adenosine diphosphate adp Search Results


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  • 99
    Millipore adenosine 5 diphosphate adp
    Antiplatelet aggregation activity results of extracts from mango and its by-products (peel, seed husk and seed) at 1.0 mg/mL against adenosine 5’-diphosphate (ADP) agonist (4 μM) expressed as mean value of inhibition percentages ( n  = 6). Data was analyzed using ANOVA of one factor. Post hoc analyses were conducted using Tukey’s test. *** denotes significant differences compared to the negative control (absence of extract) at  p  = 0.001; ns denotes no statistical differences.
    Adenosine 5 Diphosphate Adp, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 114 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Chrono-log adenosine diphosphate adp
    Src and Fyn are involved in platelet activation induced by oxPC CD36 downstream of TRAF6 (A) Human platelets were pre-incubated with 2 μM TRAF6 blocking peptide (BP) or control peptide (CP) followed by stimulation with oxPC CD36 (KODA-PC, 20 μM) for 5 minutes. Phosphorylation of Src was determined by Western blot analysis using phosphospecific antibody. Quantified data (mean ± SD) of at least 3 independent experiments are shown in the right panel. (B, C) Platelets were isolated from WT, Src −/− , Lyn −/− mice and stimulated with oxPC CD36 (KODA-PC, 20 μM) or <t>ADP</t> (10 μM). Integrin <t>α</t> IIb β 3 activation was assessed by FACS analysis and presented as mean ± SD of at least 3 independent experiments. (D–F) Human platelets were isolated by gel filtration and stimulated with oxPC CD36 (KODA-PC, 20 μM) for 5 minutes, lysed and 200 μg of protein lysate was immunoprecipitated with (D, E) phospho-tyrosine (p-Tyr) antibody or (F) c-Src antibody then c-Src (D), Fyn (E), p-Tyr (F) were detected by immunoblotting using Src and Fyn or p-Tyr primary antibody and light chain specific secondary antibody. IgG light chain (IgG LC) and p-Tyr, c-Src are shown as control. c-Src and Fyn were detected by Western blot analysis (D, E). * p
    Adenosine Diphosphate Adp, supplied by Chrono-log, used in various techniques. Bioz Stars score: 93/100, based on 112 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Roche adenosine diphosphate adp
    Src and Fyn are involved in platelet activation induced by oxPC CD36 downstream of TRAF6 (A) Human platelets were pre-incubated with 2 μM TRAF6 blocking peptide (BP) or control peptide (CP) followed by stimulation with oxPC CD36 (KODA-PC, 20 μM) for 5 minutes. Phosphorylation of Src was determined by Western blot analysis using phosphospecific antibody. Quantified data (mean ± SD) of at least 3 independent experiments are shown in the right panel. (B, C) Platelets were isolated from WT, Src −/− , Lyn −/− mice and stimulated with oxPC CD36 (KODA-PC, 20 μM) or <t>ADP</t> (10 μM). Integrin <t>α</t> IIb β 3 activation was assessed by FACS analysis and presented as mean ± SD of at least 3 independent experiments. (D–F) Human platelets were isolated by gel filtration and stimulated with oxPC CD36 (KODA-PC, 20 μM) for 5 minutes, lysed and 200 μg of protein lysate was immunoprecipitated with (D, E) phospho-tyrosine (p-Tyr) antibody or (F) c-Src antibody then c-Src (D), Fyn (E), p-Tyr (F) were detected by immunoblotting using Src and Fyn or p-Tyr primary antibody and light chain specific secondary antibody. IgG light chain (IgG LC) and p-Tyr, c-Src are shown as control. c-Src and Fyn were detected by Western blot analysis (D, E). * p
    Adenosine Diphosphate Adp, supplied by Roche, used in various techniques. Bioz Stars score: 93/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Bio/Data adenosine diphosphate adp
    Src and Fyn are involved in platelet activation induced by oxPC CD36 downstream of TRAF6 (A) Human platelets were pre-incubated with 2 μM TRAF6 blocking peptide (BP) or control peptide (CP) followed by stimulation with oxPC CD36 (KODA-PC, 20 μM) for 5 minutes. Phosphorylation of Src was determined by Western blot analysis using phosphospecific antibody. Quantified data (mean ± SD) of at least 3 independent experiments are shown in the right panel. (B, C) Platelets were isolated from WT, Src −/− , Lyn −/− mice and stimulated with oxPC CD36 (KODA-PC, 20 μM) or <t>ADP</t> (10 μM). Integrin <t>α</t> IIb β 3 activation was assessed by FACS analysis and presented as mean ± SD of at least 3 independent experiments. (D–F) Human platelets were isolated by gel filtration and stimulated with oxPC CD36 (KODA-PC, 20 μM) for 5 minutes, lysed and 200 μg of protein lysate was immunoprecipitated with (D, E) phospho-tyrosine (p-Tyr) antibody or (F) c-Src antibody then c-Src (D), Fyn (E), p-Tyr (F) were detected by immunoblotting using Src and Fyn or p-Tyr primary antibody and light chain specific secondary antibody. IgG light chain (IgG LC) and p-Tyr, c-Src are shown as control. c-Src and Fyn were detected by Western blot analysis (D, E). * p
    Adenosine Diphosphate Adp, supplied by Bio/Data, used in various techniques. Bioz Stars score: 92/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Boehringer Mannheim adenosine diphosphate adp
    Src and Fyn are involved in platelet activation induced by oxPC CD36 downstream of TRAF6 (A) Human platelets were pre-incubated with 2 μM TRAF6 blocking peptide (BP) or control peptide (CP) followed by stimulation with oxPC CD36 (KODA-PC, 20 μM) for 5 minutes. Phosphorylation of Src was determined by Western blot analysis using phosphospecific antibody. Quantified data (mean ± SD) of at least 3 independent experiments are shown in the right panel. (B, C) Platelets were isolated from WT, Src −/− , Lyn −/− mice and stimulated with oxPC CD36 (KODA-PC, 20 μM) or <t>ADP</t> (10 μM). Integrin <t>α</t> IIb β 3 activation was assessed by FACS analysis and presented as mean ± SD of at least 3 independent experiments. (D–F) Human platelets were isolated by gel filtration and stimulated with oxPC CD36 (KODA-PC, 20 μM) for 5 minutes, lysed and 200 μg of protein lysate was immunoprecipitated with (D, E) phospho-tyrosine (p-Tyr) antibody or (F) c-Src antibody then c-Src (D), Fyn (E), p-Tyr (F) were detected by immunoblotting using Src and Fyn or p-Tyr primary antibody and light chain specific secondary antibody. IgG light chain (IgG LC) and p-Tyr, c-Src are shown as control. c-Src and Fyn were detected by Western blot analysis (D, E). * p
    Adenosine Diphosphate Adp, supplied by Boehringer Mannheim, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    ARKRAY adenosine diphosphate adp
    Src and Fyn are involved in platelet activation induced by oxPC CD36 downstream of TRAF6 (A) Human platelets were pre-incubated with 2 μM TRAF6 blocking peptide (BP) or control peptide (CP) followed by stimulation with oxPC CD36 (KODA-PC, 20 μM) for 5 minutes. Phosphorylation of Src was determined by Western blot analysis using phosphospecific antibody. Quantified data (mean ± SD) of at least 3 independent experiments are shown in the right panel. (B, C) Platelets were isolated from WT, Src −/− , Lyn −/− mice and stimulated with oxPC CD36 (KODA-PC, 20 μM) or <t>ADP</t> (10 μM). Integrin <t>α</t> IIb β 3 activation was assessed by FACS analysis and presented as mean ± SD of at least 3 independent experiments. (D–F) Human platelets were isolated by gel filtration and stimulated with oxPC CD36 (KODA-PC, 20 μM) for 5 minutes, lysed and 200 μg of protein lysate was immunoprecipitated with (D, E) phospho-tyrosine (p-Tyr) antibody or (F) c-Src antibody then c-Src (D), Fyn (E), p-Tyr (F) were detected by immunoblotting using Src and Fyn or p-Tyr primary antibody and light chain specific secondary antibody. IgG light chain (IgG LC) and p-Tyr, c-Src are shown as control. c-Src and Fyn were detected by Western blot analysis (D, E). * p
    Adenosine Diphosphate Adp, supplied by ARKRAY, used in various techniques. Bioz Stars score: 91/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Helena Laboratories adenosine diphosphate adp
    GPIbα and platelet function are unperturbed by 14-3-3ζ deficiency. ( a ) Hirudin-anticoagulated blood from 14-3-3ζ-wt and 14-3-3ζ-deficient (14-3-3ζ-null) mice was perfused through collagen-coated (250 μg ml −1 Type I) microslides at 1,800 s −1 for 5 min. (i) DIC images are taken from 1 representative of four independent experiments (scale bar, 20 μm). (ii) Thrombi surface coverage was quantified using ImageJ software (4–5 fields analysed per flow). The histogram depicts the mean±s.e.m. ( n= 5; analysed using two-way ANOVA with Bonferroni's post hoc testing). ( b ) VWF binding was measured as described under ‘Methods'. The graph represents one of three independent experiments. ( c ) Aggregation of washed mouse platelets in the presence of human VWF (10 μg ml −1 ) and botrocetin (10 μg ml −1 ), with stirring. The graph depicts aggregation traces from one representative of three independent experiments. ( d ) Comparative aggregation of washed 14-3-3ζ-wt and 14-3-3ζ-null platelets in response to <t>CRP</t> or <t>ADP</t> ((i) ADP 1 μM; (ii) CRP 20 ng ml −1 ). Results are taken from one representative experiment. A histogram depicting the mean±s.e.m. ( n= 3; analysed using a two-way ANOVA with Bonferroni's post hoc testing), is presented in Supplementary Fig. 2b . ( e , f ) Diluted whole blood samples from 14-3-3ζ-wt (black bars) or 14-3-3ζ-null (white bars) mice were incubated with PE-JON/A ( e ) or FITC-anti P-selectin antibody ( f ), as described under ‘Methods', to examine integrin α IIb β 3 and degranulation of platelet α-granules, respectively, and analysed by flow cytometry, following incubation with the indicated agonist/concentration for 15 min. Results depict the % of gated platelets positive for antibody binding and are expressed as the mean±s.e.m. (( e ) PAR4P: n= 10; CRP: n= 3; ADP: n= 4; ( f ) PAR4P: n= 10; CRP: n= 5), where NS P > 0.05. Note: no significant difference was observed in the geometric mean of fluorescence intensity for the same experiments. ( g – i ) Resting whole cell lysates were prepared from 14-3-3ζ-wt (wt) and 14-3-3ζ-null (null) washed platelets. ( g ) Expression levels of 14-3-3 isoforms were compared using SDS–PAGE and immunoblot analysis, as described under ‘Methods', with immunoblots probed with the indicated 14-3-3 isoform-selective or pan-14-3-3 antibodies. These studies confirm deletion of 14-3-3ζ protein in the 14-3-3ζ-null mice, with some upregulation of 14-3-3γ. ( h , i ) Association of 14-3-3 proteins with the GPIbα cytoplasmic tail in the absence of 14-3-3ζ—GPIbα was immunoprecipitated from 14-3-3ζ-wt and 14-3-3ζ-null platelet lysates as described under ‘Methods', and analysed via immunoblotting, using ( h ) anti-14-3-3ζ or ( i ) anti-pan-14-3-3. Immunoblots are taken from one representative of three independent experiments.
