Journal: Investigative Ophthalmology & Visual Science

Article Title: Antimicrobial Peptides Derived from the Immune Defense Protein CAP37 Inhibit TLR4 Activation by S100A9

doi: 10.1167/iovs.61.4.16

Figure Lengend Snippet: Identification of proteins pulled down by CAP37. Corneal epithelial cells hTCEpi were incubated with TriCEPS conjugated to insulin or CAP37. Cell pellets were analyzed by mass spectrometry at Dualsystems Biotech AG. The resulting volcano plot is shown. Each identified protein is plotted according to its relative abundance in CAP37 versus insulin samples on the x -axis (log2 of fold change) and according to its adjusted P value on the y -axis. The upper right quadrant delimited by the bold lines shows the most significant CAP37-interacting candidates. SLPI, secretory leukocyte protease inhibitor; Rab-3A, Ras-related small GTPase 3A.

Article Snippet: CAP37 (Azurocidin, 16-14-012621), neutrophil elastase (NE, 16-14-051200), and cathepsin G (CG, 16-14-030107), purified from human neutrophils, were purchased from Athens Research and Technology (Athens, GA, USA).

Techniques: Incubation, Mass Spectrometry, Protease Inhibitor

Journal: Investigative Ophthalmology & Visual Science

Article Title: Antimicrobial Peptides Derived from the Immune Defense Protein CAP37 Inhibit TLR4 Activation by S100A9

doi: 10.1167/iovs.61.4.16

Figure Lengend Snippet: Significant CAP37-Interacting Partner Candidates

Article Snippet: CAP37 (Azurocidin, 16-14-012621), neutrophil elastase (NE, 16-14-051200), and cathepsin G (CG, 16-14-030107), purified from human neutrophils, were purchased from Athens Research and Technology (Athens, GA, USA).

Techniques:

Journal: Investigative Ophthalmology & Visual Science

Article Title: Antimicrobial Peptides Derived from the Immune Defense Protein CAP37 Inhibit TLR4 Activation by S100A9

doi: 10.1167/iovs.61.4.16

Figure Lengend Snippet: CAP37 and four CAP37-derived peptides directly bind S100A9 in vitro. ELISA plates were coated with the indicated target proteins and peptides. ( A , C ) His-tagged S100A9 was added to the coated wells at 0 or 10 nM, and binding was quantified using anti-His tag antibody. Bar graph shows the mean of OD values ± SEM from three independent experiments, each done in triplicate. For each experiment, values obtained with 0-nM S100A9 were subtracted as background. A one-way ANOVA followed by Dunnett's multiple comparisons test was used to compare the interaction of S100A9 with each protein ( A ) or peptide ( C ) to the interaction of S100A9 with BSA. Significances of *** P < 0.001 and **** P < 0.0001 are shown. ( B ) Binding of increasing concentrations of S100A9 to indicated proteins. Data points are mean ± SEM of values obtained from three independent experiments, each done in duplicate. Experimental results were fit to a nonlinear regression curve using GraphPad Prism. For statistical analysis, a two-way ANOVA, followed by Dunnett's multiple comparisons test, was used to compare the interaction of each protein to that of BSA at the same concentration of S100A9. Significances of *** P < 0.001 and **** P < 0.0001 are shown. ( D ) Binding of increasing concentrations of S100A9 to the indicated peptides. Results are plotted and analyzed as described in ( B ). Binding of S100A9 to peptides 20-44 and 120-146 WH had significance of * P < 0.05 at 5 nM and significance of **** P < 0.0001 at all tested doses of S100A9 above 5 nM. Binding of S100A9 to peptides 20-44 5R-MP and 120-146 WH 5R-MP had maximum significance ( **** P < 0.0001) at all tested doses of S100A9. Binding of peptides 95-122 and 95-122 5R-MP was not significant at any tested dose of S100A9.

Article Snippet: CAP37 (Azurocidin, 16-14-012621), neutrophil elastase (NE, 16-14-051200), and cathepsin G (CG, 16-14-030107), purified from human neutrophils, were purchased from Athens Research and Technology (Athens, GA, USA).

