bone morphogenetic protein 4 (bmp4) Search Results


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MedChemExpress bmp4
Fig. 2 BMSC-EVs upregulated Smad 6 expression in NSCs via the secretion of TGF-β. A. To confirm whether IL-6, <t>BMP4,</t> and TGF-β existed in the BMSC-EVs, the expression of these factors was determined by PCR (n = 3, Student’s t-test). B. ELISA from five individual samples confirmed the presence of TGF-β and IL-6 in BMSC- EVs. C, D. To evaluate whether TGF-β or IL-6 played a key role in mediating the expression of Smad 6 in NSCs, we added SB431542 and JSH-23, respec- tively, to NSCs in the presence of BMSC-EVs. This revealed that the BMSC-EVs-induced upregulation of Smad 6 could be abolished by the addition of SB431542 (C, n = 5; the data were revealed as fold changes to control NSCs, Student’s t-test). Conversely, the addition of JSH- 23 did not alter the expression of Smad 6 in NSCs (D, n = 5; the data were presented as fold changes to control BMSC-EV treated NSCs, Student’s t-test) E. We added TGF-β to NSCs to assess the effect of TGF-β on mediating Smad 6 expression; this resulted in an increase of Smad 6 expression in NSCs. This TGF-β-induced upregula- tion of Smad 6 expression could be significantly abolished by the addition of SB431542 (n = 5; the data were presented as fold changes to control NSCs, Stu- dent’s t-test). (Smad 6 mRNA expression was normalized to GAPDH mRNA; the data were presented as mean ± S.D; *p < 0.05, **p < 0.01, ***p < 0.001, #p > 0.05.)
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Cusabio mouse bone morphogenetic protein 4 bmp 4 elisa kit
Fig. 2 BMSC-EVs upregulated Smad 6 expression in NSCs via the secretion of TGF-β. A. To confirm whether IL-6, <t>BMP4,</t> and TGF-β existed in the BMSC-EVs, the expression of these factors was determined by PCR (n = 3, Student’s t-test). B. ELISA from five individual samples confirmed the presence of TGF-β and IL-6 in BMSC- EVs. C, D. To evaluate whether TGF-β or IL-6 played a key role in mediating the expression of Smad 6 in NSCs, we added SB431542 and JSH-23, respec- tively, to NSCs in the presence of BMSC-EVs. This revealed that the BMSC-EVs-induced upregulation of Smad 6 could be abolished by the addition of SB431542 (C, n = 5; the data were revealed as fold changes to control NSCs, Student’s t-test). Conversely, the addition of JSH- 23 did not alter the expression of Smad 6 in NSCs (D, n = 5; the data were presented as fold changes to control BMSC-EV treated NSCs, Student’s t-test) E. We added TGF-β to NSCs to assess the effect of TGF-β on mediating Smad 6 expression; this resulted in an increase of Smad 6 expression in NSCs. This TGF-β-induced upregula- tion of Smad 6 expression could be significantly abolished by the addition of SB431542 (n = 5; the data were presented as fold changes to control NSCs, Stu- dent’s t-test). (Smad 6 mRNA expression was normalized to GAPDH mRNA; the data were presented as mean ± S.D; *p < 0.05, **p < 0.01, ***p < 0.001, #p > 0.05.)
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Proteintech anti bmp4
Fig. 2 BMSC-EVs upregulated Smad 6 expression in NSCs via the secretion of TGF-β. A. To confirm whether IL-6, <t>BMP4,</t> and TGF-β existed in the BMSC-EVs, the expression of these factors was determined by PCR (n = 3, Student’s t-test). B. ELISA from five individual samples confirmed the presence of TGF-β and IL-6 in BMSC- EVs. C, D. To evaluate whether TGF-β or IL-6 played a key role in mediating the expression of Smad 6 in NSCs, we added SB431542 and JSH-23, respec- tively, to NSCs in the presence of BMSC-EVs. This revealed that the BMSC-EVs-induced upregulation of Smad 6 could be abolished by the addition of SB431542 (C, n = 5; the data were revealed as fold changes to control NSCs, Student’s t-test). Conversely, the addition of JSH- 23 did not alter the expression of Smad 6 in NSCs (D, n = 5; the data were presented as fold changes to control BMSC-EV treated NSCs, Student’s t-test) E. We added TGF-β to NSCs to assess the effect of TGF-β on mediating Smad 6 expression; this resulted in an increase of Smad 6 expression in NSCs. This TGF-β-induced upregula- tion of Smad 6 expression could be significantly abolished by the addition of SB431542 (n = 5; the data were presented as fold changes to control NSCs, Stu- dent’s t-test). (Smad 6 mRNA expression was normalized to GAPDH mRNA; the data were presented as mean ± S.D; *p < 0.05, **p < 0.01, ***p < 0.001, #p > 0.05.)
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Proteintech recombinant bmp4 protein
The bone morphogenetic protein (BMP) signaling pathway is activated in intestinal epithelial cells and intraepithelial lymphocytes (IELs) following ischemia/reperfusion (I/R). (A) The level of <t>BMP4</t> protein (red) expression significantly increased in the mid-to-distal villus region after 6 h of I/R, according to immunofluorescence staining. (B) The expression levels of the type I BMP receptor and phosphorylated nuclear factor (p-NF)-κB were both significantly increased after 6 h of I/R in IELs. * P<0.05, 3-4 mice/group; the results are representative of three independent experiments.
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Proteintech bmp4
The bone morphogenetic protein (BMP) signaling pathway is activated in intestinal epithelial cells and intraepithelial lymphocytes (IELs) following ischemia/reperfusion (I/R). (A) The level of <t>BMP4</t> protein (red) expression significantly increased in the mid-to-distal villus region after 6 h of I/R, according to immunofluorescence staining. (B) The expression levels of the type I BMP receptor and phosphorylated nuclear factor (p-NF)-κB were both significantly increased after 6 h of I/R in IELs. * P<0.05, 3-4 mice/group; the results are representative of three independent experiments.
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Boster Bio mouse bmp 4 elisa kit
miR‐1187 directly targets BMP4. (A) The predicted binding site between miR‐1187 <t>and</t> <t>BMP4</t> by bioinformatics analysis. (B) The luciferase activity of the BMP4‐WT and BMP4‐MUT in MC3T3‐E1 cells treated with miR‐1187 mimics or NC. (C) mRNA expression of Bmp4 was significantly downregulated in the miR‐1187 mimics‐transfected group. (D) Western blot analysis for the expression of BMP4 protein in miR‐1187 mimics and inhibitor‐transfected MC3T3‐E1 cells on Pti. (E) ELISA assay analysis for the expression of supernatant BMP4 secreted protein in miR‐1187 mimics and inhibitor‐transfected MC3T3‐E1cells on Pti. All values represent means ± SD.( n = 3). * p < 0.05, ** p < 0.01.
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MedChemExpress bmp 4
miR‐1187 directly targets BMP4. (A) The predicted binding site between miR‐1187 <t>and</t> <t>BMP4</t> by bioinformatics analysis. (B) The luciferase activity of the BMP4‐WT and BMP4‐MUT in MC3T3‐E1 cells treated with miR‐1187 mimics or NC. (C) mRNA expression of Bmp4 was significantly downregulated in the miR‐1187 mimics‐transfected group. (D) Western blot analysis for the expression of BMP4 protein in miR‐1187 mimics and inhibitor‐transfected MC3T3‐E1 cells on Pti. (E) ELISA assay analysis for the expression of supernatant BMP4 secreted protein in miR‐1187 mimics and inhibitor‐transfected MC3T3‐E1cells on Pti. All values represent means ± SD.( n = 3). * p < 0.05, ** p < 0.01.
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Boster Bio cd44
Effect of PTE on the cell cycle of MSCs in vitro and in vivo. (a) Representative cell cycle analysis for PI of MSCs cultured treatment with a different dose of PTE (30 µg/ml, 300 µg/ml) for 1 day and 3 days. PI levels of MSCs cultured increased with increasing dose and time of PTE. (b) Representative cell cycle analysis for PI of MSCs isolated from rats that were administered with different dose of PTE (3 mg/kg/day, 30 mg/kg/day) for 1 and 3 days in vivo. The PT levels of MSCs cultured increased with increasing dose and time of PTE. PTE strongly promoted increasing of PI of MSCs in vivo in time‐ and dose‐dependent manner. *P < 0.05; **P < 0.01 compared to control at the same time point. ***P < 0.05; ****P < 0.01 PI levels from 3 days MSCs cultured with and without PTE were compared to those from 1 day MSCs cultured with or without PTE. (c) Detection of <t>CD44</t> expression by flow cytometry. MSCs isolated from rats that were administered with and without PTE for 3 days in vivo were analysed for expression of CD44 by flow cytometry, negative control represent MSCs incubated with FITC‐conjugated antibody alone. Vertical lines represent maximum fluorescence intensity for FITC‐conjugated antibody. CD44 expression of MSCs isolated from rats that were administered with PTE increased in dose‐dependent manner.
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Cusabio bmp4
Fig. 1 Serum levels of (A) BMP2 and (B) <t>BMP4</t> in the studied groups. BMP2: Bone morphogenetic protein-2, BMP4: Bone morphogenetic protein-4.
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Angiocrine bone morphogenetic protein 4 (bmp4)
Fig. 1 Serum levels of (A) BMP2 and (B) <t>BMP4</t> in the studied groups. BMP2: Bone morphogenetic protein-2, BMP4: Bone morphogenetic protein-4.
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Novocastra bone morphogenetic protein-4 (bmp-4)
Fig. 1 Serum levels of (A) BMP2 and (B) <t>BMP4</t> in the studied groups. BMP2: Bone morphogenetic protein-2, BMP4: Bone morphogenetic protein-4.
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Gemini Bio bmp4 morphogen
Fig. 1 Serum levels of (A) BMP2 and (B) <t>BMP4</t> in the studied groups. BMP2: Bone morphogenetic protein-2, BMP4: Bone morphogenetic protein-4.
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Image Search Results