    Adenosine Diphosphate Adp, supplied by Helena Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Millipore mgadp
    A : Representative macroscopic current recordings of the <t>MgADP</t> stimulatory effects of 0.1 mmol/l MgADP in the presence of 0.1 mmol/l <t>MgATP.</t> B : Concentration response curves for the stimulatory effects of increasing MgADP concentrations in the presence of 0.1 mmol/l MgATP. Results show no significant differences in MgADP stimulation between the E23/S1369 and K23/A1369 haplotypes across a range of MgADP concentrations ( P > 0.05). n = 3–10 patches per group.
    Mgadp, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Amresco adenosine diphosphate na2
    A : Representative macroscopic current recordings of the <t>MgADP</t> stimulatory effects of 0.1 mmol/l MgADP in the presence of 0.1 mmol/l <t>MgATP.</t> B : Concentration response curves for the stimulatory effects of increasing MgADP concentrations in the presence of 0.1 mmol/l MgATP. Results show no significant differences in MgADP stimulation between the E23/S1369 and K23/A1369 haplotypes across a range of MgADP concentrations ( P > 0.05). n = 3–10 patches per group.
    Adenosine Diphosphate Na2, supplied by Amresco, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Beckman Coulter cyan adenosine diphosphate
    A : Representative macroscopic current recordings of the <t>MgADP</t> stimulatory effects of 0.1 mmol/l MgADP in the presence of 0.1 mmol/l <t>MgATP.</t> B : Concentration response curves for the stimulatory effects of increasing MgADP concentrations in the presence of 0.1 mmol/l MgATP. Results show no significant differences in MgADP stimulation between the E23/S1369 and K23/A1369 haplotypes across a range of MgADP concentrations ( P > 0.05). n = 3–10 patches per group.
    Cyan Adenosine Diphosphate, supplied by Beckman Coulter, used in various techniques. Bioz Stars score: 86/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Chrono-log adenosine diphospate adp
    A : Representative macroscopic current recordings of the <t>MgADP</t> stimulatory effects of 0.1 mmol/l MgADP in the presence of 0.1 mmol/l <t>MgATP.</t> B : Concentration response curves for the stimulatory effects of increasing MgADP concentrations in the presence of 0.1 mmol/l MgATP. Results show no significant differences in MgADP stimulation between the E23/S1369 and K23/A1369 haplotypes across a range of MgADP concentrations ( P > 0.05). n = 3–10 patches per group.
    Adenosine Diphospate Adp, supplied by Chrono-log, used in various techniques. Bioz Stars score: 84/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore adenosine diphosphate adp agarose
    A : Representative macroscopic current recordings of the <t>MgADP</t> stimulatory effects of 0.1 mmol/l MgADP in the presence of 0.1 mmol/l <t>MgATP.</t> B : Concentration response curves for the stimulatory effects of increasing MgADP concentrations in the presence of 0.1 mmol/l MgATP. Results show no significant differences in MgADP stimulation between the E23/S1369 and K23/A1369 haplotypes across a range of MgADP concentrations ( P > 0.05). n = 3–10 patches per group.
    Adenosine Diphosphate Adp Agarose, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Chrono-log adenosine 5 diphosphate adp
    The antiplatelet effect of natto in normal rat platelet-rich plasma against <t>ADP</t> and collagen induced platelet aggregation. The inhibitory effects of natto water extract on adenosine 5′-diphosphate (ADP) and collagen induced normal rat platelet aggregation. (a) ADP induced aggregation, (b) collagen induced aggregation.
    Adenosine 5 Diphosphate Adp, supplied by Chrono-log, used in various techniques. Bioz Stars score: 92/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore adenosine 5 diphosphate adp disodium salt
    The antiplatelet effect of natto in normal rat platelet-rich plasma against <t>ADP</t> and collagen induced platelet aggregation. The inhibitory effects of natto water extract on adenosine 5′-diphosphate (ADP) and collagen induced normal rat platelet aggregation. (a) ADP induced aggregation, (b) collagen induced aggregation.
    Adenosine 5 Diphosphate Adp Disodium Salt, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore adenosine 5
    Bar graphs illustrate the effects of <t>α,β-methylene-adenosine-5′-diphosphate</t> (AMPCP; 100 μmol/l; CD73 inhibitor) on adenosine levels in the medium of rat PTCs, TALCs, and CDCs incubated with 10 μmol/l of either 5′-AMP
    Adenosine 5, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 644 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Bio/Data adenosine 5 diphosphate adp
    Bar graphs illustrate the effects of <t>α,β-methylene-adenosine-5′-diphosphate</t> (AMPCP; 100 μmol/l; CD73 inhibitor) on adenosine levels in the medium of rat PTCs, TALCs, and CDCs incubated with 10 μmol/l of either 5′-AMP
    Adenosine 5 Diphosphate Adp, supplied by Bio/Data, used in various techniques. Bioz Stars score: 88/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Siemens AG adenosine diphosphate adp
    Bar graphs illustrate the effects of <t>α,β-methylene-adenosine-5′-diphosphate</t> (AMPCP; 100 μmol/l; CD73 inhibitor) on adenosine levels in the medium of rat PTCs, TALCs, and CDCs incubated with 10 μmol/l of either 5′-AMP
    Adenosine Diphosphate Adp, supplied by Siemens AG, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Enzo Biochem adenosine diphosphate adp
    Bar graphs illustrate the effects of <t>α,β-methylene-adenosine-5′-diphosphate</t> (AMPCP; 100 μmol/l; CD73 inhibitor) on adenosine levels in the medium of rat PTCs, TALCs, and CDCs incubated with 10 μmol/l of either 5′-AMP
    Adenosine Diphosphate Adp, supplied by Enzo Biochem, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore caution adenosine diphosphate
    Bar graphs illustrate the effects of <t>α,β-methylene-adenosine-5′-diphosphate</t> (AMPCP; 100 μmol/l; CD73 inhibitor) on adenosine levels in the medium of rat PTCs, TALCs, and CDCs incubated with 10 μmol/l of either 5′-AMP
    Caution Adenosine Diphosphate, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies adenosine diphosphate adp
    Bar graphs illustrate the effects of <t>α,β-methylene-adenosine-5′-diphosphate</t> (AMPCP; 100 μmol/l; CD73 inhibitor) on adenosine levels in the medium of rat PTCs, TALCs, and CDCs incubated with 10 μmol/l of either 5′-AMP
    Adenosine Diphosphate Adp, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Becton Dickinson adenosine diphosphate adp
    Bar graphs illustrate the effects of <t>α,β-methylene-adenosine-5′-diphosphate</t> (AMPCP; 100 μmol/l; CD73 inhibitor) on adenosine levels in the medium of rat PTCs, TALCs, and CDCs incubated with 10 μmol/l of either 5′-AMP
    Adenosine Diphosphate Adp, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 95/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam adenosine diphosphate adp
    Mitofilin is indispensable for mitochondrial homeostasis and osteogenesis of BMMSCs. (A-D) Representative transmission electron microscopy images (A) and quantitative analysis of the ratio of mitochondrial inner membrane versus outer membrane (B) as well as mitochondrial average area (C) and number (D) per cell in BMMSCs. Bars: 125 nm (high magnification). (E, F) Rhodamine 123 detection of mitochondrial membrane potential of BMMSCs (E) with quantitative analysis of fluorescence intensity (F) . Bars: 10 μm. (G, H) DCFDA detection of total ROS level in BMMSCs (G) with flow cytometric quantitative analysis of fluorescence intensity (H) . Bars: 10 μm. (I) Quantitative analysis of <t>ATP</t> production versus <t>ADP</t> ratio in BMMSCs. (J) qRT-PCR analysis of mRNA expression levels of all 13 mtDNA-encoded mitochondrial complex subunits in BMMSCs. (K-M) Representative images of ALP and alizarin red staining (K) with quantification of ALP activity (L) and mineralization (M) in osteogenic differentiation of BMMSCs. Bars: 5 mm. (N) qRT-PCR analysis of mRNA expression levels of osteogenic marker genes in osteogenic differentiation of BMMSCs. BMMSCs from 4-month-old SAMR1 mice were transfected with either the shRNA for Immt (Mitofilin) or the negative control (a scrambled sequence, NC) by a lentiviral vector. n = 3 per group. Data represent mean ± SD. * P
    Adenosine Diphosphate Adp, supplied by Abcam, used in various techniques. Bioz Stars score: 94/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    GE Healthcare adenosine diphosphate adp
    Processive strand incision requires the closed form of MutL. ( A ) Size exclusion chromatography of open and closed forms of MutL. Left panel: wild type MutL was observed in the open state without nucleotide (black), with <t>ADP</t> (green) and <t>ATP</t> (red), but closed with AMP.PNP (blue). MutL N302A was always observed in the closed state in the presence of nucleotide (middle panel) and MutL K307A was always observed in the open in the presence of nucleotides (right panel). ( B ) Incision of 0.5 nM GT#2 by 100 nM MutS, 100 nM MutL, 50 nM MutH with wild type (first panel), N302A (second panel) and K307A MutL variants (third panel with 50 nM MutH, fourth panel with 250 nM MutH). ( C ) Quantification (mean ± SD, n = 3) and fitting of strand incision by wild type, N302A and K307A MutL (with 50 and 250 nM MutH). Rate constants obtained from the fits are tabulated in Supplementary Table S1.