Techniques: Derivative Assay, In Vitro, Enzyme-linked Immunosorbent Assay, Binding Assay, Concentration Assay

Journal: Investigative Ophthalmology & Visual Science

Article Title: Antimicrobial Peptides Derived from the Immune Defense Protein CAP37 Inhibit TLR4 Activation by S100A9

doi: 10.1167/iovs.61.4.16

Figure Lengend Snippet: Binding of CAP37-Derived Peptides to S100A9 and TLR4 and the Effect on TLR4 Activation

Article Snippet: CAP37 (Azurocidin, 16-14-012621), neutrophil elastase (NE, 16-14-051200), and cathepsin G (CG, 16-14-030107), purified from human neutrophils, were purchased from Athens Research and Technology (Athens, GA, USA).

Techniques: Binding Assay, Activation Assay

Journal: Investigative Ophthalmology & Visual Science

Article Title: Antimicrobial Peptides Derived from the Immune Defense Protein CAP37 Inhibit TLR4 Activation by S100A9

doi: 10.1167/iovs.61.4.16

Figure Lengend Snippet: Potential interacting residues within region 20-44 of CAP37. ( A ) The native amino acid sequence of region 20-44 of CAP37 is shown. Shaded residues are nested inside the protein. All other residues are partly or fully exposed at the surface of the protein and could potentially be involved in the interaction with S100A9. ( B ) A ribbon representation of CAP37 made in PYMOL is shown. The 20-44 region is shown in red. It is partly exposed to the surface. ( C ) A surface representation of CAP37 made in PyMOL is shown in the same orientation of the protein shown in ( B ). Small patches of the 20-44 region are exposed at the surface, as shown in red.

Article Snippet: CAP37 (Azurocidin, 16-14-012621), neutrophil elastase (NE, 16-14-051200), and cathepsin G (CG, 16-14-030107), purified from human neutrophils, were purchased from Athens Research and Technology (Athens, GA, USA).

Techniques: Sequencing

Journal: Investigative Ophthalmology & Visual Science

Article Title: Antimicrobial Peptides Derived from the Immune Defense Protein CAP37 Inhibit TLR4 Activation by S100A9

doi: 10.1167/iovs.61.4.16

Figure Lengend Snippet: Potential interacting residues within region 120-146 of CAP37. ( A ) The native amino acid sequence of region 120-146 of CAP37 is shown. The shaded residues are nested inside the protein. All other residues are exposed at the surface of the protein. ( B ) A ribbon representation of CAP37 made in PyMOL is shown. The 120-146 region is shown in blue. It is arranged in a hairpin fashion, with two anti-parallel β-sheets that are partly buried and a large loop exposed at the surface. This surface loop contains residues Q131 and R132 (shown in yellow) that have been modified to W131 and H132 in the CAP37-derived peptide described in this study (peptide 120-146 WH). ( C ) A surface representation of CAP37 made in PyMOL is shown in the same orientation of the protein shown in ( B ). The surface loop is indicated in blue and yellow as in ( B ). It is apparent that the first five and last six residues of this region of CAP37 are surface exposed and together form another potential interacting domain in CAP37.

Article Snippet: CAP37 (Azurocidin, 16-14-012621), neutrophil elastase (NE, 16-14-051200), and cathepsin G (CG, 16-14-030107), purified from human neutrophils, were purchased from Athens Research and Technology (Athens, GA, USA).

Techniques: Sequencing, Modification, Derivative Assay

Journal: Investigative Ophthalmology & Visual Science

Article Title: Antimicrobial Peptides Derived from the Immune Defense Protein CAP37 Inhibit TLR4 Activation by S100A9

doi: 10.1167/iovs.61.4.16

Figure Lengend Snippet: CAP37 and four CAP37-derived peptides directly bind TLR4/MD-2 in vitro. ELISA plates were coated with the indicated proteins and peptides. ( A , C ) His-tagged TLR4/MD-2 (at 0 or 10 nM) was added to the coated wells and binding was quantified using anti-His tag antibody. Data are mean ± SEM of OD values from three independent experiments, after values with 0-nM TLR4/MD-2 were removed as background. A one-way ANOVA, using Dunnett's multiple comparisons test, compared the binding of each protein ( A ) or peptide (B) to the binding of BSA. Significances of * P < 0.05, ** P < 0.01, and *** P < 0.001 are shown. ( B ) Dose-dependent binding of TLR4/MD-2 to indicated proteins. Data (mean ± SEM ) are fitted to a curve of nonlinear regression. A two-way ANOVA was used with Dunnett's multiple comparisons test to compare the binding of each protein to that of BSA at the same concentration of TLR4/MD-2. LPS shows a significant binding of ** P < 0.01 to TLR4/MD-2 at 50 nM and **** P < 0.0001 at all higher doses. CAP37 shows significance with ** P < 0.01 at 10 nM and **** P < 0.0001 at all higher doses of TLR4/MD-2. S100A8 showed significant binding to TLR4/MD-2 at 75 nM ( *** P < 0.001) and at 100 nM ( **** P < 0.0001). Binding of NE and CG was not significant. ( D ) Dose-dependent binding of TLR4/MD-2 to peptides. Results are plotted and analyzed as described in ( B ). At all tested doses of TLR4/MD-2, the binding of peptide 120-146WH 5R-MP showed maximum significance of **** P < 0.0001. Peptides 20-44, 20-44 5R-MP, and 120-146WH significantly bind TLR4/MD-2 at 25 nM and reach maximum significance ( **** P < 0.0001) at 50 nM. Binding of peptides 95-122 and 95-122 5R-MP was not significant at any tested dose.