Fig. 2 BMSC-EVs upregulated Smad 6 expression in NSCs via the secretion of TGF-β. A. To confirm whether IL-6, BMP4, and TGF-β existed in the BMSC-EVs, the expression of these factors was determined by PCR (n = 3, Student’s t-test). B. ELISA from five individual samples confirmed the presence of TGF-β and IL-6 in BMSC- EVs. C, D. To evaluate whether TGF-β or IL-6 played a key role in mediating the expression of Smad 6 in NSCs, we added SB431542 and JSH-23, respec- tively, to NSCs in the presence of BMSC-EVs. This revealed that the BMSC-EVs-induced upregulation of Smad 6 could be abolished by the addition of SB431542 (C, n = 5; the data were revealed as fold changes to control NSCs, Student’s t-test). Conversely, the addition of JSH- 23 did not alter the expression of Smad 6 in NSCs (D, n = 5; the data were presented as fold changes to control BMSC-EV treated NSCs, Student’s t-test) E. We added TGF-β to NSCs to assess the effect of TGF-β on mediating Smad 6 expression; this resulted in an increase of Smad 6 expression in NSCs. This TGF-β-induced upregula- tion of Smad 6 expression could be significantly abolished by the addition of SB431542 (n = 5; the data were presented as fold changes to control NSCs, Stu- dent’s t-test). (Smad 6 mRNA expression was normalized to GAPDH mRNA; the data were presented as mean ± S.D; *p < 0.05, **p < 0.01, ***p < 0.001, #p > 0.05.)

Journal: Stem cell reviews and reports

Article Title: MSC secreted extracellular vesicles carrying TGF-beta upregulate Smad 6 expression and promote the regrowth of neurons in spinal cord injured rats.

doi: 10.1007/s12015-021-10219-6

Figure Lengend Snippet: Fig. 2 BMSC-EVs upregulated Smad 6 expression in NSCs via the secretion of TGF-β. A. To confirm whether IL-6, BMP4, and TGF-β existed in the BMSC-EVs, the expression of these factors was determined by PCR (n = 3, Student’s t-test). B. ELISA from five individual samples confirmed the presence of TGF-β and IL-6 in BMSC- EVs. C, D. To evaluate whether TGF-β or IL-6 played a key role in mediating the expression of Smad 6 in NSCs, we added SB431542 and JSH-23, respec- tively, to NSCs in the presence of BMSC-EVs. This revealed that the BMSC-EVs-induced upregulation of Smad 6 could be abolished by the addition of SB431542 (C, n = 5; the data were revealed as fold changes to control NSCs, Student’s t-test). Conversely, the addition of JSH- 23 did not alter the expression of Smad 6 in NSCs (D, n = 5; the data were presented as fold changes to control BMSC-EV treated NSCs, Student’s t-test) E. We added TGF-β to NSCs to assess the effect of TGF-β on mediating Smad 6 expression; this resulted in an increase of Smad 6 expression in NSCs. This TGF-β-induced upregula- tion of Smad 6 expression could be significantly abolished by the addition of SB431542 (n = 5; the data were presented as fold changes to control NSCs, Stu- dent’s t-test). (Smad 6 mRNA expression was normalized to GAPDH mRNA; the data were presented as mean ± S.D; *p < 0.05, **p < 0.01, ***p < 0.001, #p > 0.05.)