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    Valiant adenosine diphosphate adp
    Processive strand incision requires the closed form of MutL. ( A ) Size exclusion chromatography of open and closed forms of MutL. Left panel: wild type MutL was observed in the open state without nucleotide (black), with <t>ADP</t> (green) and <t>ATP</t> (red), but closed with AMP.PNP (blue). MutL N302A was always observed in the closed state in the presence of nucleotide (middle panel) and MutL K307A was always observed in the open in the presence of nucleotides (right panel). ( B ) Incision of 0.5 nM GT#2 by 100 nM MutS, 100 nM MutL, 50 nM MutH with wild type (first panel), N302A (second panel) and K307A MutL variants (third panel with 50 nM MutH, fourth panel with 250 nM MutH). ( C ) Quantification (mean ± SD, n = 3) and fitting of strand incision by wild type, N302A and K307A MutL (with 50 and 250 nM MutH). Rate constants obtained from the fits are tabulated in Supplementary Table S1.
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    Beckman Coulter adenosine diphosphate adp
    Myocardial measurements at baseline (BL) and during ventricular fibrillation (VF), at 10 and 16 minutes while on low-flow extracorporeal circulation simulating the hemodynamic conditions of closed-chest CPR. pCr, phosphocreatine; ATP, adenosine triphosphate; <t>ADP,</t> adenosine diphosphate; AMP, adenosine <t>monophosphate;</t> Ado, adenosine. Data was analyzed by one-way repeated measures ANOVA and differences shown after Holm-Sidak method for multiple pairwise comparisons. a vs BL, b vs VF10; * p ≤ 0.05, † p ≤ 0.001.
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    Millipore adenosine 5 diphosphate sodium salt adp
    Myocardial measurements at baseline (BL) and during ventricular fibrillation (VF), at 10 and 16 minutes while on low-flow extracorporeal circulation simulating the hemodynamic conditions of closed-chest CPR. pCr, phosphocreatine; ATP, adenosine triphosphate; <t>ADP,</t> adenosine diphosphate; AMP, adenosine <t>monophosphate;</t> Ado, adenosine. Data was analyzed by one-way repeated measures ANOVA and differences shown after Holm-Sidak method for multiple pairwise comparisons. a vs BL, b vs VF10; * p ≤ 0.05, † p ≤ 0.001.
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    Millipore adenosine 5 diphosphoribose
    Complex of the apoenzyme with adenosine <t>5′-diphosphoribose</t> (ADPR). The stereoview is derived from PDB entry 5VKR. The 2| F o | – | F c | map is contoured at ∼0.25 e – /Å 3 .
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    Millipore α β methylene adp
    Characterization of DsRed-NT5E fusion proteins. A. COS-7 cells were transiently transfected with an expression vector for DsRed fused to wild type form of human NT5E (DsRed-hNT5E WT) and fusion proteins were localized by immunofluorescence with antibodies against fluorescent DsRed (green) and native hNT5E (red) proteins, and by internal fluorescence (purple). The merged picture shows obvious overlap of all 3 signals indicating that DsRed-hNT5E fusion protein is intact and contains both antigens. Magnification 400X . B. Immunoblot analysis of total protein extracts from mock-transfected (mock) or transfected COS-7 cells with expression vectors for DsRed monomer and DsRed-hNT5E (DsRed NT5E) fusion protein using DsRed (left) and hNT5E (right) antibodies. Both antibodies detect a protein with a molecular weight of approximately 90 kiloDaltons (black arrowheads, left and right) while DsRed antibody only detects the DsRed monomer (white arrowhead, left) indicating that DsRed-hNT5E fusion is intact and contains both antigens. Total β-actin protein was used as loading control. C. Enzyme histochemistry of mock-transfected or transfected COS-7 cells with expression vectors for DsRed-hNT5E wild type (WT) and mutant (F1–3) proteins using adenosine monophosphate (AMP) as substrate. Only COS–7 cells transfected with the expression vector for DsRed-hNT5E wild type fusion protein displayed AMPase activity, which could be blocked in presence of known NT5E inhibitor <t>α/β-methylene-ADP.</t> Mock-transfected or COS-7 cells transfected with expression vectors for DsRed-hNT5E mutant (F1–3) proteins lack AMPase activity. Magnification 200X .
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    Trinity Biotech adenosine diphosphate
    Characterization of DsRed-NT5E fusion proteins. A. COS-7 cells were transiently transfected with an expression vector for DsRed fused to wild type form of human NT5E (DsRed-hNT5E WT) and fusion proteins were localized by immunofluorescence with antibodies against fluorescent DsRed (green) and native hNT5E (red) proteins, and by internal fluorescence (purple). The merged picture shows obvious overlap of all 3 signals indicating that DsRed-hNT5E fusion protein is intact and contains both antigens. Magnification 400X . B. Immunoblot analysis of total protein extracts from mock-transfected (mock) or transfected COS-7 cells with expression vectors for DsRed monomer and DsRed-hNT5E (DsRed NT5E) fusion protein using DsRed (left) and hNT5E (right) antibodies. Both antibodies detect a protein with a molecular weight of approximately 90 kiloDaltons (black arrowheads, left and right) while DsRed antibody only detects the DsRed monomer (white arrowhead, left) indicating that DsRed-hNT5E fusion is intact and contains both antigens. Total β-actin protein was used as loading control. C. Enzyme histochemistry of mock-transfected or transfected COS-7 cells with expression vectors for DsRed-hNT5E wild type (WT) and mutant (F1–3) proteins using adenosine monophosphate (AMP) as substrate. Only COS–7 cells transfected with the expression vector for DsRed-hNT5E wild type fusion protein displayed AMPase activity, which could be blocked in presence of known NT5E inhibitor <t>α/β-methylene-ADP.</t> Mock-transfected or COS-7 cells transfected with expression vectors for DsRed-hNT5E mutant (F1–3) proteins lack AMPase activity. Magnification 200X .
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    RPI Inc adenosine diphosphate
    Characterization of DsRed-NT5E fusion proteins. A. COS-7 cells were transiently transfected with an expression vector for DsRed fused to wild type form of human NT5E (DsRed-hNT5E WT) and fusion proteins were localized by immunofluorescence with antibodies against fluorescent DsRed (green) and native hNT5E (red) proteins, and by internal fluorescence (purple). The merged picture shows obvious overlap of all 3 signals indicating that DsRed-hNT5E fusion protein is intact and contains both antigens. Magnification 400X . B. Immunoblot analysis of total protein extracts from mock-transfected (mock) or transfected COS-7 cells with expression vectors for DsRed monomer and DsRed-hNT5E (DsRed NT5E) fusion protein using DsRed (left) and hNT5E (right) antibodies. Both antibodies detect a protein with a molecular weight of approximately 90 kiloDaltons (black arrowheads, left and right) while DsRed antibody only detects the DsRed monomer (white arrowhead, left) indicating that DsRed-hNT5E fusion is intact and contains both antigens. Total β-actin protein was used as loading control. C. Enzyme histochemistry of mock-transfected or transfected COS-7 cells with expression vectors for DsRed-hNT5E wild type (WT) and mutant (F1–3) proteins using adenosine monophosphate (AMP) as substrate. Only COS–7 cells transfected with the expression vector for DsRed-hNT5E wild type fusion protein displayed AMPase activity, which could be blocked in presence of known NT5E inhibitor <t>α/β-methylene-ADP.</t> Mock-transfected or COS-7 cells transfected with expression vectors for DsRed-hNT5E mutant (F1–3) proteins lack AMPase activity. Magnification 200X .
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    Merck KGaA adenosine diphosphate
    Characterization of DsRed-NT5E fusion proteins. A. COS-7 cells were transiently transfected with an expression vector for DsRed fused to wild type form of human NT5E (DsRed-hNT5E WT) and fusion proteins were localized by immunofluorescence with antibodies against fluorescent DsRed (green) and native hNT5E (red) proteins, and by internal fluorescence (purple). The merged picture shows obvious overlap of all 3 signals indicating that DsRed-hNT5E fusion protein is intact and contains both antigens. Magnification 400X . B. Immunoblot analysis of total protein extracts from mock-transfected (mock) or transfected COS-7 cells with expression vectors for DsRed monomer and DsRed-hNT5E (DsRed NT5E) fusion protein using DsRed (left) and hNT5E (right) antibodies. Both antibodies detect a protein with a molecular weight of approximately 90 kiloDaltons (black arrowheads, left and right) while DsRed antibody only detects the DsRed monomer (white arrowhead, left) indicating that DsRed-hNT5E fusion is intact and contains both antigens. Total β-actin protein was used as loading control. C. Enzyme histochemistry of mock-transfected or transfected COS-7 cells with expression vectors for DsRed-hNT5E wild type (WT) and mutant (F1–3) proteins using adenosine monophosphate (AMP) as substrate. Only COS–7 cells transfected with the expression vector for DsRed-hNT5E wild type fusion protein displayed AMPase activity, which could be blocked in presence of known NT5E inhibitor <t>α/β-methylene-ADP.</t> Mock-transfected or COS-7 cells transfected with expression vectors for DsRed-hNT5E mutant (F1–3) proteins lack AMPase activity. Magnification 200X .
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    Image Search Results