Article Snippet: CAP37 (Azurocidin, 16-14-012621), neutrophil elastase (NE, 16-14-051200), and cathepsin G (CG, 16-14-030107), purified from human neutrophils, were purchased from Athens Research and Technology (Athens, GA, USA).

Techniques: Derivative Assay, In Vitro, Enzyme-linked Immunosorbent Assay, Binding Assay, Concentration Assay

Journal: Investigative Ophthalmology & Visual Science

Article Title: Antimicrobial Peptides Derived from the Immune Defense Protein CAP37 Inhibit TLR4 Activation by S100A9

doi: 10.1167/iovs.61.4.16

Figure Lengend Snippet: Effects of CAP37 and CAP37-derived peptides on TLR4. ( A ) CAP37 and peptide 20-44 are partial agonists of TLR4. The ability of increasing concentrations of S100A9, CAP37, and CAP37-derived peptides to stimulate TLR4 was measured in HEK-hTLR4 cells. SEAP production in cell medium was measured following 24-hour incubation with ligands. Data shown are mean percent activation ± SEM relative to activation induced by S100A9 at 50 nM, arbitrarily defined as 100%. Results are from three experiments, each done in triplicate. First arrow, partial activation of TLR4 by CAP37; second arrow, partial activation of TLR4 by peptide 20-44. ( B – F ) Inhibitory effects of CAP37 protein and peptides on the activation of TLR4 by S100A9. Cells were treated with S100A9 at 10 nM alone or in combination with increasing concentrations of CAP37 ( B ) or CAP37 peptides ( C – F ). Filled symbols denote preincubation of CAP37 or the indicated peptide with 0- or 10-nM S100A9 for 1 hour before treatment. Open symbols denote co-treatment with 0- or 10-nM S100A9 without preincubation before treatment. Following 24-hour treatment, SEAP production was quantified. Results show the 50% activation of TLR4, induced by 10-nM S100A9 alone, and activations below 50% with indicated concentrations of CAP37 or CAP37 peptides. Data shown are mean ± SEM from three experiments, each done in triplicate. A two-way ANOVA, followed by Dunnett's multiple comparisons test, compared the percent activation of hTLR4 by S100A9 alone with that of S100A9 combined with CAP37 or peptide. Statistical significances of inhibitions are indicated on the graphs as follows: * P < 0.05; ** P < 0.01; *** P < 0.001; and **** P < 0.0001.

Article Snippet: CAP37 (Azurocidin, 16-14-012621), neutrophil elastase (NE, 16-14-051200), and cathepsin G (CG, 16-14-030107), purified from human neutrophils, were purchased from Athens Research and Technology (Athens, GA, USA).

Techniques: Derivative Assay, Incubation, Activation Assay

Journal: Oncology reports

Article Title: Decreased concentrations of retinol-binding protein 4 in sera of epithelial ovarian cancer patients: a potential biomarker identified by proteomics.

doi: 10.3892/or.2011.1513

Figure Lengend Snippet: Figure 3. Verification of altered RBP4 concentration. (A) Absolute RBP4 con centrations in serum samples were determined by ELISA. Each measurement represents average value from 3 replicates. Individual serum RBP4 concen trations can be found in Tables I and II. (B) Western blot analysis of RBP4 concentration in individual serum samples was performed. To enable relative comparison between healthy controls and patients five control and five patient samples (10 µg protein each) were run on each gel and processed simultane ously. Membranes were re-probed with anti-human IgG (HC) as an internal standard.

