Journal: Molecular Cancer

Article Title: A positive feed-forward loop between LncRNA-URRCC and EGFL7/P-AKT/FOXO3 signaling promotes proliferation and metastasis of clear cell renal cell carcinoma

doi: 10.1186/s12943-019-0998-y

Figure Lengend Snippet: URRCC enhances EGFL7 level by mediating histone H3 acetylation of EGFL7 promoter. a : URRCC subnetwork according to the result of Target mRNA PCR Array. Genes colored in blue are down-regulated genes after that cells were transfected with sh-URRCC. Genes colored in red are up-regulated genes after that cells were transfected with sh-URRCC. The size of the gene round represents the fold change. b : The mRNA and protein levels of EGFL7 were detected by qRT-PCR and WB assays in A498 and OSRC-2 cells after transfection with sh-control or sh-URRCC. c : The mRNA and protein levels of EGFL7 were detected by qRT-PCR and WB assays in A498 and OSRC-2 cells after transfection with mock or oe-URRCC. d : EGFL7 expression in ccRCC and normal samples from TCGA KIRC dataset. e : Representative EGFL7 IHC staining of ccRCC tissues compared to paired normal renal tissues (200×, 400×). Black scale bar represents 100 μm (200×) or 50 μm (400×). f and g : Representative EGFL7 IHC staining of xenograft tumors from sh-control, sh-URRCC, mock, and oe-URRCC groups (200×, 400×). Black scale bar represents 100 μm (200×) or 50 μm (400×). h : qRT-PCR and WB analysis of EGFL7 in A498 and OSRC-2 cells treated with DMSO or trichostatin A (TSA) (50 nM or 100 nM) for 72 h ( n = 3). i : ChIP analyses of A498 cells transfected with sh-control or sh-URRCC were conducted on the EGFL7 promoter regions using anti-acetyl-histone H3 and anti-acetyl-histone H4. Enrichment was determined relative to input controls. The data are the means ± standard deviations of three independent biological replicates. j : ChIP analyses of A498 cells transfected with sh-control or sh-URRCC were conducted on the GAPDH promoter regions using anti-acetyl-histone H3 and anti-acetyl-histone H4. Enrichment was determined relative to input controls. k : ChIP analyses of OSRC-2 cells transfected with mock or oe-URRCC were conducted on the EGFL7 promoter regions using anti-acetyl-histone H3 and anti-acetyl-histone H4. Enrichment was determined relative to input controls. The data are the means ± standard deviations of three independent biological replicates. l : EGFL7 promoter region was enriched with H3K27Ac histone mark presented with UCSC data. m : WB analysis of H3K27ac and total H3 in A498 and OSRC-2 cells treated with DMSO or TSA, β-actin was used as a loading control

Article Snippet: Immunohistochemistry for the target molecules was performed on paraffin sections using a primary antibody against EGFL7 (1:50, proteintech, 19,291–1-AP), FOXO3 (1:500, Abcam, ab12162), P-AKT (1:50, Abcam, ab131443), Ki67 (1:500, Abcam, ab92742) and the proteins in situ were visualized with 3, 3-diaminobenzidine.

Techniques: Transfection, Quantitative RT-PCR, Control, Expressing, Immunohistochemistry

Journal: Molecular Cancer

Article Title: A positive feed-forward loop between LncRNA-URRCC and EGFL7/P-AKT/FOXO3 signaling promotes proliferation and metastasis of clear cell renal cell carcinoma

doi: 10.1186/s12943-019-0998-y

Figure Lengend Snippet: URRCC is associated with EGFL7/P-AKT/FOXO3 signaling pathway. a and b : WB analysis of T-AKT, P-AKT, and FOXO3 in URRCC-overexpressing or URRCC-inhibited A498 and OSRC-2 cells compared with sh-control or mock group, β-actin was used as a loading control. c : CCK8 assays of A498 cells transfected with mock/oe-URRCC and si-NC/si-EGFL7. d : Representative images and the numbers of invasive cells per high-power field reduced after the transfection with mock/oe-URRCC and si-NC/si-EGFL7 in A498 cells. e : WB analysis for EGFL7, T-AKT, P-AKT, and FOXO3 protein levels of A498 cells transfected with mock/oe-URRCC and si-NC/si-EGFL7. β-actin was used as a loading control