Article Snippet: Passage 2 NSCs or the Smad 6-knockdown NSCs were dissociated and reseeded on glass coverslips in 5% FBSDMEM/F12 for 24 h. The medium was then switched to DMEM/F12 supplemented with one of the following: BMSC- EVs or 10 ng/mL TGF-β (R&D Systems); BMSCEVs + 10 μM SB431542 [the TGF-β type I receptor kinase inhibitor (Sigma)]; BMSC-EVs + 20 ng BMP4; 10 ng/ mL TGF-β + 10 μM SB431542; 10 ng/mL TGF-β + 20 ng BMP4 (R&D Systems); 20 ng/mL IL-6 (Sigma), with or without 30 μM JSH-23 (NF-κB inhibitor, MCE); 20 ng/mL IL-6 + BMSC-EVs, with or without SB 431,542; 20 ng/mL BMP4, with or without 200 ng/mL Noggin [BMP- antagonist (Sigma)]; 20 ng/mL BMP4 + BMSC-EVs, with or without SB 431,542; 40 ng/mL IL-6 and 40 ng/mL BMP4, with 1 3 or without BMSC-EVs.

Techniques: Expressing, Enzyme-linked Immunosorbent Assay, Control

The bone morphogenetic protein (BMP) signaling pathway is activated in intestinal epithelial cells and intraepithelial lymphocytes (IELs) following ischemia/reperfusion (I/R). (A) The level of BMP4 protein (red) expression significantly increased in the mid-to-distal villus region after 6 h of I/R, according to immunofluorescence staining. (B) The expression levels of the type I BMP receptor and phosphorylated nuclear factor (p-NF)-κB were both significantly increased after 6 h of I/R in IELs. * P<0.05, 3-4 mice/group; the results are representative of three independent experiments.

Journal: International Journal of Molecular Medicine

Article Title: The interplay of BMP4 and IL-7 regulates the apoptosis of intestinal intraepithelial lymphocytes under conditions of ischemia/reperfusion

doi: 10.3892/ijmm.2018.3480

Figure Lengend Snippet: The bone morphogenetic protein (BMP) signaling pathway is activated in intestinal epithelial cells and intraepithelial lymphocytes (IELs) following ischemia/reperfusion (I/R). (A) The level of BMP4 protein (red) expression significantly increased in the mid-to-distal villus region after 6 h of I/R, according to immunofluorescence staining. (B) The expression levels of the type I BMP receptor and phosphorylated nuclear factor (p-NF)-κB were both significantly increased after 6 h of I/R in IELs. * P<0.05, 3-4 mice/group; the results are representative of three independent experiments.

Article Snippet: Recombinant BMP4 protein (cat. no. 315-27; 30 ng/ml) and recombinant murine IL-7 protein (cat. no. 217-17; 2 ng/ml) were both purchased from ProteinTech Group, Inc. Pyrrolidine dithiocarbamate (PDTC; cat. no. S1808; 30 ng/ml), an inhibitor of NF-κB, was purchased from Beyotime Institute of Biotechnology (Wuhan, China).

Techniques: Expressing, Immunofluorescence, Staining

Activation of nuclear factor (NF)-κB signaling by bone morphogenetic protein (BMP)4 stimulation in intraepithelial lymphocytes (IELs). Flow cytometry determined the expression of the BMP type I receptor and phosphorylated NF-κB in IELs in culture. Following treatment with BMP4 for 6 h, the expression of the BMP type I receptor and phosphorylated NF-κB was significantly increased compared with that in the control group. NOGGIN partially decreased the expression of the BMP type I receptor, as well as NF-κB transcriptional activity. The results are representative of three independent experiments. P<0.05.

Journal: International Journal of Molecular Medicine

Article Title: The interplay of BMP4 and IL-7 regulates the apoptosis of intestinal intraepithelial lymphocytes under conditions of ischemia/reperfusion

doi: 10.3892/ijmm.2018.3480

Figure Lengend Snippet: Activation of nuclear factor (NF)-κB signaling by bone morphogenetic protein (BMP)4 stimulation in intraepithelial lymphocytes (IELs). Flow cytometry determined the expression of the BMP type I receptor and phosphorylated NF-κB in IELs in culture. Following treatment with BMP4 for 6 h, the expression of the BMP type I receptor and phosphorylated NF-κB was significantly increased compared with that in the control group. NOGGIN partially decreased the expression of the BMP type I receptor, as well as NF-κB transcriptional activity. The results are representative of three independent experiments. P<0.05.

Article Snippet: Recombinant BMP4 protein (cat. no. 315-27; 30 ng/ml) and recombinant murine IL-7 protein (cat. no. 217-17; 2 ng/ml) were both purchased from ProteinTech Group, Inc. Pyrrolidine dithiocarbamate (PDTC; cat. no. S1808; 30 ng/ml), an inhibitor of NF-κB, was purchased from Beyotime Institute of Biotechnology (Wuhan, China).

Techniques: Activation Assay, Flow Cytometry, Expressing, Control, Activity Assay

Bone morphogenetic protein (BMP)4 induces intraepithelial lymphocytes (IELs) to undergo apoptosis. Intestinal IELs were examined by flow cytometry for markers of apoptosis (FITC-Annexin V and PI). FITC-Annexin V + /PI + indicates late apoptosis, FITC-Annexin V + /PI − indicates early apoptosis, and FITC-Annexin V − /PI − indicates live cells. The extent of apoptosis of IELs after treatment with BMP4 for 6 h was then determined. The expression of FITC-Annexin V + /PI + IELs in the BMP4 group was significantly higher compared with that in the control group, but these effects were decreased by treatment with NOGGIN or pyrrolidine dithiocarbamate (PDTC). P<0.05, 3-4 mice/group; each experiment was repeated three times.