Article Snippet: The quantitative determination of human retinolbinding protein 4 (RBP4), α-1-antitrypsin and apolipoprotein A4 concentrations in patient and control sera was performed in triplicates using the Quantikine Human RBP4 immunoassay (R&D Systems, MN, USA), human apolipoprotein AIV ELISA Kit (Millipore, MA, USA) and α-1-antitrypsin Clearance ELISA (Immuno Diagnostik AG, Germany) according to the manufacturer's instructions using ELISA Reader Sunrise (Tecan, Austria).

Techniques: Concentration Assay, Enzyme-linked Immunosorbent Assay, Western Blot, Comparison, Control

Journal: Oncology reports

Article Title: Decreased concentrations of retinol-binding protein 4 in sera of epithelial ovarian cancer patients: a potential biomarker identified by proteomics.

doi: 10.3892/or.2011.1513

Figure Lengend Snippet: Figure 4. Serum retinol levels in EOC patients and age-matched healthy women. Levels of serum vitamin A (retinol) regulate RBP4 secrection by liver. Decreased retinol levels could affect RBP4 levels in our study. We therefore determined serum retinol levels in all 10 patients and controls by HPLC. Mean values of serum retinol concentrations are shown.

Article Snippet: The quantitative determination of human retinolbinding protein 4 (RBP4), α-1-antitrypsin and apolipoprotein A4 concentrations in patient and control sera was performed in triplicates using the Quantikine Human RBP4 immunoassay (R&D Systems, MN, USA), human apolipoprotein AIV ELISA Kit (Millipore, MA, USA) and α-1-antitrypsin Clearance ELISA (Immuno Diagnostik AG, Germany) according to the manufacturer's instructions using ELISA Reader Sunrise (Tecan, Austria).

Techniques:

Journal: EJNMMI Research

Article Title: Evaluation of retinol binding protein 4 and carbamoylated haemoglobin as potential renal toxicity biomarkers in adult mice treated with 177 Lu-octreotate

doi: 10.1186/s13550-014-0059-x

Figure Lengend Snippet: Mean absolute urinary RBP4 and creatinine concentrations and RBP4/creatinine concentration ratios

Article Snippet: RBP4 in urine samples (50 μL diluted to 100 μL) was analysed using the Mouse RBP4 ELISA kit (R&D Systems Europe Ltd., Abingdon, UK) according to the manufacturer's instructions.

Techniques: Concentration Assay

Journal: EJNMMI Research

Article Title: Evaluation of retinol binding protein 4 and carbamoylated haemoglobin as potential renal toxicity biomarkers in adult mice treated with 177 Lu-octreotate

doi: 10.1186/s13550-014-0059-x

Figure Lengend Snippet: Analysis of urinary RBP4. Mean differences between the log 10 -transformed mean values (from three consecutive days) and the log 10 -transformed baseline mean values (from three consecutive days) for (A) creatinine and (B) RBP4 and (C) RBP4/creatinine, in non-treated mice (blue circle, n = 4 to 6), and in mice treated with 60 MBq (red square, n = 5 to 6) or 120 MBq 177 Lu-octreotate (green diamond, n = 5 to 6) vs. time after study start. Log 10 -transformation was done since the values are skewed (see ‘ ’). All values are shown as mean ± SEM. Upward arrows indicate that the mean RBP4 value is higher and downward arrows that it is lower than presented (see text). The heavy asterisk indicates data statistically significant different from baseline ( p <0.05).

Article Snippet: RBP4 in urine samples (50 μL diluted to 100 μL) was analysed using the Mouse RBP4 ELISA kit (R&D Systems Europe Ltd., Abingdon, UK) according to the manufacturer's instructions.

Techniques: Transformation Assay

Journal: Virulence

Article Title: Altering retinol binding protein 4 levels in hepatitis C: Inflammation and steatosis matter

doi: 10.1080/21505594.2020.1838742

Figure Lengend Snippet: A schematic flow chart of the pathways affected by RBP4 . PEPCK: phosphoenolpyruvate carboxykinase; NAFLD: nonalcoholic fatty liver disease. Solid line: promotion; dashed line: secretion. IR: insulin resistance

Article Snippet: The cells were permeabilized with 0.1% Triton-100; incubated with HCV core (Anogen/YES Biotech Laboratories Ltd, Mississauga, Canada) or RBP4 antibodies [Proteintech Group, Inc., IL, USA, 1:100 dilution (low antibody concentration to avoid over staining)]; washed, and then incubated with secondary antibody.

