as an internal control. All data are shown as the mean ± SD of at least three independent experiments. One‐way ANOVA and Tukey's multiple comparisons test were performed to determine significance. * P < 0.05, ** P < 0.01, ns: no significance.

Journal: Molecular Oncology

doi: 10.1002/1878-0261.12399

Figure Lengend Snippet: Integrin αvβ3 mediates the effects of paracrine OPN signaling on EMT and CSC ‐like properties in PCC s. (A) Representative images from the wound healing assay after αvβ3 Ab, rh OPN , or rh OPN + αvβ3 Ab treatments in Bx PC ‐3 and CFPAC ‐1 cells. Images were obtained at 0 h and 24 h. The scale bar represents 100 μm. (B and C) Representative images of the Matrigel invasion assay after αvβ3 Ab, rh OPN , or rh OPN + αvβ3 Ab treatments in Bx PC ‐3 and CFPAC ‐1 cells. The invasive cells were quantified by counting the number of cells in 10 random fields. The scale bar represents 50 μm. (D, E, and F) Representative images from the tumorsphere formation assay after αvβ3 Ab, rh OPN , or rh OPN + αvβ3 Ab treatments in Bx PC ‐3 and CFPAC ‐1 cells. The number of tumorspheres was counted and plotted, and the percentage of tumorspheres with diameters of 50–100 μm, 100–150 μm, or >150 μm was calculated and plotted. The scale bar represents 50 μm. (G) The protein expression levels of EMT and CSC markers after αvβ3 Ab, rh OPN , or rh OPN + αvβ3 Ab treatments were determined by western blot analysis in Bx PC ‐3 and CFPAC ‐1 cells. β‐Actin was used as an internal control. All data are shown as the mean ± SD of at least three independent experiments. One‐way ANOVA and Tukey's multiple comparisons test were performed to determine significance. * P < 0.05, ** P < 0.01, ns: no significance.

Article Snippet: Integrin αvβ3 blocking antibody was obtained from Millipore (Darmstadt, Germany).

Techniques: Wound Healing Assay, Invasion Assay, Tube Formation Assay, Expressing, Western Blot, Control

FOXM 1 mediates the effects of the OPN /integrin αvβ3 axis on EMT and CSC ‐like properties in PCC s. (A) The mRNA expression levels of FOXM 1 and its downstream targets after αvβ3 Ab, rh OPN , or rh OPN + αvβ3 Ab treatments were determined by quantitative real‐time RT ‐ PCR in Bx PC ‐3 cells. (B and C) The protein expression levels of FOXM 1 and its downstream targets after αvβ3 Ab, rh OPN , or rh OPN + αvβ3 Ab treatments were determined by western blot analysis in Bx PC ‐3 cells. β‐Actin was used as an internal control. (D) Representative images from the wound healing assay after TST , rh OPN , or rh OPN + TST treatments in Bx PC ‐3 cells. Images were obtained at 0 h and 24 h. The scale bar represents 100 μm. (E and G) Representative images from the Matrigel invasion assay after TST , rh OPN , or rh OPN + TST treatments in Bx PC ‐3 cells. The invasive cells were quantified by counting the number of cells in 10 random fields. The scale bar represents 50 μm. (F, H, and I) Representative images from the tumorsphere formation assay after TST , rh OPN , or rh OPN + TST treatments in Bx PC ‐3 cells. The number of tumorspheres was counted and plotted, and percentage of tumorspheres with diameters of 50–100 μm, 100–150 μm, or >150 μm was calculated and plotted. The scale bar represents 50 μm. (J) The protein expression levels of EMT and CSC markers after TST , rh OPN , or rh OPN + TST treatments were determined by western blot analysis in Bx PC ‐3 cells. β‐Actin was used as an internal control. All data are shown as the mean ± SD of at least three independent experiments. One‐way ANOVA and Tukey's multiple comparisons test were performed to determine significance. * P < 0.05, ** P < 0.01, ns: no significance.