Journal: International Journal of Molecular Medicine

Article Title: The interplay of BMP4 and IL-7 regulates the apoptosis of intestinal intraepithelial lymphocytes under conditions of ischemia/reperfusion

doi: 10.3892/ijmm.2018.3480

Figure Lengend Snippet: Bone morphogenetic protein (BMP)4 induces intraepithelial lymphocytes (IELs) to undergo apoptosis. Intestinal IELs were examined by flow cytometry for markers of apoptosis (FITC-Annexin V and PI). FITC-Annexin V + /PI + indicates late apoptosis, FITC-Annexin V + /PI − indicates early apoptosis, and FITC-Annexin V − /PI − indicates live cells. The extent of apoptosis of IELs after treatment with BMP4 for 6 h was then determined. The expression of FITC-Annexin V + /PI + IELs in the BMP4 group was significantly higher compared with that in the control group, but these effects were decreased by treatment with NOGGIN or pyrrolidine dithiocarbamate (PDTC). P<0.05, 3-4 mice/group; each experiment was repeated three times.

Article Snippet: Recombinant BMP4 protein (cat. no. 315-27; 30 ng/ml) and recombinant murine IL-7 protein (cat. no. 217-17; 2 ng/ml) were both purchased from ProteinTech Group, Inc. Pyrrolidine dithiocarbamate (PDTC; cat. no. S1808; 30 ng/ml), an inhibitor of NF-κB, was purchased from Beyotime Institute of Biotechnology (Wuhan, China).

Techniques: Flow Cytometry, Expressing, Control

Inhibition of bone morphogenetic protein (BMP)4 induces the apoptosis of intraepithelial lymphocytes (IELs) that has been stimulated by interleukin (IL)-7. Flow cytometry and apoptosis markers (FITC-Annexin V and PI) were used to examine IEL apoptosis after treatment with BMP4, IL-7 or BMP4 + IL-7 for 6 h. The expression of FITC-Annexin V + /PI + IELs in the IL-7 treatment group was significantly lower compared with that in the control group, whereas the expression of FITC-Annexin V + /PI + IELs in the BMP4 treatment group was significantly higher compared with that in the control group. However, the expression of FITC-Annexin V + /PI + IELs in the BMP4 + IL-7 treatment group exhibited no changes compared with the control group. Each experiment was repeated three times; 4-5 mice/group. P<0.05.

Journal: International Journal of Molecular Medicine

Article Title: The interplay of BMP4 and IL-7 regulates the apoptosis of intestinal intraepithelial lymphocytes under conditions of ischemia/reperfusion

doi: 10.3892/ijmm.2018.3480

Figure Lengend Snippet: Inhibition of bone morphogenetic protein (BMP)4 induces the apoptosis of intraepithelial lymphocytes (IELs) that has been stimulated by interleukin (IL)-7. Flow cytometry and apoptosis markers (FITC-Annexin V and PI) were used to examine IEL apoptosis after treatment with BMP4, IL-7 or BMP4 + IL-7 for 6 h. The expression of FITC-Annexin V + /PI + IELs in the IL-7 treatment group was significantly lower compared with that in the control group, whereas the expression of FITC-Annexin V + /PI + IELs in the BMP4 treatment group was significantly higher compared with that in the control group. However, the expression of FITC-Annexin V + /PI + IELs in the BMP4 + IL-7 treatment group exhibited no changes compared with the control group. Each experiment was repeated three times; 4-5 mice/group. P<0.05.

Article Snippet: Recombinant BMP4 protein (cat. no. 315-27; 30 ng/ml) and recombinant murine IL-7 protein (cat. no. 217-17; 2 ng/ml) were both purchased from ProteinTech Group, Inc. Pyrrolidine dithiocarbamate (PDTC; cat. no. S1808; 30 ng/ml), an inhibitor of NF-κB, was purchased from Beyotime Institute of Biotechnology (Wuhan, China).

Techniques: Inhibition, Flow Cytometry, Expressing, Control

Interleukin (IL)-7 downregulates the bone morphogenetic protein (BMP) signaling pathway in intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs). (A) Western blot analysis was used to determine the expression of BMP4 in IEC-6 cells following treatment with IL-7 for 6 h. The expression of BMP4 was significantly decreased compared with that in the control group. (B) Flow cytometry, was used to detect the phosphorylation of nuclear factor (NF)-κB following treatment with IL-7 for 6 h. The expression of phosphorylated NF-κB was significantly decreased compared with that in the control group. Each experiment was repeated three times; 4-5 mice/group. * P<0.05 vs. control. GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

Journal: International Journal of Molecular Medicine

Article Title: The interplay of BMP4 and IL-7 regulates the apoptosis of intestinal intraepithelial lymphocytes under conditions of ischemia/reperfusion

doi: 10.3892/ijmm.2018.3480

Figure Lengend Snippet: Interleukin (IL)-7 downregulates the bone morphogenetic protein (BMP) signaling pathway in intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs). (A) Western blot analysis was used to determine the expression of BMP4 in IEC-6 cells following treatment with IL-7 for 6 h. The expression of BMP4 was significantly decreased compared with that in the control group. (B) Flow cytometry, was used to detect the phosphorylation of nuclear factor (NF)-κB following treatment with IL-7 for 6 h. The expression of phosphorylated NF-κB was significantly decreased compared with that in the control group. Each experiment was repeated three times; 4-5 mice/group. * P<0.05 vs. control. GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

Article Snippet: Recombinant BMP4 protein (cat. no. 315-27; 30 ng/ml) and recombinant murine IL-7 protein (cat. no. 217-17; 2 ng/ml) were both purchased from ProteinTech Group, Inc. Pyrrolidine dithiocarbamate (PDTC; cat. no. S1808; 30 ng/ml), an inhibitor of NF-κB, was purchased from Beyotime Institute of Biotechnology (Wuhan, China).