    Antiplatelet aggregation activity results of extracts from mango and its by-products (peel, seed husk and seed) at 1.0 mg/mL against adenosine 5’-diphosphate (ADP) agonist (4 μM) expressed as mean value of inhibition percentages ( n  = 6). Data was analyzed using ANOVA of one factor. Post hoc analyses were conducted using Tukey’s test. *** denotes significant differences compared to the negative control (absence of extract) at  p  = 0.001; ns denotes no statistical differences.

    Journal: Antioxidants

    Article Title: Antiplatelet Activity of Natural Bioactive Extracts from Mango (Mangifera Indica L.) and its By-Products

    doi: 10.3390/antiox8110517

    Figure Lengend Snippet: Antiplatelet aggregation activity results of extracts from mango and its by-products (peel, seed husk and seed) at 1.0 mg/mL against adenosine 5’-diphosphate (ADP) agonist (4 μM) expressed as mean value of inhibition percentages ( n = 6). Data was analyzed using ANOVA of one factor. Post hoc analyses were conducted using Tukey’s test. *** denotes significant differences compared to the negative control (absence of extract) at p = 0.001; ns denotes no statistical differences.

    Article Snippet: For all assays, platelet aggregation was induced by adding adenosine 5’-diphosphate (ADP, 4 μM) supplied by Sigma-Aldrich (St. Louis, Missouri, MO, USA) as an agonist.

    Techniques: Activity Assay, Inhibition, Negative Control

    Correlation of ADP-induced aggregation in platelet rich plasma pre-treated with PGE1 or with P2Y1 inhibitor. Platelet rich plasma was pre-treated with 0.31 µM PGE1 or 1 mM adenosine 3’, 5’-diphosphate (A3P5P), a P2Y1 receptor inhibitor, for 3 min at 37 °C. Broken lines represent 95% confidence interval, r=0.89, p=0.001.

    Journal: PLoS ONE

    Article Title: Comparison of a New P2Y12 Receptor Specific Platelet Aggregation Test with Other Laboratory Methods in Stroke Patients on Clopidogrel Monotherapy

    doi: 10.1371/journal.pone.0069417

    Figure Lengend Snippet: Correlation of ADP-induced aggregation in platelet rich plasma pre-treated with PGE1 or with P2Y1 inhibitor. Platelet rich plasma was pre-treated with 0.31 µM PGE1 or 1 mM adenosine 3’, 5’-diphosphate (A3P5P), a P2Y1 receptor inhibitor, for 3 min at 37 °C. Broken lines represent 95% confidence interval, r=0.89, p=0.001.

    Article Snippet: The extent of P2Y1 receptor suppression by PGE1 was compared to the effect of P2Y1 antagonist adenosine 3’, 5’-diphosphate (A3P5P; Sigma-Aldrich) [ ].

    Techniques:

    Src and Fyn are involved in platelet activation induced by oxPC CD36 downstream of TRAF6 (A) Human platelets were pre-incubated with 2 μM TRAF6 blocking peptide (BP) or control peptide (CP) followed by stimulation with oxPC CD36 (KODA-PC, 20 μM) for 5 minutes. Phosphorylation of Src was determined by Western blot analysis using phosphospecific antibody. Quantified data (mean ± SD) of at least 3 independent experiments are shown in the right panel. (B, C) Platelets were isolated from WT, Src −/− , Lyn −/− mice and stimulated with oxPC CD36 (KODA-PC, 20 μM) or ADP (10 μM). Integrin α IIb β 3 activation was assessed by FACS analysis and presented as mean ± SD of at least 3 independent experiments. (D–F) Human platelets were isolated by gel filtration and stimulated with oxPC CD36 (KODA-PC, 20 μM) for 5 minutes, lysed and 200 μg of protein lysate was immunoprecipitated with (D, E) phospho-tyrosine (p-Tyr) antibody or (F) c-Src antibody then c-Src (D), Fyn (E), p-Tyr (F) were detected by immunoblotting using Src and Fyn or p-Tyr primary antibody and light chain specific secondary antibody. IgG light chain (IgG LC) and p-Tyr, c-Src are shown as control. c-Src and Fyn were detected by Western blot analysis (D, E). * p

    Journal: Circulation research

    Article Title: TLR2 Plays a Key Role in Platelet Hyperreactivity and Accelerated Thrombosis Associated with Hyperlipidemia

    doi: 10.1161/CIRCRESAHA.117.311069

    Figure Lengend Snippet: Src and Fyn are involved in platelet activation induced by oxPC CD36 downstream of TRAF6 (A) Human platelets were pre-incubated with 2 μM TRAF6 blocking peptide (BP) or control peptide (CP) followed by stimulation with oxPC CD36 (KODA-PC, 20 μM) for 5 minutes. Phosphorylation of Src was determined by Western blot analysis using phosphospecific antibody. Quantified data (mean ± SD) of at least 3 independent experiments are shown in the right panel. (B, C) Platelets were isolated from WT, Src −/− , Lyn −/− mice and stimulated with oxPC CD36 (KODA-PC, 20 μM) or ADP (10 μM). Integrin α IIb β 3 activation was assessed by FACS analysis and presented as mean ± SD of at least 3 independent experiments. (D–F) Human platelets were isolated by gel filtration and stimulated with oxPC CD36 (KODA-PC, 20 μM) for 5 minutes, lysed and 200 μg of protein lysate was immunoprecipitated with (D, E) phospho-tyrosine (p-Tyr) antibody or (F) c-Src antibody then c-Src (D), Fyn (E), p-Tyr (F) were detected by immunoblotting using Src and Fyn or p-Tyr primary antibody and light chain specific secondary antibody. IgG light chain (IgG LC) and p-Tyr, c-Src are shown as control. c-Src and Fyn were detected by Western blot analysis (D, E). * p

    Article Snippet: Human α-thrombin was purchased from Enzyme Research Laboratories (South Bend, IN) and adenosine diphosphate (ADP) from Chrono-log (Havertown, PA).