Journal: Molecular Oncology

doi: 10.1002/1878-0261.12399

Figure Lengend Snippet: FOXM 1 mediates the effects of the OPN /integrin αvβ3 axis on EMT and CSC ‐like properties in PCC s. (A) The mRNA expression levels of FOXM 1 and its downstream targets after αvβ3 Ab, rh OPN , or rh OPN + αvβ3 Ab treatments were determined by quantitative real‐time RT ‐ PCR in Bx PC ‐3 cells. (B and C) The protein expression levels of FOXM 1 and its downstream targets after αvβ3 Ab, rh OPN , or rh OPN + αvβ3 Ab treatments were determined by western blot analysis in Bx PC ‐3 cells. β‐Actin was used as an internal control. (D) Representative images from the wound healing assay after TST , rh OPN , or rh OPN + TST treatments in Bx PC ‐3 cells. Images were obtained at 0 h and 24 h. The scale bar represents 100 μm. (E and G) Representative images from the Matrigel invasion assay after TST , rh OPN , or rh OPN + TST treatments in Bx PC ‐3 cells. The invasive cells were quantified by counting the number of cells in 10 random fields. The scale bar represents 50 μm. (F, H, and I) Representative images from the tumorsphere formation assay after TST , rh OPN , or rh OPN + TST treatments in Bx PC ‐3 cells. The number of tumorspheres was counted and plotted, and percentage of tumorspheres with diameters of 50–100 μm, 100–150 μm, or >150 μm was calculated and plotted. The scale bar represents 50 μm. (J) The protein expression levels of EMT and CSC markers after TST , rh OPN , or rh OPN + TST treatments were determined by western blot analysis in Bx PC ‐3 cells. β‐Actin was used as an internal control. All data are shown as the mean ± SD of at least three independent experiments. One‐way ANOVA and Tukey's multiple comparisons test were performed to determine significance. * P < 0.05, ** P < 0.01, ns: no significance.

Article Snippet: Integrin αvβ3 blocking antibody was obtained from Millipore (Darmstadt, Germany).

Techniques: Expressing, Quantitative RT-PCR, Western Blot, Control, Wound Healing Assay, Invasion Assay, Tube Formation Assay

The OPN /integrin αvβ3 axis induces FOXM 1 expression by activating the Akt and Erk signaling pathways in PCC s. (A and C) Western blot analysis showed that rh OPN increased Akt phosphorylation to induce FOXM 1 expression in Bx PC ‐3 cells, while this effect was antagonized by blocking integrin αvβ3 or inhibiting Akt. β‐Actin was used as an internal control. (B and D) Western blot analysis showed that rh OPN increased Erk phosphorylation to induce FOXM 1 expression in Bx PC ‐3 cells, while this effect was antagonized by blocking integrin αvβ3 or inhibiting Erk. β‐Actin was used as an internal control. All data are shown as the mean ± SD of at least three independent experiments. One‐way ANOVA and Tukey's multiple comparisons test were performed to determine significance. * P < 0.05, ** P < 0.01, ns: no significance.

Journal: Molecular Oncology

doi: 10.1002/1878-0261.12399

Figure Lengend Snippet: The OPN /integrin αvβ3 axis induces FOXM 1 expression by activating the Akt and Erk signaling pathways in PCC s. (A and C) Western blot analysis showed that rh OPN increased Akt phosphorylation to induce FOXM 1 expression in Bx PC ‐3 cells, while this effect was antagonized by blocking integrin αvβ3 or inhibiting Akt. β‐Actin was used as an internal control. (B and D) Western blot analysis showed that rh OPN increased Erk phosphorylation to induce FOXM 1 expression in Bx PC ‐3 cells, while this effect was antagonized by blocking integrin αvβ3 or inhibiting Erk. β‐Actin was used as an internal control. All data are shown as the mean ± SD of at least three independent experiments. One‐way ANOVA and Tukey's multiple comparisons test were performed to determine significance. * P < 0.05, ** P < 0.01, ns: no significance.

Article Snippet: Integrin αvβ3 blocking antibody was obtained from Millipore (Darmstadt, Germany).

Techniques: Expressing, Protein-Protein interactions, Western Blot, Phospho-proteomics, Blocking Assay, Control

Schematic of the findings of the present study. The hypoxic tumor microenvironment promotes the activation of PSC s and increases the expression and secretion of OPN in PSC s in a ROS ‐dependent manner. The OPN secreted by activated PSC s binds to integrin αvβ3 on the surface of PCC s, thus activating downstream signaling cascades, including the Akt and Erk pathways, which induces the expression of FOXM 1. EMT and CSC ‐like properties are then triggered, accelerating the progression of pancreatic cancer.