Techniques:

Journal: Virulence

Article Title: Altering retinol binding protein 4 levels in hepatitis C: Inflammation and steatosis matter

doi: 10.1080/21505594.2020.1838742

Figure Lengend Snippet: A schematic flow chart of the enrolled subjects . CHC, patients with chronic hepatitis C virus infection; SVR, sustained virological response: IHC, immunohistochemistry studies; RBP4, retinol-binding protein 4; LAP-tTA-HCV core DTM, liver activator protein promoter-tetracycline transactivator-HCV core double transgenic mice; LAP-tTA STM, liver activator protein promoter-tetracycline transactivator single transgenic mice

Article Snippet: The cells were permeabilized with 0.1% Triton-100; incubated with HCV core (Anogen/YES Biotech Laboratories Ltd, Mississauga, Canada) or RBP4 antibodies [Proteintech Group, Inc., IL, USA, 1:100 dilution (low antibody concentration to avoid over staining)]; washed, and then incubated with secondary antibody.

Techniques: Virus, Infection, Immunohistochemistry, Binding Assay, Transgenic Assay

Journal: Virulence

Article Title: Altering retinol binding protein 4 levels in hepatitis C: Inflammation and steatosis matter

doi: 10.1080/21505594.2020.1838742

Figure Lengend Snippet: Baseline characteristics of CHC patients

Article Snippet: The cells were permeabilized with 0.1% Triton-100; incubated with HCV core (Anogen/YES Biotech Laboratories Ltd, Mississauga, Canada) or RBP4 antibodies [Proteintech Group, Inc., IL, USA, 1:100 dilution (low antibody concentration to avoid over staining)]; washed, and then incubated with secondary antibody.

Techniques:

Journal: Virulence

Article Title: Altering retinol binding protein 4 levels in hepatitis C: Inflammation and steatosis matter

doi: 10.1080/21505594.2020.1838742

Figure Lengend Snippet: Associations of RBP4 levels in CHC patients at baseline

Article Snippet: The cells were permeabilized with 0.1% Triton-100; incubated with HCV core (Anogen/YES Biotech Laboratories Ltd, Mississauga, Canada) or RBP4 antibodies [Proteintech Group, Inc., IL, USA, 1:100 dilution (low antibody concentration to avoid over staining)]; washed, and then incubated with secondary antibody.

Techniques:

Journal: Virulence

Article Title: Altering retinol binding protein 4 levels in hepatitis C: Inflammation and steatosis matter

doi: 10.1080/21505594.2020.1838742

Figure Lengend Snippet: Associations of RBP4 levels in SVR patients at 24 weeks post-therapy

Article Snippet: The cells were permeabilized with 0.1% Triton-100; incubated with HCV core (Anogen/YES Biotech Laboratories Ltd, Mississauga, Canada) or RBP4 antibodies [Proteintech Group, Inc., IL, USA, 1:100 dilution (low antibody concentration to avoid over staining)]; washed, and then incubated with secondary antibody.

Techniques:

Journal: Virulence

Article Title: Altering retinol binding protein 4 levels in hepatitis C: Inflammation and steatosis matter

doi: 10.1080/21505594.2020.1838742

Figure Lengend Snippet: Comparisons between pre-therapy and 24-week post-therapy RBP4 levels and HOMA-IR of CHC patients

Article Snippet: The cells were permeabilized with 0.1% Triton-100; incubated with HCV core (Anogen/YES Biotech Laboratories Ltd, Mississauga, Canada) or RBP4 antibodies [Proteintech Group, Inc., IL, USA, 1:100 dilution (low antibody concentration to avoid over staining)]; washed, and then incubated with secondary antibody.

Techniques:

Journal: Virulence

Article Title: Altering retinol binding protein 4 levels in hepatitis C: Inflammation and steatosis matter

doi: 10.1080/21505594.2020.1838742

Figure Lengend Snippet: Hepatic expression of RBP4 of a representative 63-year-old male CHC patient (a) and a 63-year-old male control (b). RBP4 was stained in brown, and most RBP4-positive cells were hepatocytes. The areas of hepatic inflammatory infiltration and fibrosis exhibited negligible RBP4 expression

Article Snippet: The cells were permeabilized with 0.1% Triton-100; incubated with HCV core (Anogen/YES Biotech Laboratories Ltd, Mississauga, Canada) or RBP4 antibodies [Proteintech Group, Inc., IL, USA, 1:100 dilution (low antibody concentration to avoid over staining)]; washed, and then incubated with secondary antibody.