    Techniques: Activation Assay, Incubation, Blocking Assay, Western Blot, Isolation, Mouse Assay, FACS, Filtration, Immunoprecipitation

    TLR2 and TLR6 play a critical role in platelet hyperreactivity and accelerated thrombosis induced by hyperlipidemia (A) Platelet rich plasma (PRP) was isolated from ApoE −/− , ApoE −/− /TLR2 −/− , ApoE −/− /CD36 −/− , and ApoE −/− /CD36 −/− /TLR2 −/− mice fed either a chow diet or a Western diet. Integrin α IIb β 3 activation after stimulation with suboptimal concentration of (3 μM) ADP was determined by FACS analysis. Data presented as mean ± SD of at least 3 independent experiments. (B) Human platelets were isolated by gel filtration from healthy control donors and pre-incubated for 30 min either with (4 μg/ml) TLR2 blocking antibody or isotype matched control IgG followed by 30 min incubation with citrated human plasma samples containing either low endogenous levels of oxPC CD36 (

    Journal: Circulation research

    Article Title: TLR2 Plays a Key Role in Platelet Hyperreactivity and Accelerated Thrombosis Associated with Hyperlipidemia

    doi: 10.1161/CIRCRESAHA.117.311069

    Figure Lengend Snippet: TLR2 and TLR6 play a critical role in platelet hyperreactivity and accelerated thrombosis induced by hyperlipidemia (A) Platelet rich plasma (PRP) was isolated from ApoE −/− , ApoE −/− /TLR2 −/− , ApoE −/− /CD36 −/− , and ApoE −/− /CD36 −/− /TLR2 −/− mice fed either a chow diet or a Western diet. Integrin α IIb β 3 activation after stimulation with suboptimal concentration of (3 μM) ADP was determined by FACS analysis. Data presented as mean ± SD of at least 3 independent experiments. (B) Human platelets were isolated by gel filtration from healthy control donors and pre-incubated for 30 min either with (4 μg/ml) TLR2 blocking antibody or isotype matched control IgG followed by 30 min incubation with citrated human plasma samples containing either low endogenous levels of oxPC CD36 (

    Article Snippet: Human α-thrombin was purchased from Enzyme Research Laboratories (South Bend, IN) and adenosine diphosphate (ADP) from Chrono-log (Havertown, PA).

    Techniques: Isolation, Mouse Assay, Western Blot, Activation Assay, Concentration Assay, FACS, Filtration, Incubation, Blocking Assay

    TLR2 and TLR6 play a role in platelet activation induced by oxPC CD36 (A, F) Murine platelets of indicated genotypes (WT, MyD88 −/− , TLR2 −/− , and TLR6 −/− ) were isolated by gel filtration and incubated with representative member of oxPC CD36 (KODA-PC, 20 μM), ADP (10 μM), or thrombin (0.05 U/ml), and integrin α IIb β 3 activation was determined by FACS analysis using PE-conjugated integrin α IIb β 3 (JON/A) antibody. (A) Left panels present FACS analysis data as histograms, (A) right panel and (F) present data as mean ± SD of 3 independent experiments. (B–E, G–H) Human platelets were isolated by gel filtration and pre-incubated with either (B, C) 2 μM MyD88 blocking peptide (BP), or control peptide (CP) or (D, E) 4 μg/ml TLR2 neutralizing antibody, or (G, H) 4 μg/ml TLR6 neutralizing antibody or non-immune isotype matched control IgG followed by stimulation with oxPC CD36 (KODA-PC, 20 μM). P-selectin expression was assessed by FACS analysis. FACS analysis data are presented as histograms and as mean ± SD of 3 independent experiments. * p

    Journal: Circulation research

    Article Title: TLR2 Plays a Key Role in Platelet Hyperreactivity and Accelerated Thrombosis Associated with Hyperlipidemia

    doi: 10.1161/CIRCRESAHA.117.311069

    Figure Lengend Snippet: TLR2 and TLR6 play a role in platelet activation induced by oxPC CD36 (A, F) Murine platelets of indicated genotypes (WT, MyD88 −/− , TLR2 −/− , and TLR6 −/− ) were isolated by gel filtration and incubated with representative member of oxPC CD36 (KODA-PC, 20 μM), ADP (10 μM), or thrombin (0.05 U/ml), and integrin α IIb β 3 activation was determined by FACS analysis using PE-conjugated integrin α IIb β 3 (JON/A) antibody. (A) Left panels present FACS analysis data as histograms, (A) right panel and (F) present data as mean ± SD of 3 independent experiments. (B–E, G–H) Human platelets were isolated by gel filtration and pre-incubated with either (B, C) 2 μM MyD88 blocking peptide (BP), or control peptide (CP) or (D, E) 4 μg/ml TLR2 neutralizing antibody, or (G, H) 4 μg/ml TLR6 neutralizing antibody or non-immune isotype matched control IgG followed by stimulation with oxPC CD36 (KODA-PC, 20 μM). P-selectin expression was assessed by FACS analysis. FACS analysis data are presented as histograms and as mean ± SD of 3 independent experiments. * p

    Article Snippet: Human α-thrombin was purchased from Enzyme Research Laboratories (South Bend, IN) and adenosine diphosphate (ADP) from Chrono-log (Havertown, PA).

    Techniques: Activation Assay, Isolation, Filtration, Incubation, FACS, Blocking Assay, Expressing

    GPIbα and platelet function are unperturbed by 14-3-3ζ deficiency. ( a ) Hirudin-anticoagulated blood from 14-3-3ζ-wt and 14-3-3ζ-deficient (14-3-3ζ-null) mice was perfused through collagen-coated (250 μg ml −1 Type I) microslides at 1,800 s −1 for 5 min. (i) DIC images are taken from 1 representative of four independent experiments (scale bar, 20 μm). (ii) Thrombi surface coverage was quantified using ImageJ software (4–5 fields analysed per flow). The histogram depicts the mean±s.e.m. ( n= 5; analysed using two-way ANOVA with Bonferroni's post hoc testing). ( b ) VWF binding was measured as described under ‘Methods'. The graph represents one of three independent experiments. ( c ) Aggregation of washed mouse platelets in the presence of human VWF (10 μg ml −1 ) and botrocetin (10 μg ml −1 ), with stirring. The graph depicts aggregation traces from one representative of three independent experiments. ( d ) Comparative aggregation of washed 14-3-3ζ-wt and 14-3-3ζ-null platelets in response to CRP or ADP ((i) ADP 1 μM; (ii) CRP 20 ng ml −1 ). Results are taken from one representative experiment. A histogram depicting the mean±s.e.m. ( n= 3; analysed using a two-way ANOVA with Bonferroni's post hoc testing), is presented in Supplementary Fig. 2b . ( e , f ) Diluted whole blood samples from 14-3-3ζ-wt (black bars) or 14-3-3ζ-null (white bars) mice were incubated with PE-JON/A ( e ) or FITC-anti P-selectin antibody ( f ), as described under ‘Methods', to examine integrin α IIb β 3 and degranulation of platelet α-granules, respectively, and analysed by flow cytometry, following incubation with the indicated agonist/concentration for 15 min. Results depict the % of gated platelets positive for antibody binding and are expressed as the mean±s.e.m. (( e ) PAR4P: n= 10; CRP: n= 3; ADP: n= 4; ( f ) PAR4P: n= 10; CRP: n= 5), where NS P > 0.05. Note: no significant difference was observed in the geometric mean of fluorescence intensity for the same experiments. ( g – i ) Resting whole cell lysates were prepared from 14-3-3ζ-wt (wt) and 14-3-3ζ-null (null) washed platelets. ( g ) Expression levels of 14-3-3 isoforms were compared using SDS–PAGE and immunoblot analysis, as described under ‘Methods', with immunoblots probed with the indicated 14-3-3 isoform-selective or pan-14-3-3 antibodies. These studies confirm deletion of 14-3-3ζ protein in the 14-3-3ζ-null mice, with some upregulation of 14-3-3γ. ( h , i ) Association of 14-3-3 proteins with the GPIbα cytoplasmic tail in the absence of 14-3-3ζ—GPIbα was immunoprecipitated from 14-3-3ζ-wt and 14-3-3ζ-null platelet lysates as described under ‘Methods', and analysed via immunoblotting, using ( h ) anti-14-3-3ζ or ( i ) anti-pan-14-3-3. Immunoblots are taken from one representative of three independent experiments.

    Journal: Nature Communications

    Article Title: 14-3-3ζ regulates the mitochondrial respiratory reserve linked to platelet phosphatidylserine exposure and procoagulant function