Techniques: Western Blot, Expressing, Control, Flow Cytometry, Phospho-proteomics

Bone morphogenetic protein (BMP)4 regulates the interleukin (IL)-7α/CD127 signaling pathway in intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs). (A) Western blot analysis determined the expression of IL-7 in IEC-6 cells following treatment with BMP4 for 6 h. The IL-7 level was significantly decreased compared with that in the control group. (B) Flow cytometry, was used to detect the expression of CD127 and phosphorylated signal transducer and activator of transcription (STAT)5 proteins following treatment with BMP4 for 6 h. The levels of CD127 and phosphorylated STAT5 proteins were significantly decreased compared with those in the control group. Each experiment was repeated three times; 4-5 mice/group. * P<0.05 for control vs. treatment with BMP4 alone; ** P<0.05 for control vs. the BMP4 + NOGGIN group. GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

Journal: International Journal of Molecular Medicine

Article Title: The interplay of BMP4 and IL-7 regulates the apoptosis of intestinal intraepithelial lymphocytes under conditions of ischemia/reperfusion

doi: 10.3892/ijmm.2018.3480

Figure Lengend Snippet: Bone morphogenetic protein (BMP)4 regulates the interleukin (IL)-7α/CD127 signaling pathway in intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs). (A) Western blot analysis determined the expression of IL-7 in IEC-6 cells following treatment with BMP4 for 6 h. The IL-7 level was significantly decreased compared with that in the control group. (B) Flow cytometry, was used to detect the expression of CD127 and phosphorylated signal transducer and activator of transcription (STAT)5 proteins following treatment with BMP4 for 6 h. The levels of CD127 and phosphorylated STAT5 proteins were significantly decreased compared with those in the control group. Each experiment was repeated three times; 4-5 mice/group. * P<0.05 for control vs. treatment with BMP4 alone; ** P<0.05 for control vs. the BMP4 + NOGGIN group. GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

Article Snippet: Recombinant BMP4 protein (cat. no. 315-27; 30 ng/ml) and recombinant murine IL-7 protein (cat. no. 217-17; 2 ng/ml) were both purchased from ProteinTech Group, Inc. Pyrrolidine dithiocarbamate (PDTC; cat. no. S1808; 30 ng/ml), an inhibitor of NF-κB, was purchased from Beyotime Institute of Biotechnology (Wuhan, China).

Techniques: Western Blot, Expressing, Control, Flow Cytometry

miR‐1187 directly targets BMP4. (A) The predicted binding site between miR‐1187 and BMP4 by bioinformatics analysis. (B) The luciferase activity of the BMP4‐WT and BMP4‐MUT in MC3T3‐E1 cells treated with miR‐1187 mimics or NC. (C) mRNA expression of Bmp4 was significantly downregulated in the miR‐1187 mimics‐transfected group. (D) Western blot analysis for the expression of BMP4 protein in miR‐1187 mimics and inhibitor‐transfected MC3T3‐E1 cells on Pti. (E) ELISA assay analysis for the expression of supernatant BMP4 secreted protein in miR‐1187 mimics and inhibitor‐transfected MC3T3‐E1cells on Pti. All values represent means ± SD.( n = 3). * p < 0.05, ** p < 0.01.

Journal: The FASEB Journal

Article Title: Low‐Intensity Pulsed Ultrasound Promotes Osteogenesis in Porous Titanium Alloys Through miR ‐1187/ BMP4 Pathway

doi: 10.1096/fj.202403395RR

Figure Lengend Snippet: miR‐1187 directly targets BMP4. (A) The predicted binding site between miR‐1187 and BMP4 by bioinformatics analysis. (B) The luciferase activity of the BMP4‐WT and BMP4‐MUT in MC3T3‐E1 cells treated with miR‐1187 mimics or NC. (C) mRNA expression of Bmp4 was significantly downregulated in the miR‐1187 mimics‐transfected group. (D) Western blot analysis for the expression of BMP4 protein in miR‐1187 mimics and inhibitor‐transfected MC3T3‐E1 cells on Pti. (E) ELISA assay analysis for the expression of supernatant BMP4 secreted protein in miR‐1187 mimics and inhibitor‐transfected MC3T3‐E1cells on Pti. All values represent means ± SD.( n = 3). * p < 0.05, ** p < 0.01.

Article Snippet: BMP4 protein levels in the supernatant were quantified using a mouse BMP‐4 ELISA kit (EK0316, Boster, China) following the manufacturer's protocol.

Techniques: Binding Assay, Luciferase, Activity Assay, Expressing, Transfection, Western Blot, Enzyme-linked Immunosorbent Assay

BMP4 positively regulates osteogenic differentiation in MC3T3‐E1 cells. (A) Level of BMP4 decreased after transfected with different siRNA‐BMP4, si‐BMP4‐785 was identified to have the highest transfection efficiency. (B) BMP4 transcript levels was determined by RT‐PCR after transfected with overexpression plasmids of BMP4. (C) qRT‐PCR analysis. Level of Col‐1 , Alp , Runx2 , and Ocn mRNA expression was significantly downregulated in BMP4 silencing. (D) qRT‐PCR analysis. Level of Col‐1 , Alp , Runx2 , and Ocn mRNA expression was significantly upregulated in BMP4 overexpression. (E) Western blotting. Expression of BMP4 protein and osteogenesis‐related proteins COL‐1, ALP, RUNX2 as well as statistical analysis after transfecting si‐BMP4. (F) Western blotting. Expression of BMP4 protein and osteogenesis‐related proteins COL‐1, ALP, RUNX2 as well as statistical analysis after transfecting pCDNA3.1‐BMP4. (G) ALP activity detection on day 7 in si‐BMP4 and pCDNA3.1‐BMP4 transfected MC3T3‐E1cells. (H) ALP staining on day 10 in si‐BMP4 and pCDNA3.1‐BMP4 transfected MC3T3‐E1cells (scale bar = 500 μm). (I) Alizarin red S staining and quantitative analysis of Alizarin Red S accumulation on day 21 in si‐BMP4 and pCDNA3.1‐BMP4 transfected MC3T3‐E1cells (scale bar = 200 μm/100 μm), the black arrow indicate the magnified area, the magnified pictures were marked within the square frame in the image. All values represent means ± SD ( n = 3). * p < 0.05, ** p < 0.01, *** p < 0.001.