Techniques: Expressing, Control, Staining

Journal: Virulence

Article Title: Altering retinol binding protein 4 levels in hepatitis C: Inflammation and steatosis matter

doi: 10.1080/21505594.2020.1838742

Figure Lengend Snippet: Comparisons of serum variables between the 2-month-old male LAP-tTA-HCV core DTM and LAP-tTA STM

Article Snippet: The cells were permeabilized with 0.1% Triton-100; incubated with HCV core (Anogen/YES Biotech Laboratories Ltd, Mississauga, Canada) or RBP4 antibodies [Proteintech Group, Inc., IL, USA, 1:100 dilution (low antibody concentration to avoid over staining)]; washed, and then incubated with secondary antibody.

Techniques:

Journal: Virulence

Article Title: Altering retinol binding protein 4 levels in hepatitis C: Inflammation and steatosis matter

doi: 10.1080/21505594.2020.1838742

Figure Lengend Snippet: Hepatic expression of HCV core and RBP4, and hepatic lipid accumulation of mice . HCV core staining in the livers of LAP-tTA-HCV core DTM (a) and LAP-tTA STM (b), the HCV core protein was stained in brown. Oil red staining for the lipids in the livers of LAP-tTA-HCV core DTM (c) and LAP-tTA STM (d), the intrahepatic lipid was stained in red. RBP4 staining in the livers of LAP-tTA-HCV core DTM (e) and LAP-tTA STM (f), RBP4 was stained in brown. All figures were in 200× magnification

Article Snippet: The cells were permeabilized with 0.1% Triton-100; incubated with HCV core (Anogen/YES Biotech Laboratories Ltd, Mississauga, Canada) or RBP4 antibodies [Proteintech Group, Inc., IL, USA, 1:100 dilution (low antibody concentration to avoid over staining)]; washed, and then incubated with secondary antibody.

Techniques: Expressing, Staining

Journal: Diabetes

Article Title: Retinol-Binding Protein 4 in Twins

doi: 10.2337/db08-1019

Figure Lengend Snippet: Characteristics including age, anthropometry, and plasma RBP4 and retinol of subjects from population 1

Article Snippet: RBP4 , GLUT4 , and ADIPOQ (adiponectin) cDNA was quantified by TaqMan real-time PCR on an ABI Prism 7900 HT system (Applied Biosystems, Foster City, CA) using gene expression assays for RBP4 (Hs00198830_m1), GLUT4 (Hs00168966_m1), and ADIPOQ (Hs00605917_m1).

Techniques: Clinical Proteomics

Journal: Diabetes

Article Title: Retinol-Binding Protein 4 in Twins

doi: 10.2337/db08-1019

Figure Lengend Snippet: Characteristics including age, anthropometry, and plasma RBP4 and retinol of subjects from population 2

Article Snippet: RBP4 , GLUT4 , and ADIPOQ (adiponectin) cDNA was quantified by TaqMan real-time PCR on an ABI Prism 7900 HT system (Applied Biosystems, Foster City, CA) using gene expression assays for RBP4 (Hs00198830_m1), GLUT4 (Hs00168966_m1), and ADIPOQ (Hs00605917_m1).

Techniques: Clinical Proteomics, Fat

Journal: Diabetes

Article Title: Retinol-Binding Protein 4 in Twins

doi: 10.2337/db08-1019

Figure Lengend Snippet: Plasma RBP4 and glucose tolerance. Plasma RBP4 concentration (means ± SE) in subjects with normal glucose tolerance (NGT; n = 170), impaired glucose tolerance (IGT; n = 83), and type 2 diabetes (T2D; n = 42). P values are adjusted for twin pair and zygosity status. × P < 0.001 for normal glucose tolerance vs. type 2 diabetes.

Article Snippet: RBP4 , GLUT4 , and ADIPOQ (adiponectin) cDNA was quantified by TaqMan real-time PCR on an ABI Prism 7900 HT system (Applied Biosystems, Foster City, CA) using gene expression assays for RBP4 (Hs00198830_m1), GLUT4 (Hs00168966_m1), and ADIPOQ (Hs00605917_m1).