Article Snippet: Immunohistochemistry for the target molecules was performed on paraffin sections using a primary antibody against EGFL7 (1:50, proteintech, 19,291–1-AP), FOXO3 (1:500, Abcam, ab12162), P-AKT (1:50, Abcam, ab131443), Ki67 (1:500, Abcam, ab92742) and the proteins in situ were visualized with 3, 3-diaminobenzidine.

Techniques: Control, Transfection

Journal: Molecular Cancer

Article Title: A positive feed-forward loop between LncRNA-URRCC and EGFL7/P-AKT/FOXO3 signaling promotes proliferation and metastasis of clear cell renal cell carcinoma

doi: 10.1186/s12943-019-0998-y

Figure Lengend Snippet: A Schematic Diagram of LncRNA-URRCC-Based Signaling Pathway in ccRCC cells proliferation and invasion. LncRNA-URRCC upregulates AKT signaling by directly targeting EGFL7 via mediating histone H3 acetylation of EGFL7 promoter, and then inducing cell growth and invasion. AKT signaling downstream FOXO3 in turn downregulates URRCC by directly binding to its promoter

Article Snippet: Immunohistochemistry for the target molecules was performed on paraffin sections using a primary antibody against EGFL7 (1:50, proteintech, 19,291–1-AP), FOXO3 (1:500, Abcam, ab12162), P-AKT (1:50, Abcam, ab131443), Ki67 (1:500, Abcam, ab92742) and the proteins in situ were visualized with 3, 3-diaminobenzidine.

Techniques: Binding Assay

Journal: Nature neuroscience

Article Title: A glycolytic shift in Schwann cells supports injured axons

doi: 10.1038/s41593-020-0689-4

Figure Lengend Snippet: a, Top: Scheme of metabolomic analysis using extracts from nerve segments. Bottom: Concentrations of key energy metabolism intermediates in control and axotomized nerve segments from C57Bl/6J mice (F6P/G6P: fructose-6-phosphate/glucose-6-phosphate. FBP: fructose-1,6-bisphosphate. GI-OH3P: Glyceraldehyde-3-phosphate. 2PG/3PG: 2-phosphoglycerate/3-phosphoglycerate. LACT: lactate) (Error bars represent s.e.m. n=5 mice per condition and metabolite). b, Top: Scheme of extracellular flux analysis of SCs purified from C57Bl/6J mouse nerves. Bottom: Box and whiskers plot (maximum, 25th percentile, median, 75th percentile, minimum) shows glycolytic activity parameters as assessed by extracellular acidification rate (ECAR) measurements in control mouse SCs and cells with Nrg1-induced ErbB2 activation (n=9 well preparations per condition, *P=0.0080, **P=0.0464, ***P<0.0001). c, Western blot analysis (cropped blot images) of control- and Nrg1-treated C57Bl/6J mouse SCs probed with the indicated antibodies. (n=6 independent pair preparations (2 separate dishes) for PFKFB3, and n=3 independent pair preparations (2 separate dishes) for LDHA quantification). d, Intracellular and extracellular (supernatant) lactate concentrations from control and Nrg1-treated mouse SC preparations normalized to cell number and cellular protein. Note decreased intracellular and increased extracellular lactate levels in SCs treated with Nrg1 for 24h, indicating greatly increased lactate extrusion (Error bars represent s.e.m. n=3 well preparations from 3 independent experiments per condition).

Article Snippet: SCs were subsequently control-treated or treated with 200 ng/ml recombinant Nrg1 (R&D Systems, 396-HB-050) for 24h, collected in RIPA buffer containing phosphatase and protease inhibitors, and then processed for protein analysis and western blotting using standard procedures.