Journal: Molecular Oncology

doi: 10.1002/1878-0261.12399

Figure Lengend Snippet: Schematic of the findings of the present study. The hypoxic tumor microenvironment promotes the activation of PSC s and increases the expression and secretion of OPN in PSC s in a ROS ‐dependent manner. The OPN secreted by activated PSC s binds to integrin αvβ3 on the surface of PCC s, thus activating downstream signaling cascades, including the Akt and Erk pathways, which induces the expression of FOXM 1. EMT and CSC ‐like properties are then triggered, accelerating the progression of pancreatic cancer.

Article Snippet: Integrin αvβ3 blocking antibody was obtained from Millipore (Darmstadt, Germany).

Techniques: Activation Assay, Expressing

A. Immunocolocalization of BKCa and αvβ3. Representative confocal images of BKCa (red) and integrin αvβ3 (green) staining conducted in PC3 cells. Staining is more pronounced on the plasma membrane for both proteins and the merge shows that there is a co-localization (yellow to orange areas) on plasma membrane areas. B. Co-immunoprecipitation of integrin αvβ3 and BKCa in PC3 cells. Cells were transfected with BKCa or BK-shRNA and their corresponding negative control vectors. Proteins were extracted and immunoprecipitated using anti-BKCa or anti-αvβ3 antibodies; blots were probed with anti-αvβ3 or anti-BKCa antibodies respectively. Bead lanes contain the protein G conjugated sepharose beads used during the immunoprecipitation without the protein input. Equal amount of protein extract from each group was subjected to Western blot with β-actin as the loading control. All the experiments were performed in triplicate.

Journal: Oncotarget

Article Title: BKCa promotes growth and metastasis of prostate cancer through facilitating the coupling between αvβ3 integrin and FAK

doi: 10.18632/oncotarget.9559

Figure Lengend Snippet: A. Immunocolocalization of BKCa and αvβ3. Representative confocal images of BKCa (red) and integrin αvβ3 (green) staining conducted in PC3 cells. Staining is more pronounced on the plasma membrane for both proteins and the merge shows that there is a co-localization (yellow to orange areas) on plasma membrane areas. B. Co-immunoprecipitation of integrin αvβ3 and BKCa in PC3 cells. Cells were transfected with BKCa or BK-shRNA and their corresponding negative control vectors. Proteins were extracted and immunoprecipitated using anti-BKCa or anti-αvβ3 antibodies; blots were probed with anti-αvβ3 or anti-BKCa antibodies respectively. Bead lanes contain the protein G conjugated sepharose beads used during the immunoprecipitation without the protein input. Equal amount of protein extract from each group was subjected to Western blot with β-actin as the loading control. All the experiments were performed in triplicate.

Article Snippet: Cells were treated with 100 nM IBTX (BKCa channel inhibitor, Sigma, St. Louis, MO, USA), 30μM NS1619 (BKCa channel activator, Sigma), 10 μg/ml LM609 (αvβ3 integrin blocking antibody, Millipore) or 10μM Y15 (a FAK inhibitor, Abcam) for 72 hr.

Techniques: Staining, Clinical Proteomics, Membrane, Immunoprecipitation, Transfection, shRNA, Negative Control, Western Blot, Control

A. Immunocolocalization of BKCa (red) and FAK (green). B. Co-immunoprecipitation of FAK and BKCa in PC3 cells. Cells were transfected with BKCa or BK-shRNA and their corresponding negative control vectors. Proteins were extracted and immunoprecipitated using anti-BKCa or anti-FAK antibodies; blots were probed with anti-FAK, anti-pTyr100 or anti-BKCa antibodies. Bead lanes contained the protein G conjugated sepharose beads used during the immunoprecipitation without the protein input. Equal amount of protein extract from each group was subjected to Western blot with β-actin as the loading control. C-D. Western blot analysis of the expression of BKCa, p-FAK (Y397), FAK and αvβ3 integrin in response to BKCa upregulation or downregulation. All the experiments were performed in triplicate. The data are shown as the means ± se. *P < 0.05.