Techniques: Clinical Proteomics, Concentration Assay

Journal: Diabetes

Article Title: Retinol-Binding Protein 4 in Twins

doi: 10.2337/db08-1019

Figure Lengend Snippet: Plasma RBP4 and R d . Insulin-stimulated glucose disposal rate ( R d ) as a function of plasma RBP4 in 90 young (gray circles) twins ( r = −0.30, P = 0.004) and 77 elderly (black circles) twins ( r = −0.37, P = 0.001).

Article Snippet: RBP4 , GLUT4 , and ADIPOQ (adiponectin) cDNA was quantified by TaqMan real-time PCR on an ABI Prism 7900 HT system (Applied Biosystems, Foster City, CA) using gene expression assays for RBP4 (Hs00198830_m1), GLUT4 (Hs00168966_m1), and ADIPOQ (Hs00605917_m1).

Techniques: Clinical Proteomics

Journal: Diabetes

Article Title: Retinol-Binding Protein 4 in Twins

doi: 10.2337/db08-1019

Figure Lengend Snippet: Subcutaneous adipose tissue GLUT4 versus RBP4 expression. Paired GLUT4 and RBP4 mRNA expression values, normalized to PPIA (cyclophilin A) mRNA, in 141 twins. r = 0.61, P < 0.001.

Article Snippet: RBP4 , GLUT4 , and ADIPOQ (adiponectin) cDNA was quantified by TaqMan real-time PCR on an ABI Prism 7900 HT system (Applied Biosystems, Foster City, CA) using gene expression assays for RBP4 (Hs00198830_m1), GLUT4 (Hs00168966_m1), and ADIPOQ (Hs00605917_m1).

Techniques: Expressing

Journal: Diabetes

Article Title: Retinol-Binding Protein 4 in Twins

doi: 10.2337/db08-1019

Figure Lengend Snippet: Subcutaneous adipose tissue RBP4 expression and glucose tolerance. Means ± SE for RBP4 mRNA expression normalized to PPIA (cyclophilin A) mRNA expression is shown for subjects with normal glucose tolerance (NGT; n = 94), impaired glucose tolerance (IGT; n = 49), and type 2 diabetes (T2D; n = 28). P values are adjusted for twin pair and zygosity status. × P = 0.01 for normal glucose tolerance vs. impaired glucose tolerance; • P < 0.001 for normal glucose tolerance vs. type 2 diabetes.

Article Snippet: RBP4 , GLUT4 , and ADIPOQ (adiponectin) cDNA was quantified by TaqMan real-time PCR on an ABI Prism 7900 HT system (Applied Biosystems, Foster City, CA) using gene expression assays for RBP4 (Hs00198830_m1), GLUT4 (Hs00168966_m1), and ADIPOQ (Hs00605917_m1).

Techniques: Expressing

Journal: Diabetes

Article Title: Retinol-Binding Protein 4 in Twins

doi: 10.2337/db08-1019

Figure Lengend Snippet: Skeletal muscle adiponectin versus RBP4 expression. Paired log basal expression values for ADIPOQ (adiponectin) and RBP4 mRNA normalized to PPIA (cyclophilin A) mRNA expression in 96 twins ( r = 0.86, P < 0.001).

Article Snippet: RBP4 , GLUT4 , and ADIPOQ (adiponectin) cDNA was quantified by TaqMan real-time PCR on an ABI Prism 7900 HT system (Applied Biosystems, Foster City, CA) using gene expression assays for RBP4 (Hs00198830_m1), GLUT4 (Hs00168966_m1), and ADIPOQ (Hs00605917_m1).

Techniques: Expressing

Journal: Diabetes

Article Title: Retinol-Binding Protein 4 in Twins

doi: 10.2337/db08-1019

Figure Lengend Snippet: Insulin stimulation and muscle RBP4 expression. Means ± SE for basal and insulin-stimulated skeletal muscle RBP4 mRNA expression normalized to PPIA (cyclophilin A) mRNA expression in 79 twins. × P = 0.004.

Article Snippet: RBP4 , GLUT4 , and ADIPOQ (adiponectin) cDNA was quantified by TaqMan real-time PCR on an ABI Prism 7900 HT system (Applied Biosystems, Foster City, CA) using gene expression assays for RBP4 (Hs00198830_m1), GLUT4 (Hs00168966_m1), and ADIPOQ (Hs00605917_m1).

Techniques: Expressing