Techniques: Control, Purification, Activity Assay, Activation Assay, Western Blot

Journal: Molecular medicine reports

Article Title: Characterization of bone marrow-derived mesenchymal stem cells from dimethyloxallyl glycine-preconditioned mice: Evaluation of the feasibility of dimethyloxallyl glycine as a mobilization agent.

doi: 10.3892/mmr.2016.4945

Figure Lengend Snippet: Figure 5. Paracrine capacity of NBM‑MSCs and DBM‑MSCs. (A) Quantification of TGF concentration in the culture supernatant of NBM‑MSCs and DBM‑MSCs. There was no significant difference between the expression levels (P>0.05). (B) Quantification of PDGF concentration in the culture supernatant of NBM‑MSCs and DBM‑MSCs. No significant difference was identified between them (P>0.05). TGF and PDGF concentrations were detected using enzyme‑linked immunosorbent assays. Data are presented as the mean ± standard deviation. BM‑MSCs, bone marrow‑derived mes enchymal stem cells from normal saline‑treated mice; DBM‑MSCs, bone marrow‑derived mesenchymal stem cells from dimethyloxallyl glycine‑pre conditioned mice; TGF, transforming growth factor; PDGF, platelet‑derived growth factor.

Article Snippet: Mouse TGF (β IG-H3) and PDGF ELISA kits (Wuhan Boster Biological Co., Ltd., Wuhan, China) were used, according to the manufacturer's protocol.

Techniques: Concentration Assay, Expressing, Standard Deviation

Journal: Arteriosclerosis, Thrombosis, and Vascular Biology

Article Title: Nrg1β Released in Remote Ischemic Preconditioning Improves Myocardial Perfusion and Decreases Ischemia/Reperfusion Injury via ErbB2-Mediated Rescue of Endothelial Nitric Oxide Synthase and Abrogation of Trx2 Autophagy

doi: 10.1161/atvbaha.121.315957

Figure Lengend Snippet: Figure 1. Superoxide-induced Nrg1 (neuregulin 1) release by the microvascular endothelial bed of the hindlimb acts as remote ischemic preconditioning (RIPC)-factor and protects the myocardium from ischemia/reperfusion (I/R)-induced injury. A, Mice were either subjected to sham or three cycles of 5 min hindlimb ischemia followed by 5 min reperfusion. Thirty minutes after the last I/R cycle, serum Nrg1 levels were determined by ELISA. Mean±SEM was plotted as a bar graph (n=5). *P<0.01 vs sham. B, Formaldehyde fixed paraffine embedded gastrocnemius muscle sections from sham or RIPC-treated mice were immunostained with anti-Nrg1 (Continued )

Article Snippet: Recombinant human Nrg1β1 active domain (catalog No. 396-HB) and neutralizing anti-Nrg1 antibody (catalog No. AF-396-NA) were bought from R&D Systems.

Techniques: Enzyme-linked Immunosorbent Assay

Journal: Arteriosclerosis, Thrombosis, and Vascular Biology

Article Title: Nrg1β Released in Remote Ischemic Preconditioning Improves Myocardial Perfusion and Decreases Ischemia/Reperfusion Injury via ErbB2-Mediated Rescue of Endothelial Nitric Oxide Synthase and Abrogation of Trx2 Autophagy