Journal: Oncotarget

Article Title: BKCa promotes growth and metastasis of prostate cancer through facilitating the coupling between αvβ3 integrin and FAK

doi: 10.18632/oncotarget.9559

Figure Lengend Snippet: A. Immunocolocalization of BKCa (red) and FAK (green). B. Co-immunoprecipitation of FAK and BKCa in PC3 cells. Cells were transfected with BKCa or BK-shRNA and their corresponding negative control vectors. Proteins were extracted and immunoprecipitated using anti-BKCa or anti-FAK antibodies; blots were probed with anti-FAK, anti-pTyr100 or anti-BKCa antibodies. Bead lanes contained the protein G conjugated sepharose beads used during the immunoprecipitation without the protein input. Equal amount of protein extract from each group was subjected to Western blot with β-actin as the loading control. C-D. Western blot analysis of the expression of BKCa, p-FAK (Y397), FAK and αvβ3 integrin in response to BKCa upregulation or downregulation. All the experiments were performed in triplicate. The data are shown as the means ± se. *P < 0.05.

Techniques: Immunoprecipitation, Transfection, shRNA, Negative Control, Western Blot, Control, Expressing

A. Western blot analysis of FAK and p-FAK(397) in BKCa or Vector transfected prostate cancer PC3 cells treated with NS1619 (30 μM), IBTX (100 nM), LM609 (10 μg/ml) or Y15 (10μM) for 24 hr. B. MTT assay showed that BKCa-enhanced cell viability was abrogated by inhibition of the αvβ3/FAK signaling. C. Migration assay revealed that BKCa-enhanced cell migration was abrogated by inhibition of the αvβ3/FAK signaling.

Journal: Oncotarget

Article Title: BKCa promotes growth and metastasis of prostate cancer through facilitating the coupling between αvβ3 integrin and FAK

doi: 10.18632/oncotarget.9559

Figure Lengend Snippet: A. Western blot analysis of FAK and p-FAK(397) in BKCa or Vector transfected prostate cancer PC3 cells treated with NS1619 (30 μM), IBTX (100 nM), LM609 (10 μg/ml) or Y15 (10μM) for 24 hr. B. MTT assay showed that BKCa-enhanced cell viability was abrogated by inhibition of the αvβ3/FAK signaling. C. Migration assay revealed that BKCa-enhanced cell migration was abrogated by inhibition of the αvβ3/FAK signaling.

Techniques: Western Blot, Plasmid Preparation, Transfection, MTT Assay, Inhibition, Migration

A. Under normal conditions, BKCa forms complex with integrin αvβ3 and triggers FAK activation/phosphorylation. The activated FAK promotes prostate cancer cell proliferation, migration and invasion. B. Overexpression of BKCa enhance its interaction with integrin αvβ3, recruits more FAK to the integrin αvβ3/BKCa complex and promotes activation/phosphorylation of FAK, resulting in increased cell proliferation, migration and invasion. C. Downregulation of BKCa disrupts the integrin αvβ3/BKCa complex and abolishes BKCa-mediated αvβ3/FAK coupling. Thus, BKCa-induced cancer cell proliferation, migration and invasion are counteracted.

Journal: Oncotarget

Article Title: BKCa promotes growth and metastasis of prostate cancer through facilitating the coupling between αvβ3 integrin and FAK

doi: 10.18632/oncotarget.9559

Figure Lengend Snippet: A. Under normal conditions, BKCa forms complex with integrin αvβ3 and triggers FAK activation/phosphorylation. The activated FAK promotes prostate cancer cell proliferation, migration and invasion. B. Overexpression of BKCa enhance its interaction with integrin αvβ3, recruits more FAK to the integrin αvβ3/BKCa complex and promotes activation/phosphorylation of FAK, resulting in increased cell proliferation, migration and invasion. C. Downregulation of BKCa disrupts the integrin αvβ3/BKCa complex and abolishes BKCa-mediated αvβ3/FAK coupling. Thus, BKCa-induced cancer cell proliferation, migration and invasion are counteracted.

Techniques: Activation Assay, Phospho-proteomics, Migration, Over Expression

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