    doi: 10.1038/ncomms12862

    Figure Lengend Snippet: GPIbα and platelet function are unperturbed by 14-3-3ζ deficiency. ( a ) Hirudin-anticoagulated blood from 14-3-3ζ-wt and 14-3-3ζ-deficient (14-3-3ζ-null) mice was perfused through collagen-coated (250 μg ml −1 Type I) microslides at 1,800 s −1 for 5 min. (i) DIC images are taken from 1 representative of four independent experiments (scale bar, 20 μm). (ii) Thrombi surface coverage was quantified using ImageJ software (4–5 fields analysed per flow). The histogram depicts the mean±s.e.m. ( n= 5; analysed using two-way ANOVA with Bonferroni's post hoc testing). ( b ) VWF binding was measured as described under ‘Methods'. The graph represents one of three independent experiments. ( c ) Aggregation of washed mouse platelets in the presence of human VWF (10 μg ml −1 ) and botrocetin (10 μg ml −1 ), with stirring. The graph depicts aggregation traces from one representative of three independent experiments. ( d ) Comparative aggregation of washed 14-3-3ζ-wt and 14-3-3ζ-null platelets in response to CRP or ADP ((i) ADP 1 μM; (ii) CRP 20 ng ml −1 ). Results are taken from one representative experiment. A histogram depicting the mean±s.e.m. ( n= 3; analysed using a two-way ANOVA with Bonferroni's post hoc testing), is presented in Supplementary Fig. 2b . ( e , f ) Diluted whole blood samples from 14-3-3ζ-wt (black bars) or 14-3-3ζ-null (white bars) mice were incubated with PE-JON/A ( e ) or FITC-anti P-selectin antibody ( f ), as described under ‘Methods', to examine integrin α IIb β 3 and degranulation of platelet α-granules, respectively, and analysed by flow cytometry, following incubation with the indicated agonist/concentration for 15 min. Results depict the % of gated platelets positive for antibody binding and are expressed as the mean±s.e.m. (( e ) PAR4P: n= 10; CRP: n= 3; ADP: n= 4; ( f ) PAR4P: n= 10; CRP: n= 5), where NS P > 0.05. Note: no significant difference was observed in the geometric mean of fluorescence intensity for the same experiments. ( g – i ) Resting whole cell lysates were prepared from 14-3-3ζ-wt (wt) and 14-3-3ζ-null (null) washed platelets. ( g ) Expression levels of 14-3-3 isoforms were compared using SDS–PAGE and immunoblot analysis, as described under ‘Methods', with immunoblots probed with the indicated 14-3-3 isoform-selective or pan-14-3-3 antibodies. These studies confirm deletion of 14-3-3ζ protein in the 14-3-3ζ-null mice, with some upregulation of 14-3-3γ. ( h , i ) Association of 14-3-3 proteins with the GPIbα cytoplasmic tail in the absence of 14-3-3ζ—GPIbα was immunoprecipitated from 14-3-3ζ-wt and 14-3-3ζ-null platelet lysates as described under ‘Methods', and analysed via immunoblotting, using ( h ) anti-14-3-3ζ or ( i ) anti-pan-14-3-3. Immunoblots are taken from one representative of three independent experiments.

    Article Snippet: All aggregation studies were initiated by addition of the indicated concentrations of adenosine diphosphate (ADP) or CRP to platelet suspensions stirred at 600 r.p.m. for 10 min at 37 °C in a four-channel automated platelet analyser (AggRAM, Helena Laboratories, Tyne and Wear, UK) in the presence of 1 mM calcium and 0.5 mg ml−1 fibrinogen.

    Techniques: Mouse Assay, Software, Flow Cytometry, Binding Assay, Incubation, Cytometry, Concentration Assay, Fluorescence, Expressing, SDS Page, Western Blot, Immunoprecipitation

    A : Representative macroscopic current recordings of the MgADP stimulatory effects of 0.1 mmol/l MgADP in the presence of 0.1 mmol/l MgATP. B : Concentration response curves for the stimulatory effects of increasing MgADP concentrations in the presence of 0.1 mmol/l MgATP. Results show no significant differences in MgADP stimulation between the E23/S1369 and K23/A1369 haplotypes across a range of MgADP concentrations ( P > 0.05). n = 3–10 patches per group.

    Journal: Diabetes

    Article Title: Coexpression of the Type 2 Diabetes Susceptibility Gene Variants KCNJ11 E23K and ABCC8 S1369A Alter the ATP and Sulfonylurea Sensitivities of the ATP-Sensitive K+ Channel

    doi: 10.2337/db09-0143

    Figure Lengend Snippet: A : Representative macroscopic current recordings of the MgADP stimulatory effects of 0.1 mmol/l MgADP in the presence of 0.1 mmol/l MgATP. B : Concentration response curves for the stimulatory effects of increasing MgADP concentrations in the presence of 0.1 mmol/l MgATP. Results show no significant differences in MgADP stimulation between the E23/S1369 and K23/A1369 haplotypes across a range of MgADP concentrations ( P > 0.05). n = 3–10 patches per group.

    Article Snippet: MgATP and MgADP (Sigma, Oakville, Ontario) were prepared as 10 mmol/l stocks in ddH2 O immediately prior to use.

    Techniques: Concentration Assay

    The increased gliclazide sensitivity of K23/A1369 variant K ATP channels is maintained in the presence of MgADP and is conferred upon the K ATP channel complex by the ABCC8 A1369 risk allele. A and B : Representative macroscopic current recordings showing the inhibitory effect of gliclazide (300 nmol/l) on the two variants in the presence of MgADP. C : Grouped data demonstrating that the K23/A1369 variant K ATP channels are significantly more sensitive to gliclazide in the presence of MgADP than the E23/S1369 variant K ATP channels. n = 10–12 patches per group. D–F : Representative current recordings and grouped data showing the increased gliclazide inhibitory effect is dependent on the presence of the ABCC8 A1369 variant and not the KCNJ11 K23 variant. n = 15 patches per group. * P

    Journal: Diabetes

    Article Title: Coexpression of the Type 2 Diabetes Susceptibility Gene Variants KCNJ11 E23K and ABCC8 S1369A Alter the ATP and Sulfonylurea Sensitivities of the ATP-Sensitive K+ Channel

    doi: 10.2337/db09-0143

    Figure Lengend Snippet: The increased gliclazide sensitivity of K23/A1369 variant K ATP channels is maintained in the presence of MgADP and is conferred upon the K ATP channel complex by the ABCC8 A1369 risk allele. A and B : Representative macroscopic current recordings showing the inhibitory effect of gliclazide (300 nmol/l) on the two variants in the presence of MgADP. C : Grouped data demonstrating that the K23/A1369 variant K ATP channels are significantly more sensitive to gliclazide in the presence of MgADP than the E23/S1369 variant K ATP channels. n = 10–12 patches per group. D–F : Representative current recordings and grouped data showing the increased gliclazide inhibitory effect is dependent on the presence of the ABCC8 A1369 variant and not the KCNJ11 K23 variant. n = 15 patches per group. * P

    Article Snippet: MgATP and MgADP (Sigma, Oakville, Ontario) were prepared as 10 mmol/l stocks in ddH2 O immediately prior to use.

    Techniques: Variant Assay

    Compared DNAzyme activity of experiments carried out with 22AG (100 nM), hemin (1 µM), H 2 O 2 (6 mM), ABTS ( A , 5 mM) or TMB ( B/C , 0.25 mM) in the presence of 10 mM ATP (brown lines), ADP (grey lines) or ADP-N-P (blue lines). The oxidation of ABTS is monitored via the appearance of the final product typical UV-Vis signal (420 nm, A ), the oxidation of TMB via that of both the final product (450 nm, B ) and the charge-transfer intermediate (652 nm, C ).

    Journal: Nucleic Acids Research

    Article Title: Insights into how nucleotide supplements enhance the peroxidase-mimicking DNAzyme activity of the G-quadruplex/hemin system

    doi: 10.1093/nar/gks581

    Figure Lengend Snippet: Compared DNAzyme activity of experiments carried out with 22AG (100 nM), hemin (1 µM), H 2 O 2 (6 mM), ABTS ( A , 5 mM) or TMB ( B/C , 0.25 mM) in the presence of 10 mM ATP (brown lines), ADP (grey lines) or ADP-N-P (blue lines). The oxidation of ABTS is monitored via the appearance of the final product typical UV-Vis signal (420 nm, A ), the oxidation of TMB via that of both the final product (450 nm, B ) and the charge-transfer intermediate (652 nm, C ).

    Article Snippet: Hemin, ABTS, 3,3′,5,5′-tetramethylbenzidine (TMB), adenosine diphosphate (ADP), nucleoside triphosphate (NTP) (N = A, T, C, G) were purchased from Sigma-Aldrich, and adenosine 5'-(β,γ-imido)triphosphate (ADP-N-P) from Jena Bioscience; all the chemicals were used without further purification.

    Techniques: Activity Assay

    Effect of an acute load of fructose in short-term high fructose fed fasted rats. ( A ) An acute load of fructose (2 g/kg BW) induced a significant increase in hepatic ADP in parallel with ATP depletion, thus increasing ADP/ATP ratio. Allopurinol treatment prevented such effect. ( B ) Plasma and ( C ) hepatic uric acid and triglycerides were increased by fructose acute load and allopurinol treatment prevented this effect. ( D ) Fructose induced hepatic oxidative stress that was prevented by allopurinol. On the other hand, glucose acute load did not induce any of the deleterious effects exerted by fructose in short term high glucose fed rats (white bars in all graphs). ** = p

    Journal: Biomolecules

    Article Title: Allopurinol Prevents the Lipogenic Response Induced by an Acute Oral Fructose Challenge in Short-Term Fructose Fed Rats

    doi: 10.3390/biom9100601

    Figure Lengend Snippet: Effect of an acute load of fructose in short-term high fructose fed fasted rats. ( A ) An acute load of fructose (2 g/kg BW) induced a significant increase in hepatic ADP in parallel with ATP depletion, thus increasing ADP/ATP ratio. Allopurinol treatment prevented such effect. ( B ) Plasma and ( C ) hepatic uric acid and triglycerides were increased by fructose acute load and allopurinol treatment prevented this effect. ( D ) Fructose induced hepatic oxidative stress that was prevented by allopurinol. On the other hand, glucose acute load did not induce any of the deleterious effects exerted by fructose in short term high glucose fed rats (white bars in all graphs). ** = p

    Article Snippet: Also, in liver samples from fasted or acute fructose/glucose loaded rats, markers of oxidative stress (lipid peroxidation and protein oxidation) and adenosine diphosphate/adenosine triphosphate (ADP/ATP) ratio (Sigma Aldrich, Darmstadt, Germany) were evaluated.