doi: 10.1161/atvbaha.121.315957

Figure Lengend Snippet: Figure 2. Remote ischemic preconditioning (RIPC) improved cardiac perfusion via Nrg1 (neuregulin 1)-dependent eNOS (endothelial nitric oxide synthase) activation. A, Mice were subjected to sham or myocardial ischemia/reperfusion (I/R) or RIPC+I/R surgery, and at the end of the reperfusion period, the nontargeted contrast agent was injected to mice via femoral vein while collecting B-mode/contrast mode images of the heart from long-axis view using Vevo 3100. To block the function of circulating Nrg1 in mice, neutralizing anti-Nrg1 antibodies (150 µg/kg) was administered to mice before RIPC and then subjected to RIPC+I/R injury. B, Contrast intensities in the left ventricle (LV) anterior wall downstream to the ligation site were quantitated and plotted over time. Loss of peak height and the rightward shift of peak indicates hypoperfusion. C, From the rate of contrast agent intensity change, the perfusion index was calculated. Percentage of perfusion was calculated based on the perfusion index assuming its level in the sham group is 100% and blotted as a bar graph (n=5) and shown as a heat map over the anterior LV in A. Values are means±SEM (n=5 mice). *P<0.01 vs sham, **P<0.01 vs I/R, §P<0.01 vs RIPC+I/R (ANOVA). D, Left coronary artery from mice were isolated, and after indicated treatments, NO formation was detected by electron spin resonance (EPR) spectrometry using NO spin trap Fe2+-(N-methyl-D-glucamine dithiocarbamate) 2 (Fe-[MGD]2) as described in methods. E, NO-Fe(MGD) 2 spin count was quantified and plotted as a bar graph (n=5). *P<0.01 vs sham; **P<0.01 vs I/R (ANOVA). F–H, HMVECs were exposed to 2 h hypoxia followed by 1-hour reoxygenation, and the medium was collected (preconditioned medium [PM]). HCAECs were treated with PM for the indicated period, lysed, and cell lysates were collected. An equal amount of cell lysates were analyzed for eNOS activity (F) and plotted as a bar graph (n=3). *P<0.01 vs control (ANOVA). An equal amount of cell lysates were analyzed for eNOS phosphorylation at Ser 1177 by Western blotting using its phospho-specific antibodies and normalized with total eNOS levels (G), or the cell lysates were immunoprecipitated with anti-eNOS antibodies, and the immunoprecipitates were analyzed by Western blotting using anti-phospho-tyrosine specific antibodies (H). (Continued )

Article Snippet: Recombinant human Nrg1β1 active domain (catalog No. 396-HB) and neutralizing anti-Nrg1 antibody (catalog No. AF-396-NA) were bought from R&D Systems.

Techniques: Activation Assay, Injection, Blocking Assay, Ligation, Isolation, Electron Paramagnetic Resonance, Activity Assay, Control, Phospho-proteomics, Western Blot, Immunoprecipitation

Journal: Arteriosclerosis, Thrombosis, and Vascular Biology

Article Title: Nrg1β Released in Remote Ischemic Preconditioning Improves Myocardial Perfusion and Decreases Ischemia/Reperfusion Injury via ErbB2-Mediated Rescue of Endothelial Nitric Oxide Synthase and Abrogation of Trx2 Autophagy