Journal: The FASEB Journal

Article Title: Low‐Intensity Pulsed Ultrasound Promotes Osteogenesis in Porous Titanium Alloys Through miR ‐1187/ BMP4 Pathway

doi: 10.1096/fj.202403395RR

Figure Lengend Snippet: BMP4 positively regulates osteogenic differentiation in MC3T3‐E1 cells. (A) Level of BMP4 decreased after transfected with different siRNA‐BMP4, si‐BMP4‐785 was identified to have the highest transfection efficiency. (B) BMP4 transcript levels was determined by RT‐PCR after transfected with overexpression plasmids of BMP4. (C) qRT‐PCR analysis. Level of Col‐1 , Alp , Runx2 , and Ocn mRNA expression was significantly downregulated in BMP4 silencing. (D) qRT‐PCR analysis. Level of Col‐1 , Alp , Runx2 , and Ocn mRNA expression was significantly upregulated in BMP4 overexpression. (E) Western blotting. Expression of BMP4 protein and osteogenesis‐related proteins COL‐1, ALP, RUNX2 as well as statistical analysis after transfecting si‐BMP4. (F) Western blotting. Expression of BMP4 protein and osteogenesis‐related proteins COL‐1, ALP, RUNX2 as well as statistical analysis after transfecting pCDNA3.1‐BMP4. (G) ALP activity detection on day 7 in si‐BMP4 and pCDNA3.1‐BMP4 transfected MC3T3‐E1cells. (H) ALP staining on day 10 in si‐BMP4 and pCDNA3.1‐BMP4 transfected MC3T3‐E1cells (scale bar = 500 μm). (I) Alizarin red S staining and quantitative analysis of Alizarin Red S accumulation on day 21 in si‐BMP4 and pCDNA3.1‐BMP4 transfected MC3T3‐E1cells (scale bar = 200 μm/100 μm), the black arrow indicate the magnified area, the magnified pictures were marked within the square frame in the image. All values represent means ± SD ( n = 3). * p < 0.05, ** p < 0.01, *** p < 0.001.

Article Snippet: BMP4 protein levels in the supernatant were quantified using a mouse BMP‐4 ELISA kit (EK0316, Boster, China) following the manufacturer's protocol.

Techniques: Transfection, Reverse Transcription Polymerase Chain Reaction, Over Expression, Quantitative RT-PCR, Expressing, Western Blot, Activity Assay, Staining

LIPUS promotes osteogenic differentiation of MC3T3‐E1 through inhibiting miR‐1187 and upregulating BMP4. (A) qRT‐PCR analysis. Effect of daily LIPUS stimulation on mRNA expression of Bmp4. (B) ELISA. Supernatant BMP4 secreted by cultured MC3T3‐E1 cells was determined by ELISA assay. (C) Western blotting. BMP4 level was analyzed by western blot after 7 days LIPUS treatment. (D) Expression of osteogenesis‐related mRNA was analyzed by qRT‐PCR after si‐BMP4 or si‐bmp4 + LIPUS treatment. (E) Expression of osteogenesis‐related protein was analyzed by western blot after si‐BMP4 or si‐BMP4 + LIPUS treatment. (F) ALP activity detection on day 7 in si‐BMP4 and si‐BMP4 + LIPUS‐treated MC3T3‐E1 cells. (G) Bmp4 and osteogenesis‐related genes Col‐1, Alp, Runx2, and Ocn expression in MC3T3‐E1 cells on Pti as indicated treatment by qRT‐PCR. (H) ALP activity in MC3T3‐E1 cells on Pti on day 7 as indicated treatment. (I) Expression of BMP4 and osteogenesis‐related proteins including COL‐1, ALP, RUNX2 in MC3T3‐E1 cells on Pti as indicated treatment by Western blot analysis. All values represent means ± SD ( n = 3). Expression of osteogenesis‐related protein was analyzed by western blot (E1) and quantitative analysis (E2) after si‐BMP4, LIPUS or si‐BMP4+LIPUS treated. Expression of BMP4 and osteogenesis‐ related proteins including COL‐ 1, ALP, RUNX2 in MC3T3‐ E1 cells on Pti as indicated treatment by Western blot analysis(I)andquantitative analysis (J). * p < 0.05, ** p < 0.01, *** p < 0.001.

Journal: The FASEB Journal

Article Title: Low‐Intensity Pulsed Ultrasound Promotes Osteogenesis in Porous Titanium Alloys Through miR ‐1187/ BMP4 Pathway

doi: 10.1096/fj.202403395RR

Figure Lengend Snippet: LIPUS promotes osteogenic differentiation of MC3T3‐E1 through inhibiting miR‐1187 and upregulating BMP4. (A) qRT‐PCR analysis. Effect of daily LIPUS stimulation on mRNA expression of Bmp4. (B) ELISA. Supernatant BMP4 secreted by cultured MC3T3‐E1 cells was determined by ELISA assay. (C) Western blotting. BMP4 level was analyzed by western blot after 7 days LIPUS treatment. (D) Expression of osteogenesis‐related mRNA was analyzed by qRT‐PCR after si‐BMP4 or si‐bmp4 + LIPUS treatment. (E) Expression of osteogenesis‐related protein was analyzed by western blot after si‐BMP4 or si‐BMP4 + LIPUS treatment. (F) ALP activity detection on day 7 in si‐BMP4 and si‐BMP4 + LIPUS‐treated MC3T3‐E1 cells. (G) Bmp4 and osteogenesis‐related genes Col‐1, Alp, Runx2, and Ocn expression in MC3T3‐E1 cells on Pti as indicated treatment by qRT‐PCR. (H) ALP activity in MC3T3‐E1 cells on Pti on day 7 as indicated treatment. (I) Expression of BMP4 and osteogenesis‐related proteins including COL‐1, ALP, RUNX2 in MC3T3‐E1 cells on Pti as indicated treatment by Western blot analysis. All values represent means ± SD ( n = 3). Expression of osteogenesis‐related protein was analyzed by western blot (E1) and quantitative analysis (E2) after si‐BMP4, LIPUS or si‐BMP4+LIPUS treated. Expression of BMP4 and osteogenesis‐ related proteins including COL‐ 1, ALP, RUNX2 in MC3T3‐ E1 cells on Pti as indicated treatment by Western blot analysis(I)andquantitative analysis (J). * p < 0.05, ** p < 0.01, *** p < 0.001.