    Techniques:

    The antiplatelet effect of natto in normal rat platelet-rich plasma against ADP and collagen induced platelet aggregation. The inhibitory effects of natto water extract on adenosine 5′-diphosphate (ADP) and collagen induced normal rat platelet aggregation. (a) ADP induced aggregation, (b) collagen induced aggregation.

    Journal: Preventive Nutrition and Food Science

    Article Title: The Antithrombotic and Fibrinolytic Effect of Natto in Hypercholesterolemia Rats

    doi: 10.3746/pnf.2012.17.1.078

    Figure Lengend Snippet: The antiplatelet effect of natto in normal rat platelet-rich plasma against ADP and collagen induced platelet aggregation. The inhibitory effects of natto water extract on adenosine 5′-diphosphate (ADP) and collagen induced normal rat platelet aggregation. (a) ADP induced aggregation, (b) collagen induced aggregation.

    Article Snippet: Adenosine 5′-diphosphate (ADP) and collagen were purchased from the Chrono-log Corporation (Chicago, IL, USA) and aspirin from the Kun-wha Pharmaceutical Company (Seoul, Korea).

    Techniques:

    Bar graphs illustrate the effects of α,β-methylene-adenosine-5′-diphosphate (AMPCP; 100 μmol/l; CD73 inhibitor) on adenosine levels in the medium of rat PTCs, TALCs, and CDCs incubated with 10 μmol/l of either 5′-AMP

    Journal: American Journal of Physiology - Renal Physiology

    Article Title: Extracellular 2?,3?-cAMP-adenosine pathway in proximal tubular, thick ascending limb, and collecting duct epithelial cells

    doi: 10.1152/ajprenal.00571.2012

    Figure Lengend Snippet: Bar graphs illustrate the effects of α,β-methylene-adenosine-5′-diphosphate (AMPCP; 100 μmol/l; CD73 inhibitor) on adenosine levels in the medium of rat PTCs, TALCs, and CDCs incubated with 10 μmol/l of either 5′-AMP

    Article Snippet: Cells were washed twice with HEPES-buffered Hanks balanced salt solution and then incubated for 1 h in 0.5 ml of Dulbecco's phosphate-buffered saline with HEPES (25 mmol/l) and NaHCO3 (13 mmol/l) in the presence and absence of 2′,3′-cAMP, 5′-AMP, 3′-AMP, or 2′-AMP with or without α,β-methylene-adenosine-5′-diphosphate (AMPCP; selective inhibitor of CD73) , 3-isobutyl-1-methylxanthine (IBMX; broad spectrum phosphodiesterase inhibitor) , 1,3-dipropyl-8-p-sulfophenylxanthine (DPSPX; ecto-phosphodiesterase inhibitor) ( , , ), all from Sigma (St. Louis, MO).

    Techniques: Incubation

    Mitofilin is indispensable for mitochondrial homeostasis and osteogenesis of BMMSCs. (A-D) Representative transmission electron microscopy images (A) and quantitative analysis of the ratio of mitochondrial inner membrane versus outer membrane (B) as well as mitochondrial average area (C) and number (D) per cell in BMMSCs. Bars: 125 nm (high magnification). (E, F) Rhodamine 123 detection of mitochondrial membrane potential of BMMSCs (E) with quantitative analysis of fluorescence intensity (F) . Bars: 10 μm. (G, H) DCFDA detection of total ROS level in BMMSCs (G) with flow cytometric quantitative analysis of fluorescence intensity (H) . Bars: 10 μm. (I) Quantitative analysis of ATP production versus ADP ratio in BMMSCs. (J) qRT-PCR analysis of mRNA expression levels of all 13 mtDNA-encoded mitochondrial complex subunits in BMMSCs. (K-M) Representative images of ALP and alizarin red staining (K) with quantification of ALP activity (L) and mineralization (M) in osteogenic differentiation of BMMSCs. Bars: 5 mm. (N) qRT-PCR analysis of mRNA expression levels of osteogenic marker genes in osteogenic differentiation of BMMSCs. BMMSCs from 4-month-old SAMR1 mice were transfected with either the shRNA for Immt (Mitofilin) or the negative control (a scrambled sequence, NC) by a lentiviral vector. n = 3 per group. Data represent mean ± SD. * P

    Journal: Theranostics

    Article Title: Resveratrol counteracts bone loss via mitofilin-mediated osteogenic improvement of mesenchymal stem cells in senescence-accelerated mice

    doi: 10.7150/thno.23620

    Figure Lengend Snippet: Mitofilin is indispensable for mitochondrial homeostasis and osteogenesis of BMMSCs. (A-D) Representative transmission electron microscopy images (A) and quantitative analysis of the ratio of mitochondrial inner membrane versus outer membrane (B) as well as mitochondrial average area (C) and number (D) per cell in BMMSCs. Bars: 125 nm (high magnification). (E, F) Rhodamine 123 detection of mitochondrial membrane potential of BMMSCs (E) with quantitative analysis of fluorescence intensity (F) . Bars: 10 μm. (G, H) DCFDA detection of total ROS level in BMMSCs (G) with flow cytometric quantitative analysis of fluorescence intensity (H) . Bars: 10 μm. (I) Quantitative analysis of ATP production versus ADP ratio in BMMSCs. (J) qRT-PCR analysis of mRNA expression levels of all 13 mtDNA-encoded mitochondrial complex subunits in BMMSCs. (K-M) Representative images of ALP and alizarin red staining (K) with quantification of ALP activity (L) and mineralization (M) in osteogenic differentiation of BMMSCs. Bars: 5 mm. (N) qRT-PCR analysis of mRNA expression levels of osteogenic marker genes in osteogenic differentiation of BMMSCs. BMMSCs from 4-month-old SAMR1 mice were transfected with either the shRNA for Immt (Mitofilin) or the negative control (a scrambled sequence, NC) by a lentiviral vector. n = 3 per group. Data represent mean ± SD. * P

    Article Snippet: Metabolic analysis The ratio of adenosine triphosphate (ATP) over adenosine diphosphate (ADP) was measured according to recent papers using the ADP/ATP Ratio Assay Kit (Abcam, UK) following the manufacturer's instructions .

    Techniques: Transmission Assay, Electron Microscopy, Fluorescence, Flow Cytometry, Quantitative RT-PCR, Expressing, ALP Assay, Staining, Activity Assay, Marker, Mouse Assay, Transfection, shRNA, Negative Control, Sequencing, Plasmid Preparation

    Resveratrol improves mitochondrial functionality and transcription in BMMSCs derived from SAMP6 mice. (A) Quantitative analysis of ATP production versus ADP ratio in BMMSCs. (B, C) DCFDA detection of total ROS level in BMMSCs (B) with flow cytometric quantitative analysis of fluorescence intensity (C) . Bars: 10 μm. (D, E) Rhodamine 123 detection of mitochondrial membrane potential of BMMSCs (D) with quantitative analysis of fluorescence intensity (E) . Bars: 10 μm. (F) Kinetic analysis of oxygen consumption as an index of mitochondrial OXPHOS activity in cultured BMMSCs. (G, H) qRT-PCR analysis of mRNA expression levels of nuclear-encoded (G) and mtDNA-encoded (H) gene representatives for mitochondrial complex subunits of BMMSCs. BMMSCs from 4-month-old SAMP6 mice were treated with either resveratrol (10 μM) or the DMSO (0.001%) solvent control. n = 3 per group. Data represent mean ± SD. * P

    Journal: Theranostics

    Article Title: Resveratrol counteracts bone loss via mitofilin-mediated osteogenic improvement of mesenchymal stem cells in senescence-accelerated mice

    doi: 10.7150/thno.23620

    Figure Lengend Snippet: Resveratrol improves mitochondrial functionality and transcription in BMMSCs derived from SAMP6 mice. (A) Quantitative analysis of ATP production versus ADP ratio in BMMSCs. (B, C) DCFDA detection of total ROS level in BMMSCs (B) with flow cytometric quantitative analysis of fluorescence intensity (C) . Bars: 10 μm. (D, E) Rhodamine 123 detection of mitochondrial membrane potential of BMMSCs (D) with quantitative analysis of fluorescence intensity (E) . Bars: 10 μm. (F) Kinetic analysis of oxygen consumption as an index of mitochondrial OXPHOS activity in cultured BMMSCs. (G, H) qRT-PCR analysis of mRNA expression levels of nuclear-encoded (G) and mtDNA-encoded (H) gene representatives for mitochondrial complex subunits of BMMSCs. BMMSCs from 4-month-old SAMP6 mice were treated with either resveratrol (10 μM) or the DMSO (0.001%) solvent control. n = 3 per group. Data represent mean ± SD. * P

    Article Snippet: Metabolic analysis The ratio of adenosine triphosphate (ATP) over adenosine diphosphate (ADP) was measured according to recent papers using the ADP/ATP Ratio Assay Kit (Abcam, UK) following the manufacturer's instructions .