doi: 10.1161/atvbaha.121.315957

Figure Lengend Snippet: Figure 3. Only preischemic and not postischemic Nrg1β (neuregulin 1) administration protects myocardium due to loss of endothelial-ErbB2 (Erb-B2 receptor tyrosine kinase 2) during ischemia. A, To determine the protective function of Nrg1 during ischemia or reperfusion, recombinant Nrg1β (4 µg/kg) was injected into mice before ischemia (preischemia) or after ischemia (postischemia) but before reperfusion. After ischemia/reperfusion (I/R), the heart was isolated and perfused with annexin-V-Fe complex. The infarcted tissue was excised, and tissue bound annexin-V was quantified by electron spin resonance (EPR). B, The absolute spin count was calculated from the EPR spectra of paramagnetic-Fe bound to annexin-V and plotted as a bar graph. Values are means±SD (n=5 mice). *P<0.01 vs sham; **P<0.01 vs I/R, †P<0.01 vs Nrg1 (preischemic) plus IR (ANOVA). C, Mice were subjected to sham, I/R, remote ischemic preconditioning (RIPC) or RIPC+I/R, and the infarcted tissue region was excised. Protein extract was prepared from the excised tissue and analyzed by Western blotting for ErbB2 and ErbB4 levels. D, Sections of sham and I/R mouse heart were subjected to immunofluorescence staining using anti-ErbB2 and anti-α-actinin (cardiomyocyte marker) antibodies. Isolectin-Alexa Fluor 647 conjugate was used to stain endothelial cells selectively. Fluorescent images of the stained sections were obtained using an upright Zeiss fluorescence microscope (AxioImager Z2) via 40×/1.4 NA objective. Scale bar=20 mm. E and F, Adult mouse cardiomyocytes and mouse cardiac endothelial cells were isolated from adult mouse heart, and cell lysate was prepared. An equal amount of protein from cell lysates was analyzed for ErbB2 levels by Western blotting. Blot was reprobed for α-actinin and CD31 (F). ErbB2 levels were quantified and plotted as a bar graph (n=3). *P<0.01 vs MCEC (Student t test). G, HCAECs were pretreated with preconditioned medium (PM) or Nrg1-neutralized PM, then exposed to hypoxia/reoxygenation (H/R), and cell lysates were prepared. An equal amount of protein from each sample was analyzed for ErbB2 and ErbB4 levels by Western blotting. H, HCAECs were pretreated with or without PM and exposed to H/R. At the end of treatment, cells undergoing apoptosis were labeled with annexin V-FITC conjugate, and the percentage of apoptotic cells was quantitated by fluorescence- activated cell sorting analysis using Attune NxT Flow Cytometer and plotted as a bar graph (n=3). *P<0.01 vs normoxia, **P<0.01 vs H/R (ANOVA). I, HCAECs were transfected with nontarget (NT) or ErbB4 or ErbB4 siRNA (100 nmol/L), and after recovery from transfection, they were treated with or without PM and exposed to H/R. Cells undergoing apoptosis were labeled with annexin V-FITC conjugate, and the percentage of apoptotic cells was quantitated and plotted as a bar graph (n=3). *P<0.01 vs NT siRNA normoxia, **P<0.01 vs NT siRNA H/R; †P<0.01 vs NT siRNA PM+H/R (ANOVA). ANOVA followed by Tukey post test was performed using GraphPad-Prism software (version 8).

Article Snippet: Recombinant human Nrg1β1 active domain (catalog No. 396-HB) and neutralizing anti-Nrg1 antibody (catalog No. AF-396-NA) were bought from R&D Systems.

Techniques: Recombinant, Injection, Isolation, Electron Paramagnetic Resonance, Western Blot, Immunofluorescence, Staining, Marker, Fluorescence, Microscopy, Labeling, FACS, Flow Cytometry, Transfection, Software

Journal: Arteriosclerosis, Thrombosis, and Vascular Biology

Article Title: Nrg1β Released in Remote Ischemic Preconditioning Improves Myocardial Perfusion and Decreases Ischemia/Reperfusion Injury via ErbB2-Mediated Rescue of Endothelial Nitric Oxide Synthase and Abrogation of Trx2 Autophagy

doi: 10.1161/atvbaha.121.315957

Figure Lengend Snippet: Figure 6. Endothelial-ErbB2 (Erb-B2 receptor tyrosine kinase 2) directly associates with Src and activate eNOS (endothelial nitric oxide synthase). A, Human coronary artery endothelial cells (HCAECs) were treated with preconditioned medium (PM) for the indicated period, and cell lysates were prepared. An equal amount of protein from cell lysates was immunoprecipitated using the anti-ErbB2 antibody. The immunoprecipitates were analyzed by Western blotting for tyrosine phosphorylation of ErbB2, level of associated Src, ErbB4, and ErbB2 using their specific antibodies. B, HCAECs were treated with CM for 1 or 4 h, and proximity ligation assay (PLA) was performed using anti-ErbB2 and anti- Src antibodies. Scale bar=20 mm. C, PLA signals were counted and plotted as a bar graph (n=5). *P<0.01 vs control (ANOVA). D, To determine the role of Nrg1 (neuregulin 1) released by HMVEC in PM, PM was pretreated with neutralizing anti-Nrg1 and then incubated with HCAECs for 1 h. At the end of treatment, cell lysates were prepared and analyzed for ErbB2 tyrosine phosphorylation and its interaction with Src immunoprecipitation followed by Western blotting. E, HCAECs were incubated with PM or Nrg1 neutralized-PM for 1 h. and PLA was performed using anti-ErbB2 and anti-Src antibodies. Scale bar=20 mm. F, PLA signals were counted and plotted as a bar graph (n=5). *P<0.01 vs control (ANOVA). G, HCAECs were pretreated with Herceptin and incubated with PM for 1 h, and cell lysates were prepared. An equal amount of proteins from cell lysates were immunoprecipitated with anti-ErbB2 antibodies, and the immunocomplexes were analyzed for associated Src by Western blotting. H, HCAEC were transfected with ErbB2 siRNA, treated with PM for 1 h, and cell lysates were prepared and analyzed for eNOS tyrosine phosphorylation. I, HCAECs were pretreated with control IgG, Herceptin, or Nrg1 neutralizing antibodies and then incubated with PM for 1 h, and cell lysates were prepared. An equal amount of proteins from cell lysates were analyzed for eNOS-Tyr81 phosphorylation by Western blotting using its specific antibodies. J, HCAECs were pretreated with control IgG or Herceptin and incubated with PM for 1 h, and cell lysates were prepared. An equal amount of protein from cell lysates was analyzed for eNOS activity and plotted as a bar graph. *P<0.01 vs control IgG, **P<0.01 vs control IgG+PM (ANOVA).