Article Snippet: BMP4 protein levels in the supernatant were quantified using a mouse BMP‐4 ELISA kit (EK0316, Boster, China) following the manufacturer's protocol.

Techniques: Quantitative RT-PCR, Expressing, Enzyme-linked Immunosorbent Assay, Cell Culture, Western Blot, Activity Assay

LIPUS regulates bone formation in vivo. (A) Study plan of the vitro study. (B) qRT‐PCR analysis of mRNA expression of Bmp4 as well as other osteogenesis‐related gene in the de novo bone of different groups. B1: MRNA expression of Bmp4; B2, B3: Osteogenesis‐related gene including Col‐1, Alp, Runx2, and Ocn at 4 weeks and 8 weeks respectively. (C) Micro‐CT analysis. C1: 3D reconstruction of the bone defect area at week 4 and 8. More bone ingrowth is observed as time increases in each group. The white part is the scaffold and the red part is the bone tissue. C2: The POF values for the Pti at 4 and 8 weeks. The POF values differ significantly between the LIPUS and control group, between the si‐BMP4 and control group, as well as between the si‐BMP4 and si‐BMP4 + LIPUS group. (D) D1: The representative merged images of fluorescent double labeling of calcein(green color) and xylenol orange(orange color). The red square indicate the magnified area, the magnified pictures were marked within the white square frame in the image. (scale bar = 200 μm/100 μm). D2: The MAR of the four groups at 4 and 8 weeks. All values represent means ± SD ( n = 3). * p < 0.05, ** p < 0.01, *** p < 0.001.

Journal: The FASEB Journal

Article Title: Low‐Intensity Pulsed Ultrasound Promotes Osteogenesis in Porous Titanium Alloys Through miR ‐1187/ BMP4 Pathway

doi: 10.1096/fj.202403395RR

Figure Lengend Snippet: LIPUS regulates bone formation in vivo. (A) Study plan of the vitro study. (B) qRT‐PCR analysis of mRNA expression of Bmp4 as well as other osteogenesis‐related gene in the de novo bone of different groups. B1: MRNA expression of Bmp4; B2, B3: Osteogenesis‐related gene including Col‐1, Alp, Runx2, and Ocn at 4 weeks and 8 weeks respectively. (C) Micro‐CT analysis. C1: 3D reconstruction of the bone defect area at week 4 and 8. More bone ingrowth is observed as time increases in each group. The white part is the scaffold and the red part is the bone tissue. C2: The POF values for the Pti at 4 and 8 weeks. The POF values differ significantly between the LIPUS and control group, between the si‐BMP4 and control group, as well as between the si‐BMP4 and si‐BMP4 + LIPUS group. (D) D1: The representative merged images of fluorescent double labeling of calcein(green color) and xylenol orange(orange color). The red square indicate the magnified area, the magnified pictures were marked within the white square frame in the image. (scale bar = 200 μm/100 μm). D2: The MAR of the four groups at 4 and 8 weeks. All values represent means ± SD ( n = 3). * p < 0.05, ** p < 0.01, *** p < 0.001.

Article Snippet: BMP4 protein levels in the supernatant were quantified using a mouse BMP‐4 ELISA kit (EK0316, Boster, China) following the manufacturer's protocol.

Techniques: In Vivo, Quantitative RT-PCR, Expressing, Micro-CT, Control, Labeling

The schematic of LIPUS promotes osteogenesis of porous titanium alloys through inhibiting miR‐1187 and upregulating BMP4.

Journal: The FASEB Journal

Article Title: Low‐Intensity Pulsed Ultrasound Promotes Osteogenesis in Porous Titanium Alloys Through miR ‐1187/ BMP4 Pathway

doi: 10.1096/fj.202403395RR

Figure Lengend Snippet: The schematic of LIPUS promotes osteogenesis of porous titanium alloys through inhibiting miR‐1187 and upregulating BMP4.

Article Snippet: BMP4 protein levels in the supernatant were quantified using a mouse BMP‐4 ELISA kit (EK0316, Boster, China) following the manufacturer's protocol.

Techniques:

Effect of PTE on the cell cycle of MSCs in vitro and in vivo. (a) Representative cell cycle analysis for PI of MSCs cultured treatment with a different dose of PTE (30 µg/ml, 300 µg/ml) for 1 day and 3 days. PI levels of MSCs cultured increased with increasing dose and time of PTE. (b) Representative cell cycle analysis for PI of MSCs isolated from rats that were administered with different dose of PTE (3 mg/kg/day, 30 mg/kg/day) for 1 and 3 days in vivo. The PT levels of MSCs cultured increased with increasing dose and time of PTE. PTE strongly promoted increasing of PI of MSCs in vivo in time‐ and dose‐dependent manner. *P < 0.05; **P < 0.01 compared to control at the same time point. ***P < 0.05; ****P < 0.01 PI levels from 3 days MSCs cultured with and without PTE were compared to those from 1 day MSCs cultured with or without PTE. (c) Detection of CD44 expression by flow cytometry. MSCs isolated from rats that were administered with and without PTE for 3 days in vivo were analysed for expression of CD44 by flow cytometry, negative control represent MSCs incubated with FITC‐conjugated antibody alone. Vertical lines represent maximum fluorescence intensity for FITC‐conjugated antibody. CD44 expression of MSCs isolated from rats that were administered with PTE increased in dose‐dependent manner.