    Techniques: Derivative Assay, Mouse Assay, Flow Cytometry, Fluorescence, Activity Assay, Cell Culture, Quantitative RT-PCR, Expressing

    Processive strand incision requires the closed form of MutL. ( A ) Size exclusion chromatography of open and closed forms of MutL. Left panel: wild type MutL was observed in the open state without nucleotide (black), with ADP (green) and ATP (red), but closed with AMP.PNP (blue). MutL N302A was always observed in the closed state in the presence of nucleotide (middle panel) and MutL K307A was always observed in the open in the presence of nucleotides (right panel). ( B ) Incision of 0.5 nM GT#2 by 100 nM MutS, 100 nM MutL, 50 nM MutH with wild type (first panel), N302A (second panel) and K307A MutL variants (third panel with 50 nM MutH, fourth panel with 250 nM MutH). ( C ) Quantification (mean ± SD, n = 3) and fitting of strand incision by wild type, N302A and K307A MutL (with 50 and 250 nM MutH). Rate constants obtained from the fits are tabulated in Supplementary Table S1.

    Journal: Nucleic Acids Research

    Article Title: Dual daughter strand incision is processive and increases the efficiency of DNA mismatch repair

    doi: 10.1093/nar/gkw411

    Figure Lengend Snippet: Processive strand incision requires the closed form of MutL. ( A ) Size exclusion chromatography of open and closed forms of MutL. Left panel: wild type MutL was observed in the open state without nucleotide (black), with ADP (green) and ATP (red), but closed with AMP.PNP (blue). MutL N302A was always observed in the closed state in the presence of nucleotide (middle panel) and MutL K307A was always observed in the open in the presence of nucleotides (right panel). ( B ) Incision of 0.5 nM GT#2 by 100 nM MutS, 100 nM MutL, 50 nM MutH with wild type (first panel), N302A (second panel) and K307A MutL variants (third panel with 50 nM MutH, fourth panel with 250 nM MutH). ( C ) Quantification (mean ± SD, n = 3) and fitting of strand incision by wild type, N302A and K307A MutL (with 50 and 250 nM MutH). Rate constants obtained from the fits are tabulated in Supplementary Table S1.

    Article Snippet: Size exclusion chromatography MutL (1.5 mg/ml) in 25 mM Hepes-KOH pH 7.5, 150 mM KCl, 5 mM MgCl2 , 10% glycerol, 10 mM β-mercaptoethanol was mixed with 1 mM adenosine diphosphate (ADP), ATP or adenylylimidodiphosphate (AMPPNP), or buffer as control, incubated for 16 h at 4°C and injected on an Superdex 200 size exclusion column equilibrated in 25 mM Hepes-KOH pH 7.5, 150 mM KCl, 5 mM MgCl2 , 10% glycerol and operated by an ÄktaMikro (GE Healthcare).

    Techniques: Size-exclusion Chromatography

    Myocardial measurements at baseline (BL) and during ventricular fibrillation (VF), at 10 and 16 minutes while on low-flow extracorporeal circulation simulating the hemodynamic conditions of closed-chest CPR. pCr, phosphocreatine; ATP, adenosine triphosphate; ADP, adenosine diphosphate; AMP, adenosine monophosphate; Ado, adenosine. Data was analyzed by one-way repeated measures ANOVA and differences shown after Holm-Sidak method for multiple pairwise comparisons. a vs BL, b vs VF10; * p ≤ 0.05, † p ≤ 0.001.

    Journal: PLoS ONE

    Article Title: Ventricular Fibrillation Waveform Changes during Controlled Coronary Perfusion Using Extracorporeal Circulation in a Swine Model

    doi: 10.1371/journal.pone.0161166

    Figure Lengend Snippet: Myocardial measurements at baseline (BL) and during ventricular fibrillation (VF), at 10 and 16 minutes while on low-flow extracorporeal circulation simulating the hemodynamic conditions of closed-chest CPR. pCr, phosphocreatine; ATP, adenosine triphosphate; ADP, adenosine diphosphate; AMP, adenosine monophosphate; Ado, adenosine. Data was analyzed by one-way repeated measures ANOVA and differences shown after Holm-Sidak method for multiple pairwise comparisons. a vs BL, b vs VF10; * p ≤ 0.05, † p ≤ 0.001.

    Article Snippet: Samples were immersed in liquid N2 within 10 seconds, stored at -80°C, and subsequently processed for creatine, phosphocreatine, adenosine, adenosine monophosphate, adenosine diphosphate (ADP), and adenosine triphosphate (ATP) using reverse-phase high-performance liquid chromatography (System Gold, Beckman, and 32 Karat Software 5.0, Fullerton, CA) along with lactate concentration as previously described [ ].

    Techniques: Flow Cytometry, Polymerase Chain Reaction

    Complex of the apoenzyme with adenosine 5′-diphosphoribose (ADPR). The stereoview is derived from PDB entry 5VKR. The 2| F o | – | F c | map is contoured at ∼0.25 e – /Å 3 .

    Journal: Biochemistry

    Article Title: Horse Liver Alcohol Dehydrogenase: Zinc Coordination and Catalysis

    doi: 10.1021/acs.biochem.7b00446

    Figure Lengend Snippet: Complex of the apoenzyme with adenosine 5′-diphosphoribose (ADPR). The stereoview is derived from PDB entry 5VKR. The 2| F o | – | F c | map is contoured at ∼0.25 e – /Å 3 .

    Article Snippet: 1,10-Phenanthroline, 2,2′-bipyridine, and adenosine 5′-diphosphoribose were obtained from Sigma.

    Techniques: Derivative Assay

    Characterization of DsRed-NT5E fusion proteins. A. COS-7 cells were transiently transfected with an expression vector for DsRed fused to wild type form of human NT5E (DsRed-hNT5E WT) and fusion proteins were localized by immunofluorescence with antibodies against fluorescent DsRed (green) and native hNT5E (red) proteins, and by internal fluorescence (purple). The merged picture shows obvious overlap of all 3 signals indicating that DsRed-hNT5E fusion protein is intact and contains both antigens. Magnification 400X . B. Immunoblot analysis of total protein extracts from mock-transfected (mock) or transfected COS-7 cells with expression vectors for DsRed monomer and DsRed-hNT5E (DsRed NT5E) fusion protein using DsRed (left) and hNT5E (right) antibodies. Both antibodies detect a protein with a molecular weight of approximately 90 kiloDaltons (black arrowheads, left and right) while DsRed antibody only detects the DsRed monomer (white arrowhead, left) indicating that DsRed-hNT5E fusion is intact and contains both antigens. Total β-actin protein was used as loading control. C. Enzyme histochemistry of mock-transfected or transfected COS-7 cells with expression vectors for DsRed-hNT5E wild type (WT) and mutant (F1–3) proteins using adenosine monophosphate (AMP) as substrate. Only COS–7 cells transfected with the expression vector for DsRed-hNT5E wild type fusion protein displayed AMPase activity, which could be blocked in presence of known NT5E inhibitor α/β-methylene-ADP. Mock-transfected or COS-7 cells transfected with expression vectors for DsRed-hNT5E mutant (F1–3) proteins lack AMPase activity. Magnification 200X .

    Journal: PLoS ONE

    Article Title: NT5E Mutations That Cause Human Disease Are Associated with Intracellular Mistrafficking of NT5E Protein

    doi: 10.1371/journal.pone.0098568

    Figure Lengend Snippet: Characterization of DsRed-NT5E fusion proteins. A. COS-7 cells were transiently transfected with an expression vector for DsRed fused to wild type form of human NT5E (DsRed-hNT5E WT) and fusion proteins were localized by immunofluorescence with antibodies against fluorescent DsRed (green) and native hNT5E (red) proteins, and by internal fluorescence (purple). The merged picture shows obvious overlap of all 3 signals indicating that DsRed-hNT5E fusion protein is intact and contains both antigens. Magnification 400X . B. Immunoblot analysis of total protein extracts from mock-transfected (mock) or transfected COS-7 cells with expression vectors for DsRed monomer and DsRed-hNT5E (DsRed NT5E) fusion protein using DsRed (left) and hNT5E (right) antibodies. Both antibodies detect a protein with a molecular weight of approximately 90 kiloDaltons (black arrowheads, left and right) while DsRed antibody only detects the DsRed monomer (white arrowhead, left) indicating that DsRed-hNT5E fusion is intact and contains both antigens. Total β-actin protein was used as loading control. C. Enzyme histochemistry of mock-transfected or transfected COS-7 cells with expression vectors for DsRed-hNT5E wild type (WT) and mutant (F1–3) proteins using adenosine monophosphate (AMP) as substrate. Only COS–7 cells transfected with the expression vector for DsRed-hNT5E wild type fusion protein displayed AMPase activity, which could be blocked in presence of known NT5E inhibitor α/β-methylene-ADP. Mock-transfected or COS-7 cells transfected with expression vectors for DsRed-hNT5E mutant (F1–3) proteins lack AMPase activity. Magnification 200X .

    Article Snippet: In a separate set of experiments, 1 mM α/β-methylene-ADP (Sigma) was used as a hNT5E inhibitor.

    Techniques: Transfection, Expressing, Plasmid Preparation, Immunofluorescence, Fluorescence, Molecular Weight, Mutagenesis, Activity Assay