Article Snippet: Recombinant human Nrg1β1 active domain (catalog No. 396-HB) and neutralizing anti-Nrg1 antibody (catalog No. AF-396-NA) were bought from R&D Systems.

Techniques: Immunoprecipitation, Western Blot, Phospho-proteomics, Proximity Ligation Assay, Control, Incubation, Transfection, Activity Assay

Journal: Arteriosclerosis, Thrombosis, and Vascular Biology

Article Title: Nrg1β Released in Remote Ischemic Preconditioning Improves Myocardial Perfusion and Decreases Ischemia/Reperfusion Injury via ErbB2-Mediated Rescue of Endothelial Nitric Oxide Synthase and Abrogation of Trx2 Autophagy

doi: 10.1161/atvbaha.121.315957

Figure Lengend Snippet: Figure 7. Endothelial ErbB2 (Erb-B2 receptor tyrosine kinase 2) dimerizes with ErbB4, recruits Src and mediates Nrg1 (neuregulin 1)-dependent eNOS (endothelial nitric oxide synthase) activation during ischemic preconditioning. A, HCAECs were treated with preconditioned medium (PM) for the indicated period, and cell lysates were prepared. An equal amount of protein from cell lysates was immunoprecipitated using anti-ErbB4 antibody, and the immunoprecipitates were analyzed by Western blotting for tyrosine phosphorylation of ErbB4 and associated ErbB2 levels using their specific antibodies. B, To study the in vivo interaction of ErbB2 and ErbB4, HCAECs were treated with PM for 1 or 4 h, and proximity ligation assay (PLA) was performed using anti-ErbB2 and anti-ErbB4 antibodies. Scale bar=20 mm. C, Green foci-proximity signals of ErbB2 and ErbB2 association were counted and plotted as a bar graph. *P<0.01 vs control (ANOVA). D–F, HCAECs were incubated with PM or Nrg1 neutralized-PM for 1 h, and either cell lysates were prepared and analyzed for ErbB4 tyrosine phosphorylation and its interaction with ErbB2 by Western blotting as described in A or subjected to PLA (E) using anti-ErbB2 and anti-ErbB4 antibodies as described in B. PLA signals were counted and plotted as a bar graph (n=5), Scale bar=20 mm (F). *P<0.01 vs control IgG; **P<0.01 vs neutralizing anti-Nrg1 antibody+PM. G–J, HCAECs were transfected with ErbB4 siRNA, treated with PM for 1 h., and the cell lysates were prepared and analyzed for ErbB2 tyrosine phosphorylation (G), Src activation (H), or eNOS tyrosine phosphorylation (I). An equal amount of protein from cell lysates was analyzed for eNOS activity (J). *P<0.01 vs nontarget (NT) siRNA; **P<0.01 vs NT siRNA+PM (ANOVA). K, To study the role of ErbB2 and ErbB4 in NO formation in coronary arteries, left coronary artery were isolated and incubated with control IgG, neutralizing anti-ErbB2 or neutralizing anti-ErbB4 antibodies, and NO release in response to ACh (10 µmol/L) was determined by electron spin resonance (EPR) using Fe- (MGD)2. L, Spin count of the NO-Fe(MGD)2 was calculated from EPR signals were plotted as a bar graph. *P<0.01 vs control IgG (ANOVA).

Article Snippet: Recombinant human Nrg1β1 active domain (catalog No. 396-HB) and neutralizing anti-Nrg1 antibody (catalog No. AF-396-NA) were bought from R&D Systems.

Techniques: Activation Assay, Immunoprecipitation, Western Blot, Phospho-proteomics, In Vivo, Proximity Ligation Assay, Control, Incubation, Transfection, Activity Assay, Isolation, Electron Paramagnetic Resonance

Journal: Acta diabetologica

Article Title: A rare missense variant in the milk fat globule-EGF factor 8 (MFGE8) increases T2DM susceptibility and cardiovascular disease risk with population-specific effects

doi: 10.1007/s00592-019-01463-x

Figure Lengend Snippet: a The distribution of circulating Mfge8 concentrations by MFGE8 genotypes. b The distribution of serum triglyceride levels by MFGE8 genotypes. p values are from the analysis of covariance (ANCOVA) showing difference between group means after adjusting for the confounding effects of age, gender, and BMI. Serum Mfge8 measures were available in 78 subjects including 39 T2DM cases and age- and gender-matched 39 controls

Article Snippet: Circulating concentrations of Mfge8 levels were quantified using frozen serum aliquots by enzyme-linked immunosorbent assay (ELISA) kits from Boster Biological Technology (Pleasanton, CA, USA) following the standard protocols following manufacturer’s instructions. ( www.bosterbio.com ).

Techniques:

Journal: Acta diabetologica

Article Title: A rare missense variant in the milk fat globule-EGF factor 8 (MFGE8) increases T2DM susceptibility and cardiovascular disease risk with population-specific effects

doi: 10.1007/s00592-019-01463-x

Figure Lengend Snippet: Multivariate regression analysis showing interactions between [T2DM status * Mfge8 concentrations] and [MFGE8 genotype * Mfge8 concentrations] for affecting triglyceride levels

Article Snippet: Circulating concentrations of Mfge8 levels were quantified using frozen serum aliquots by enzyme-linked immunosorbent assay (ELISA) kits from Boster Biological Technology (Pleasanton, CA, USA) following the standard protocols following manufacturer’s instructions. ( www.bosterbio.com ).

Techniques:

Journal: Acta diabetologica

Article Title: A rare missense variant in the milk fat globule-EGF factor 8 (MFGE8) increases T2DM susceptibility and cardiovascular disease risk with population-specific effects

doi: 10.1007/s00592-019-01463-x

Figure Lengend Snippet: Distribution of rs371227978 ( MFGE8 ) genotypes and allele frequencies in study samples stratified by diabetes status and association testing using logistic regression modeling

Article Snippet: Circulating concentrations of Mfge8 levels were quantified using frozen serum aliquots by enzyme-linked immunosorbent assay (ELISA) kits from Boster Biological Technology (Pleasanton, CA, USA) following the standard protocols following manufacturer’s instructions. ( www.bosterbio.com ).

Techniques:

Journal: Acta diabetologica

Article Title: A rare missense variant in the milk fat globule-EGF factor 8 (MFGE8) increases T2DM susceptibility and cardiovascular disease risk with population-specific effects

doi: 10.1007/s00592-019-01463-x

Figure Lengend Snippet: Multivariate linear regression analysis modeling showing genotype–phenotype association of MFGE8 variant for affecting serum Mfge8 concentrations

Article Snippet: Circulating concentrations of Mfge8 levels were quantified using frozen serum aliquots by enzyme-linked immunosorbent assay (ELISA) kits from Boster Biological Technology (Pleasanton, CA, USA) following the standard protocols following manufacturer’s instructions. ( www.bosterbio.com ).

Techniques: Variant Assay