Journal: Cell Proliferation

Article Title: Extracts from plastrum testudinis promote proliferation of rat bone‐marrow‐derived mesenchymal stem cells

doi: 10.1111/j.1365-2184.2007.00431.x

Figure Lengend Snippet: Effect of PTE on the cell cycle of MSCs in vitro and in vivo. (a) Representative cell cycle analysis for PI of MSCs cultured treatment with a different dose of PTE (30 µg/ml, 300 µg/ml) for 1 day and 3 days. PI levels of MSCs cultured increased with increasing dose and time of PTE. (b) Representative cell cycle analysis for PI of MSCs isolated from rats that were administered with different dose of PTE (3 mg/kg/day, 30 mg/kg/day) for 1 and 3 days in vivo. The PT levels of MSCs cultured increased with increasing dose and time of PTE. PTE strongly promoted increasing of PI of MSCs in vivo in time‐ and dose‐dependent manner. *P < 0.05; **P < 0.01 compared to control at the same time point. ***P < 0.05; ****P < 0.01 PI levels from 3 days MSCs cultured with and without PTE were compared to those from 1 day MSCs cultured with or without PTE. (c) Detection of CD44 expression by flow cytometry. MSCs isolated from rats that were administered with and without PTE for 3 days in vivo were analysed for expression of CD44 by flow cytometry, negative control represent MSCs incubated with FITC‐conjugated antibody alone. Vertical lines represent maximum fluorescence intensity for FITC‐conjugated antibody. CD44 expression of MSCs isolated from rats that were administered with PTE increased in dose‐dependent manner.

Article Snippet: CD44, probes of BMP4 mRNA, digoxigenin‐labelled probe detection kit, and diaminobenzidine were purchased from Wuhan Boster Biological Technology Co., Ltd. (Wuhan, China); chemicals such as dimethyl sulphoxide (DMSO) and other reagents were also obtained from Sigma.

Techniques: In Vitro, In Vivo, Cell Cycle Assay, Cell Culture, Isolation, Control, Expressing, Flow Cytometry, Negative Control, Incubation, Fluorescence

Fig. 1 Serum levels of (A) BMP2 and (B) BMP4 in the studied groups. BMP2: Bone morphogenetic protein-2, BMP4: Bone morphogenetic protein-4.

Journal: Egyptian Journal of Pure and Applied Science

Article Title: Assessment of serum levels of bone morphogenetic proteins as sensitive biomarkers for early prediction of acute myocardial infarction.

doi: 10.21608/ejaps.2023.188530.1051

Figure Lengend Snippet: Fig. 1 Serum levels of (A) BMP2 and (B) BMP4 in the studied groups. BMP2: Bone morphogenetic protein-2, BMP4: Bone morphogenetic protein-4.

Article Snippet: Assays for BMP2 and BMP4 Serum levels of BMP2 (Cat# CSB-E04507h) and BMP4 (Cat# CSB-E17298h) were determined according to the manufacturer’s instructions of commercial sandwich enzymelinked immunosorbent assay (ELISA) kits (Cusabio, TX, USA).

Techniques:

Fig. 2 Receiver operating characteristic (ROC) curves of (A) cTnI, BMP2 and BMP4, and (B) Combined BMP2 and BMP4 to

Journal: Egyptian Journal of Pure and Applied Science

Article Title: Assessment of serum levels of bone morphogenetic proteins as sensitive biomarkers for early prediction of acute myocardial infarction.

doi: 10.21608/ejaps.2023.188530.1051

Figure Lengend Snippet: Fig. 2 Receiver operating characteristic (ROC) curves of (A) cTnI, BMP2 and BMP4, and (B) Combined BMP2 and BMP4 to

Article Snippet: Assays for BMP2 and BMP4 Serum levels of BMP2 (Cat# CSB-E04507h) and BMP4 (Cat# CSB-E17298h) were determined according to the manufacturer’s instructions of commercial sandwich enzymelinked immunosorbent assay (ELISA) kits (Cusabio, TX, USA).

Techniques:

Fig. 3 Receiver operating characteristic (ROC) curves of (A) cTnI, BMP2 and BMP4, and (B) Combined BMP2 and BMP4 to

Journal: Egyptian Journal of Pure and Applied Science

Article Title: Assessment of serum levels of bone morphogenetic proteins as sensitive biomarkers for early prediction of acute myocardial infarction.

doi: 10.21608/ejaps.2023.188530.1051

Figure Lengend Snippet: Fig. 3 Receiver operating characteristic (ROC) curves of (A) cTnI, BMP2 and BMP4, and (B) Combined BMP2 and BMP4 to

Article Snippet: Assays for BMP2 and BMP4 Serum levels of BMP2 (Cat# CSB-E04507h) and BMP4 (Cat# CSB-E17298h) were determined according to the manufacturer’s instructions of commercial sandwich enzymelinked immunosorbent assay (ELISA) kits (Cusabio, TX, USA).

Techniques:

Fig. 4 Receiver operating characteristic (ROC) curves of (A) cTnI, BMP2 and BMP4, and (B) Combined BMP2 and BMP4 to

Journal: Egyptian Journal of Pure and Applied Science

Article Title: Assessment of serum levels of bone morphogenetic proteins as sensitive biomarkers for early prediction of acute myocardial infarction.

doi: 10.21608/ejaps.2023.188530.1051

Figure Lengend Snippet: Fig. 4 Receiver operating characteristic (ROC) curves of (A) cTnI, BMP2 and BMP4, and (B) Combined BMP2 and BMP4 to

Article Snippet: Assays for BMP2 and BMP4 Serum levels of BMP2 (Cat# CSB-E04507h) and BMP4 (Cat# CSB-E17298h) were determined according to the manufacturer’s instructions of commercial sandwich enzymelinked immunosorbent assay (ELISA) kits (Cusabio, TX, USA).

Techniques:

Fig. 5 Receiver operating characteristic (ROC) curves of (A) BMP2 and (B) cTnI and BMP4 to discriminate between AMI patients without HC or DM and AMI patients with DM. AMI: Acute myocardial infarction, HC: Hypercholesterolemia, DM:

Journal: Egyptian Journal of Pure and Applied Science

Article Title: Assessment of serum levels of bone morphogenetic proteins as sensitive biomarkers for early prediction of acute myocardial infarction.

doi: 10.21608/ejaps.2023.188530.1051

Figure Lengend Snippet: Fig. 5 Receiver operating characteristic (ROC) curves of (A) BMP2 and (B) cTnI and BMP4 to discriminate between AMI patients without HC or DM and AMI patients with DM. AMI: Acute myocardial infarction, HC: Hypercholesterolemia, DM:

Article Snippet: Assays for BMP2 and BMP4 Serum levels of BMP2 (Cat# CSB-E04507h) and BMP4 (Cat# CSB-E17298h) were determined according to the manufacturer’s instructions of commercial sandwich enzymelinked immunosorbent assay (ELISA) kits (Cusabio, TX, USA).

Techniques: