biotinylated cardiolipin  (Echelon Biosciences)


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    Echelon Biosciences biotinylated cardiolipin
    Related to main . (a) Effect of <t>cardiolipin</t> on far-UV circular diagram (CD) spectra of α-Syn. Phosphate buffer, pH – 7.2, at 25 °C. In presence of cardiolipin, secondary structure of α-Syn changes from the random coil to alpha-helical form measured in pH 7.2 Phosphate buffer at 25 °C. In the absence of cardiolipin vesicles CD spectra was flat except minima at around 198 (black curve), which is characteristic spectra of a random coil. In the presence of CL vesicles at protein to lipid ratio 1:8 (red curve) and 1:16 (blue curve) a significant change occurred in the spectra, with minima at value at 222 nm and 208 nm, which is the characteristic spectra of the alpha-helical form of proteins. (b) Kinetics of amyloid formation by α-Syn (50 µM) in the presence of DMPS (curve 1 – 4) and in the presence of DMPC (curve 5 – 8). Measurements were performed at 30 °C and pH 7.4. Protein concentration was 50 µM and lipid vesicle concentration was 400 µM. ThT fluorescence was excited at 450 nm, and the emission wavelength was 482 nm. (c) Control images for .
    Biotinylated Cardiolipin, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93/100 stars

    Images

    1) Product Images from "Structural conversion of α-synuclein at the mitochondria induces neuronal toxicity"

    Article Title: Structural conversion of α-synuclein at the mitochondria induces neuronal toxicity

    Journal: bioRxiv

    doi: 10.1101/2022.06.07.494932

    Related to main . (a) Effect of cardiolipin on far-UV circular diagram (CD) spectra of α-Syn. Phosphate buffer, pH – 7.2, at 25 °C. In presence of cardiolipin, secondary structure of α-Syn changes from the random coil to alpha-helical form measured in pH 7.2 Phosphate buffer at 25 °C. In the absence of cardiolipin vesicles CD spectra was flat except minima at around 198 (black curve), which is characteristic spectra of a random coil. In the presence of CL vesicles at protein to lipid ratio 1:8 (red curve) and 1:16 (blue curve) a significant change occurred in the spectra, with minima at value at 222 nm and 208 nm, which is the characteristic spectra of the alpha-helical form of proteins. (b) Kinetics of amyloid formation by α-Syn (50 µM) in the presence of DMPS (curve 1 – 4) and in the presence of DMPC (curve 5 – 8). Measurements were performed at 30 °C and pH 7.4. Protein concentration was 50 µM and lipid vesicle concentration was 400 µM. ThT fluorescence was excited at 450 nm, and the emission wavelength was 482 nm. (c) Control images for .
    Figure Legend Snippet: Related to main . (a) Effect of cardiolipin on far-UV circular diagram (CD) spectra of α-Syn. Phosphate buffer, pH – 7.2, at 25 °C. In presence of cardiolipin, secondary structure of α-Syn changes from the random coil to alpha-helical form measured in pH 7.2 Phosphate buffer at 25 °C. In the absence of cardiolipin vesicles CD spectra was flat except minima at around 198 (black curve), which is characteristic spectra of a random coil. In the presence of CL vesicles at protein to lipid ratio 1:8 (red curve) and 1:16 (blue curve) a significant change occurred in the spectra, with minima at value at 222 nm and 208 nm, which is the characteristic spectra of the alpha-helical form of proteins. (b) Kinetics of amyloid formation by α-Syn (50 µM) in the presence of DMPS (curve 1 – 4) and in the presence of DMPC (curve 5 – 8). Measurements were performed at 30 °C and pH 7.4. Protein concentration was 50 µM and lipid vesicle concentration was 400 µM. ThT fluorescence was excited at 450 nm, and the emission wavelength was 482 nm. (c) Control images for .

    Techniques Used: Protein Concentration, Concentration Assay, Fluorescence

    (ai – iv) 50 µM A53T monomer led to a dramatically fast increase in ThT fluorescence in the presence of 40 % or 100 % cardiolipin as compared to WT monomer. (bi) TEM images show that in the presence of cardiolipin, fibrils of α-Syn have different morphology. A total 200 fibrils were analyzed for each group by Image J software . (bii) Quantitative histogram of fibril width shows large distribution of width in the presence of cardiolipin, which is expected for a hierarchical self-assembly model of amyloid formation. (c) TIRFM analysis shows co-localization of cardiolipin and α-Syn fibrils (ThT positive). 0.5 µM α -Syn amyloid fibrils and in the presence of 4 µM cardiolipin vesicles (containing 2 mol % of biotinylated lipid) in the presence of 1 nM streptavidin-AF647 and 5 µµM ThT. Images were recorded for 50 frames from the red channel (AF647 emission) with 641 nm illumination, followed by green channel (ThT emission) with 405 nm illumination. Note . Data are represented as mean ± SEM; n = 3 independent experiments. See also .
    Figure Legend Snippet: (ai – iv) 50 µM A53T monomer led to a dramatically fast increase in ThT fluorescence in the presence of 40 % or 100 % cardiolipin as compared to WT monomer. (bi) TEM images show that in the presence of cardiolipin, fibrils of α-Syn have different morphology. A total 200 fibrils were analyzed for each group by Image J software . (bii) Quantitative histogram of fibril width shows large distribution of width in the presence of cardiolipin, which is expected for a hierarchical self-assembly model of amyloid formation. (c) TIRFM analysis shows co-localization of cardiolipin and α-Syn fibrils (ThT positive). 0.5 µM α -Syn amyloid fibrils and in the presence of 4 µM cardiolipin vesicles (containing 2 mol % of biotinylated lipid) in the presence of 1 nM streptavidin-AF647 and 5 µµM ThT. Images were recorded for 50 frames from the red channel (AF647 emission) with 641 nm illumination, followed by green channel (ThT emission) with 405 nm illumination. Note . Data are represented as mean ± SEM; n = 3 independent experiments. See also .

    Techniques Used: Fluorescence, Software

    (ai) Representative images showing both FRET intensity and FRET efficiency of A53T are reduced by treatment with Mito-TEMPO. (aii & iii) Mito-TEMPO treated cells show reduced A53T FRET intensity (A53T alone vs Mito-T (Mito-TEMPO): p = 0.024, A53T alone vs Trolox: p = 0.021) and efficiency (A53T alone vs Mito-T: p = 0.011, A53T alone vs Trolox: p = 0.039). (aiv) Application of Trolox to cells reduces FRET intensity signal through reducing uptake of donor (A53T alone vs Trolox: p = 0.020). (bi & ii) Cell death induced by 48-hour incubation of A53T ( p = 0.027), but by WT nor A30P/E46K. (ci & ii) A53T induced cell death was rescued by treatment either with Trolox (A53T alone vs Trolox: p = 0.018) or Mito-TEMPO (A53T alone vs Mito-T: p < 0.0001). (d) Graphical illustration demonstrating how α-Syn monomers form aggregates inside neurons and induce cell toxicity; The intracellular monomeric population begins to self-assemble first into a population of amorphous loosely ordered oligomeric species, and progresses to form highly ordered oligomeric species. Aggregates form with a dense central core of highly ordered oligomer surrounded by a rim of loosely packed oligomers, and occur in multiple hotspots throughout the cell body including the nucleus, Golgi and mitochondria. Mitochondria are a crucial site of aggregation: cardiolipin triggers oligomerization of A53T α-Syn. A53T α-Syn induces over-production of mROS promoting oligomerization of α-Syn. A53T α-Syn oligomerization promotes early opening of mPTP leading to cell death. Note . 100 μM Trolox, 0.5 μM Mito-TEMPO were pre-treated 30 min prior to α-Syn application. Data are presented as mean ± SEM. n = 3 – 5 number of wells. Total number of cells = 180 – 491. All experiments were independently repeated 2 – 3 times. *p<0.05, **p<0.001, ***p<0.0001.
    Figure Legend Snippet: (ai) Representative images showing both FRET intensity and FRET efficiency of A53T are reduced by treatment with Mito-TEMPO. (aii & iii) Mito-TEMPO treated cells show reduced A53T FRET intensity (A53T alone vs Mito-T (Mito-TEMPO): p = 0.024, A53T alone vs Trolox: p = 0.021) and efficiency (A53T alone vs Mito-T: p = 0.011, A53T alone vs Trolox: p = 0.039). (aiv) Application of Trolox to cells reduces FRET intensity signal through reducing uptake of donor (A53T alone vs Trolox: p = 0.020). (bi & ii) Cell death induced by 48-hour incubation of A53T ( p = 0.027), but by WT nor A30P/E46K. (ci & ii) A53T induced cell death was rescued by treatment either with Trolox (A53T alone vs Trolox: p = 0.018) or Mito-TEMPO (A53T alone vs Mito-T: p < 0.0001). (d) Graphical illustration demonstrating how α-Syn monomers form aggregates inside neurons and induce cell toxicity; The intracellular monomeric population begins to self-assemble first into a population of amorphous loosely ordered oligomeric species, and progresses to form highly ordered oligomeric species. Aggregates form with a dense central core of highly ordered oligomer surrounded by a rim of loosely packed oligomers, and occur in multiple hotspots throughout the cell body including the nucleus, Golgi and mitochondria. Mitochondria are a crucial site of aggregation: cardiolipin triggers oligomerization of A53T α-Syn. A53T α-Syn induces over-production of mROS promoting oligomerization of α-Syn. A53T α-Syn oligomerization promotes early opening of mPTP leading to cell death. Note . 100 μM Trolox, 0.5 μM Mito-TEMPO were pre-treated 30 min prior to α-Syn application. Data are presented as mean ± SEM. n = 3 – 5 number of wells. Total number of cells = 180 – 491. All experiments were independently repeated 2 – 3 times. *p<0.05, **p<0.001, ***p<0.0001.

    Techniques Used: Incubation

    cardiolipin  (Echelon Biosciences)


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    Echelon Biosciences cardiolipin
    ( A ) Schematic diagrams of the full-length spartin with the MIT and the plant-related senescence domains and the MBP-spartin (421–607) construct encompassing the plant-related senescence domain. Numbers represent the amino acid residues, showing the boundaries of indicated domains. ( B ) Coomassie blue staining of affinity-purified MBP and MBP-spartin (421–607) separated on a polyacrylamide gel. The asterisk (*) indicates a degradation product of MBP-spartin (421–607). Sizes of protein standards are indicated to the left in kDa. ( C ) Detection of MBP-spartin (421–607) binding to <t>cardiolipin</t> but not to phosphatidylethanolamine or phosphatidylcholine in a lipid-protein overlay assay. MBP alone (negative control) did not associate with cardiolipin, phosphatidylethanolamine, or phosphatidylcholine.
    Cardiolipin, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "SPG20 Protein Spartin Associates with Cardiolipin via Its Plant-Related Senescence Domain and Regulates Mitochondrial Ca 2+ Homeostasis"

    Article Title: SPG20 Protein Spartin Associates with Cardiolipin via Its Plant-Related Senescence Domain and Regulates Mitochondrial Ca 2+ Homeostasis

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0019290

    ( A ) Schematic diagrams of the full-length spartin with the MIT and the plant-related senescence domains and the MBP-spartin (421–607) construct encompassing the plant-related senescence domain. Numbers represent the amino acid residues, showing the boundaries of indicated domains. ( B ) Coomassie blue staining of affinity-purified MBP and MBP-spartin (421–607) separated on a polyacrylamide gel. The asterisk (*) indicates a degradation product of MBP-spartin (421–607). Sizes of protein standards are indicated to the left in kDa. ( C ) Detection of MBP-spartin (421–607) binding to cardiolipin but not to phosphatidylethanolamine or phosphatidylcholine in a lipid-protein overlay assay. MBP alone (negative control) did not associate with cardiolipin, phosphatidylethanolamine, or phosphatidylcholine.
    Figure Legend Snippet: ( A ) Schematic diagrams of the full-length spartin with the MIT and the plant-related senescence domains and the MBP-spartin (421–607) construct encompassing the plant-related senescence domain. Numbers represent the amino acid residues, showing the boundaries of indicated domains. ( B ) Coomassie blue staining of affinity-purified MBP and MBP-spartin (421–607) separated on a polyacrylamide gel. The asterisk (*) indicates a degradation product of MBP-spartin (421–607). Sizes of protein standards are indicated to the left in kDa. ( C ) Detection of MBP-spartin (421–607) binding to cardiolipin but not to phosphatidylethanolamine or phosphatidylcholine in a lipid-protein overlay assay. MBP alone (negative control) did not associate with cardiolipin, phosphatidylethanolamine, or phosphatidylcholine.

    Techniques Used: Construct, Staining, Affinity Purification, Binding Assay, Overlay Assay, Negative Control

    biotinylated cardiolipin  (Echelon Biosciences)


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    Echelon Biosciences biotinylated cardiolipin
    Related to main . (a) Effect of <t>cardiolipin</t> on far-UV circular diagram (CD) spectra of α-Syn. Phosphate buffer, pH – 7.2, at 25 °C. In presence of cardiolipin, secondary structure of α-Syn changes from the random coil to alpha-helical form measured in pH 7.2 Phosphate buffer at 25 °C. In the absence of cardiolipin vesicles CD spectra was flat except minima at around 198 (black curve), which is characteristic spectra of a random coil. In the presence of CL vesicles at protein to lipid ratio 1:8 (red curve) and 1:16 (blue curve) a significant change occurred in the spectra, with minima at value at 222 nm and 208 nm, which is the characteristic spectra of the alpha-helical form of proteins. (b) Kinetics of amyloid formation by α-Syn (50 µM) in the presence of DMPS (curve 1 – 4) and in the presence of DMPC (curve 5 – 8). Measurements were performed at 30 °C and pH 7.4. Protein concentration was 50 µM and lipid vesicle concentration was 400 µM. ThT fluorescence was excited at 450 nm, and the emission wavelength was 482 nm. (c) Control images for .
    Biotinylated Cardiolipin, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated cardiolipin/product/Echelon Biosciences
    Average 93 stars, based on 1 article reviews
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    biotinylated cardiolipin - by Bioz Stars, 2023-03
    93/100 stars

    Images

    1) Product Images from "Structural conversion of α-synuclein at the mitochondria induces neuronal toxicity"

    Article Title: Structural conversion of α-synuclein at the mitochondria induces neuronal toxicity

    Journal: bioRxiv

    doi: 10.1101/2022.06.07.494932

    Related to main . (a) Effect of cardiolipin on far-UV circular diagram (CD) spectra of α-Syn. Phosphate buffer, pH – 7.2, at 25 °C. In presence of cardiolipin, secondary structure of α-Syn changes from the random coil to alpha-helical form measured in pH 7.2 Phosphate buffer at 25 °C. In the absence of cardiolipin vesicles CD spectra was flat except minima at around 198 (black curve), which is characteristic spectra of a random coil. In the presence of CL vesicles at protein to lipid ratio 1:8 (red curve) and 1:16 (blue curve) a significant change occurred in the spectra, with minima at value at 222 nm and 208 nm, which is the characteristic spectra of the alpha-helical form of proteins. (b) Kinetics of amyloid formation by α-Syn (50 µM) in the presence of DMPS (curve 1 – 4) and in the presence of DMPC (curve 5 – 8). Measurements were performed at 30 °C and pH 7.4. Protein concentration was 50 µM and lipid vesicle concentration was 400 µM. ThT fluorescence was excited at 450 nm, and the emission wavelength was 482 nm. (c) Control images for .
    Figure Legend Snippet: Related to main . (a) Effect of cardiolipin on far-UV circular diagram (CD) spectra of α-Syn. Phosphate buffer, pH – 7.2, at 25 °C. In presence of cardiolipin, secondary structure of α-Syn changes from the random coil to alpha-helical form measured in pH 7.2 Phosphate buffer at 25 °C. In the absence of cardiolipin vesicles CD spectra was flat except minima at around 198 (black curve), which is characteristic spectra of a random coil. In the presence of CL vesicles at protein to lipid ratio 1:8 (red curve) and 1:16 (blue curve) a significant change occurred in the spectra, with minima at value at 222 nm and 208 nm, which is the characteristic spectra of the alpha-helical form of proteins. (b) Kinetics of amyloid formation by α-Syn (50 µM) in the presence of DMPS (curve 1 – 4) and in the presence of DMPC (curve 5 – 8). Measurements were performed at 30 °C and pH 7.4. Protein concentration was 50 µM and lipid vesicle concentration was 400 µM. ThT fluorescence was excited at 450 nm, and the emission wavelength was 482 nm. (c) Control images for .

    Techniques Used: Protein Concentration, Concentration Assay, Fluorescence

    (ai – iv) 50 µM A53T monomer led to a dramatically fast increase in ThT fluorescence in the presence of 40 % or 100 % cardiolipin as compared to WT monomer. (bi) TEM images show that in the presence of cardiolipin, fibrils of α-Syn have different morphology. A total 200 fibrils were analyzed for each group by Image J software . (bii) Quantitative histogram of fibril width shows large distribution of width in the presence of cardiolipin, which is expected for a hierarchical self-assembly model of amyloid formation. (c) TIRFM analysis shows co-localization of cardiolipin and α-Syn fibrils (ThT positive). 0.5 µM α -Syn amyloid fibrils and in the presence of 4 µM cardiolipin vesicles (containing 2 mol % of biotinylated lipid) in the presence of 1 nM streptavidin-AF647 and 5 µµM ThT. Images were recorded for 50 frames from the red channel (AF647 emission) with 641 nm illumination, followed by green channel (ThT emission) with 405 nm illumination. Note . Data are represented as mean ± SEM; n = 3 independent experiments. See also .
    Figure Legend Snippet: (ai – iv) 50 µM A53T monomer led to a dramatically fast increase in ThT fluorescence in the presence of 40 % or 100 % cardiolipin as compared to WT monomer. (bi) TEM images show that in the presence of cardiolipin, fibrils of α-Syn have different morphology. A total 200 fibrils were analyzed for each group by Image J software . (bii) Quantitative histogram of fibril width shows large distribution of width in the presence of cardiolipin, which is expected for a hierarchical self-assembly model of amyloid formation. (c) TIRFM analysis shows co-localization of cardiolipin and α-Syn fibrils (ThT positive). 0.5 µM α -Syn amyloid fibrils and in the presence of 4 µM cardiolipin vesicles (containing 2 mol % of biotinylated lipid) in the presence of 1 nM streptavidin-AF647 and 5 µµM ThT. Images were recorded for 50 frames from the red channel (AF647 emission) with 641 nm illumination, followed by green channel (ThT emission) with 405 nm illumination. Note . Data are represented as mean ± SEM; n = 3 independent experiments. See also .

    Techniques Used: Fluorescence, Software

    (ai) Representative images showing both FRET intensity and FRET efficiency of A53T are reduced by treatment with Mito-TEMPO. (aii & iii) Mito-TEMPO treated cells show reduced A53T FRET intensity (A53T alone vs Mito-T (Mito-TEMPO): p = 0.024, A53T alone vs Trolox: p = 0.021) and efficiency (A53T alone vs Mito-T: p = 0.011, A53T alone vs Trolox: p = 0.039). (aiv) Application of Trolox to cells reduces FRET intensity signal through reducing uptake of donor (A53T alone vs Trolox: p = 0.020). (bi & ii) Cell death induced by 48-hour incubation of A53T ( p = 0.027), but by WT nor A30P/E46K. (ci & ii) A53T induced cell death was rescued by treatment either with Trolox (A53T alone vs Trolox: p = 0.018) or Mito-TEMPO (A53T alone vs Mito-T: p < 0.0001). (d) Graphical illustration demonstrating how α-Syn monomers form aggregates inside neurons and induce cell toxicity; The intracellular monomeric population begins to self-assemble first into a population of amorphous loosely ordered oligomeric species, and progresses to form highly ordered oligomeric species. Aggregates form with a dense central core of highly ordered oligomer surrounded by a rim of loosely packed oligomers, and occur in multiple hotspots throughout the cell body including the nucleus, Golgi and mitochondria. Mitochondria are a crucial site of aggregation: cardiolipin triggers oligomerization of A53T α-Syn. A53T α-Syn induces over-production of mROS promoting oligomerization of α-Syn. A53T α-Syn oligomerization promotes early opening of mPTP leading to cell death. Note . 100 μM Trolox, 0.5 μM Mito-TEMPO were pre-treated 30 min prior to α-Syn application. Data are presented as mean ± SEM. n = 3 – 5 number of wells. Total number of cells = 180 – 491. All experiments were independently repeated 2 – 3 times. *p<0.05, **p<0.001, ***p<0.0001.
    Figure Legend Snippet: (ai) Representative images showing both FRET intensity and FRET efficiency of A53T are reduced by treatment with Mito-TEMPO. (aii & iii) Mito-TEMPO treated cells show reduced A53T FRET intensity (A53T alone vs Mito-T (Mito-TEMPO): p = 0.024, A53T alone vs Trolox: p = 0.021) and efficiency (A53T alone vs Mito-T: p = 0.011, A53T alone vs Trolox: p = 0.039). (aiv) Application of Trolox to cells reduces FRET intensity signal through reducing uptake of donor (A53T alone vs Trolox: p = 0.020). (bi & ii) Cell death induced by 48-hour incubation of A53T ( p = 0.027), but by WT nor A30P/E46K. (ci & ii) A53T induced cell death was rescued by treatment either with Trolox (A53T alone vs Trolox: p = 0.018) or Mito-TEMPO (A53T alone vs Mito-T: p < 0.0001). (d) Graphical illustration demonstrating how α-Syn monomers form aggregates inside neurons and induce cell toxicity; The intracellular monomeric population begins to self-assemble first into a population of amorphous loosely ordered oligomeric species, and progresses to form highly ordered oligomeric species. Aggregates form with a dense central core of highly ordered oligomer surrounded by a rim of loosely packed oligomers, and occur in multiple hotspots throughout the cell body including the nucleus, Golgi and mitochondria. Mitochondria are a crucial site of aggregation: cardiolipin triggers oligomerization of A53T α-Syn. A53T α-Syn induces over-production of mROS promoting oligomerization of α-Syn. A53T α-Syn oligomerization promotes early opening of mPTP leading to cell death. Note . 100 μM Trolox, 0.5 μM Mito-TEMPO were pre-treated 30 min prior to α-Syn application. Data are presented as mean ± SEM. n = 3 – 5 number of wells. Total number of cells = 180 – 491. All experiments were independently repeated 2 – 3 times. *p<0.05, **p<0.001, ***p<0.0001.

    Techniques Used: Incubation

    cardiolipin  (Echelon Biosciences)


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    Structured Review

    Echelon Biosciences cardiolipin
    Sphingosine binds to <t>cardiolipin.</t> A , agarose-bound cardiolipin or control phosphatidylethanolamine ( PE ) and phosphatidylcholine ( PC ) beads were co-incubated with 1 nmol of SPH at the indicated pH, extensively washed, and extracted, and the amount of bound sphingosine was determined by a sphingosine kinase assay. The solvent octylglucopyranoside (used as a control; not shown) showed no background binding to cardiolipin in the kinase assays. Addition of 0.1% NP-40 removed the residual binding of sphingosine to phosphatidylethanolamine and phosphatidylcholine beads. Shown are the means ± S.D. from four independent experiments and each of the percentage of the added 1 nmol of SPH that was bound to cardiolipin; ***, p < 0.001; ANOVA. B , agarose-bound sphingosine or control beads were co-incubated with 2 nmol of cardiolipin ( CLP ) and extensively washed, and the amount of bound cardiolipin was measured with a fluorescence assay. Sphingosine beads showed no background in the assay. Shown are the means ± S.D. from five experiments each of the percentage of the added 2 nmol of CLP that was bound to cardiolipin. C , membrane fluidity of different liposomes prior to and after addition of sphingosine was measured by a fluorescence assay using the fluorescent probe DPH. The lipid composition is indicated in the figure in mol %. Shown are means ± S.D. from five independent experiments each; ***, p < 0.001, t test.
    Cardiolipin, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 86 stars, based on 1 article reviews
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    cardiolipin - by Bioz Stars, 2023-03
    86/100 stars

    Images

    1) Product Images from "Sphingosine kills bacteria by binding to cardiolipin"

    Article Title: Sphingosine kills bacteria by binding to cardiolipin

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.RA119.012325

    Sphingosine binds to cardiolipin. A , agarose-bound cardiolipin or control phosphatidylethanolamine ( PE ) and phosphatidylcholine ( PC ) beads were co-incubated with 1 nmol of SPH at the indicated pH, extensively washed, and extracted, and the amount of bound sphingosine was determined by a sphingosine kinase assay. The solvent octylglucopyranoside (used as a control; not shown) showed no background binding to cardiolipin in the kinase assays. Addition of 0.1% NP-40 removed the residual binding of sphingosine to phosphatidylethanolamine and phosphatidylcholine beads. Shown are the means ± S.D. from four independent experiments and each of the percentage of the added 1 nmol of SPH that was bound to cardiolipin; ***, p < 0.001; ANOVA. B , agarose-bound sphingosine or control beads were co-incubated with 2 nmol of cardiolipin ( CLP ) and extensively washed, and the amount of bound cardiolipin was measured with a fluorescence assay. Sphingosine beads showed no background in the assay. Shown are the means ± S.D. from five experiments each of the percentage of the added 2 nmol of CLP that was bound to cardiolipin. C , membrane fluidity of different liposomes prior to and after addition of sphingosine was measured by a fluorescence assay using the fluorescent probe DPH. The lipid composition is indicated in the figure in mol %. Shown are means ± S.D. from five independent experiments each; ***, p < 0.001, t test.
    Figure Legend Snippet: Sphingosine binds to cardiolipin. A , agarose-bound cardiolipin or control phosphatidylethanolamine ( PE ) and phosphatidylcholine ( PC ) beads were co-incubated with 1 nmol of SPH at the indicated pH, extensively washed, and extracted, and the amount of bound sphingosine was determined by a sphingosine kinase assay. The solvent octylglucopyranoside (used as a control; not shown) showed no background binding to cardiolipin in the kinase assays. Addition of 0.1% NP-40 removed the residual binding of sphingosine to phosphatidylethanolamine and phosphatidylcholine beads. Shown are the means ± S.D. from four independent experiments and each of the percentage of the added 1 nmol of SPH that was bound to cardiolipin; ***, p < 0.001; ANOVA. B , agarose-bound sphingosine or control beads were co-incubated with 2 nmol of cardiolipin ( CLP ) and extensively washed, and the amount of bound cardiolipin was measured with a fluorescence assay. Sphingosine beads showed no background in the assay. Shown are the means ± S.D. from five experiments each of the percentage of the added 2 nmol of CLP that was bound to cardiolipin. C , membrane fluidity of different liposomes prior to and after addition of sphingosine was measured by a fluorescence assay using the fluorescent probe DPH. The lipid composition is indicated in the figure in mol %. Shown are means ± S.D. from five independent experiments each; ***, p < 0.001, t test.

    Techniques Used: Incubation, Kinase Assay, Binding Assay, Fluorescence

    Sphingosine-mediated killing of bacteria requires cardiolipin. A , each of the 5000 cfu of E. coli strain JW1241-5 (with a deletion of cardiolipin synthase A (Δ clsA ) or the parental WT strain BW25113) was incubated with 5 or 10 μ m SPH or with the corresponding concentration of the solvent OGP or left untreated in PBS (pH 7.0) for 60 min. The bacteria were then washed; aliquots were plated on TSB plates, and cfu were counted after growth overnight. Shown are the means ± S.D. of four independent experiments each; **, p < 0.01; ***, p < 0.001, ANOVA. B , WT or cardiolipin synthase-deficient P. aeruginosa PAO-1 was treated with 10 or 20 μ m sphingosine for 1 h, plated, and grown overnight, and cfu were counted. Displayed are the means ± S.D. of four independent experiments each; *** p < 0.001; ANOVA. C and D , WT mice or CF mice (CF MHH ) were intranasally infected with 5 × 10 7 cfu of PAO-1 or the cardiolipin synthase-deficient mutants of PAO-1 and inhaled with 800 μl of a 125 μ m SPH suspension in 0.9% NaCl 1 h after the infection, and the numbers of bacteria in the lung ( C ) and the sickness score ( D ) were determined 5 h after the infection. Inhalation with the solvent, i.e. 0.0625% OGP in 0.9% NaCl, served as controls. Shown are the means ± S.D. of four independent experiments each; ***, p < 0.001; t test. E , P. aeruginosa 762 (10 5 cfu) was grown and treated with 10 μ m sphingosine for 1 h under hypoxic or normoxic conditions in a BD Gas Pak chamber (BD Biosciences), and bacteria were plated, and cfu were determined after overnight growth. Displayed are the means ± S.D. of four independent experiments each; ***, p < 0.001, ANOVA.
    Figure Legend Snippet: Sphingosine-mediated killing of bacteria requires cardiolipin. A , each of the 5000 cfu of E. coli strain JW1241-5 (with a deletion of cardiolipin synthase A (Δ clsA ) or the parental WT strain BW25113) was incubated with 5 or 10 μ m SPH or with the corresponding concentration of the solvent OGP or left untreated in PBS (pH 7.0) for 60 min. The bacteria were then washed; aliquots were plated on TSB plates, and cfu were counted after growth overnight. Shown are the means ± S.D. of four independent experiments each; **, p < 0.01; ***, p < 0.001, ANOVA. B , WT or cardiolipin synthase-deficient P. aeruginosa PAO-1 was treated with 10 or 20 μ m sphingosine for 1 h, plated, and grown overnight, and cfu were counted. Displayed are the means ± S.D. of four independent experiments each; *** p < 0.001; ANOVA. C and D , WT mice or CF mice (CF MHH ) were intranasally infected with 5 × 10 7 cfu of PAO-1 or the cardiolipin synthase-deficient mutants of PAO-1 and inhaled with 800 μl of a 125 μ m SPH suspension in 0.9% NaCl 1 h after the infection, and the numbers of bacteria in the lung ( C ) and the sickness score ( D ) were determined 5 h after the infection. Inhalation with the solvent, i.e. 0.0625% OGP in 0.9% NaCl, served as controls. Shown are the means ± S.D. of four independent experiments each; ***, p < 0.001; t test. E , P. aeruginosa 762 (10 5 cfu) was grown and treated with 10 μ m sphingosine for 1 h under hypoxic or normoxic conditions in a BD Gas Pak chamber (BD Biosciences), and bacteria were plated, and cfu were determined after overnight growth. Displayed are the means ± S.D. of four independent experiments each; ***, p < 0.001, ANOVA.

    Techniques Used: Incubation, Concentration Assay, Infection

    cardiolipin  (Echelon Biosciences)


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    Echelon Biosciences cardiolipin
    Cardiolipin, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    cardiolipin agarose  (Echelon Biosciences)


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    Echelon Biosciences cardiolipin agarose
    Cardiolipin Agarose, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    synthetic 16 0 ca  (Echelon Biosciences)


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    Echelon Biosciences synthetic 16 0 ca
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    synthetic 16 0 cardiolipin  (Echelon Biosciences)


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    Echelon Biosciences synthetic 16 0 cardiolipin
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    cardiolipin coated beads  (Echelon Biosciences)


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    Echelon Biosciences cardiolipin coated beads
    (A) Levels of PHB1 and SLP-2 were measured in whole cell lysates by immunoblot. HSP60 was used as a loading control. (B) <t>Cardiolipin</t> content was measured in mitochondria isolated from shSCR and shPHB PC12 cells. (C) Cardiolipin binding proteins were pulled down from mitochondrial lysates using cardiolipin coated beads and separated by SDS-PAGE for immunoblotting. Uncoated beads were used to control for non-specific binding and unbound lysate was used as an input control. *p<0.05, n=3 separate experiments. (D) The data are shown as mean±SEM.
    Cardiolipin Coated Beads, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Prohibitin is a positive modulator of mitochondrial function in PC12 cells under oxidative stress"

    Article Title: Prohibitin is a positive modulator of mitochondrial function in PC12 cells under oxidative stress

    Journal: Journal of neurochemistry

    doi: 10.1111/jnc.14472

    (A) Levels of PHB1 and SLP-2 were measured in whole cell lysates by immunoblot. HSP60 was used as a loading control. (B) Cardiolipin content was measured in mitochondria isolated from shSCR and shPHB PC12 cells. (C) Cardiolipin binding proteins were pulled down from mitochondrial lysates using cardiolipin coated beads and separated by SDS-PAGE for immunoblotting. Uncoated beads were used to control for non-specific binding and unbound lysate was used as an input control. *p<0.05, n=3 separate experiments. (D) The data are shown as mean±SEM.
    Figure Legend Snippet: (A) Levels of PHB1 and SLP-2 were measured in whole cell lysates by immunoblot. HSP60 was used as a loading control. (B) Cardiolipin content was measured in mitochondria isolated from shSCR and shPHB PC12 cells. (C) Cardiolipin binding proteins were pulled down from mitochondrial lysates using cardiolipin coated beads and separated by SDS-PAGE for immunoblotting. Uncoated beads were used to control for non-specific binding and unbound lysate was used as an input control. *p<0.05, n=3 separate experiments. (D) The data are shown as mean±SEM.

    Techniques Used: Western Blot, Isolation, Binding Assay, SDS Page

    mitochondrial cardiolipin  (Echelon Biosciences)


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    Echelon Biosciences mitochondrial cardiolipin
    (A) Levels of PHB1 and SLP-2 were measured in whole cell lysates by immunoblot. HSP60 was used as a loading control. (B) <t>Cardiolipin</t> content was measured in mitochondria isolated from shSCR and shPHB PC12 cells. (C) Cardiolipin binding proteins were pulled down from mitochondrial lysates using cardiolipin coated beads and separated by SDS-PAGE for immunoblotting. Uncoated beads were used to control for non-specific binding and unbound lysate was used as an input control. *p<0.05, n=3 separate experiments. (D) The data are shown as mean±SEM.
    Mitochondrial Cardiolipin, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Prohibitin is a positive modulator of mitochondrial function in PC12 cells under oxidative stress"

    Article Title: Prohibitin is a positive modulator of mitochondrial function in PC12 cells under oxidative stress

    Journal: Journal of neurochemistry

    doi: 10.1111/jnc.14472

    (A) Levels of PHB1 and SLP-2 were measured in whole cell lysates by immunoblot. HSP60 was used as a loading control. (B) Cardiolipin content was measured in mitochondria isolated from shSCR and shPHB PC12 cells. (C) Cardiolipin binding proteins were pulled down from mitochondrial lysates using cardiolipin coated beads and separated by SDS-PAGE for immunoblotting. Uncoated beads were used to control for non-specific binding and unbound lysate was used as an input control. *p<0.05, n=3 separate experiments. (D) The data are shown as mean±SEM.
    Figure Legend Snippet: (A) Levels of PHB1 and SLP-2 were measured in whole cell lysates by immunoblot. HSP60 was used as a loading control. (B) Cardiolipin content was measured in mitochondria isolated from shSCR and shPHB PC12 cells. (C) Cardiolipin binding proteins were pulled down from mitochondrial lysates using cardiolipin coated beads and separated by SDS-PAGE for immunoblotting. Uncoated beads were used to control for non-specific binding and unbound lysate was used as an input control. *p<0.05, n=3 separate experiments. (D) The data are shown as mean±SEM.

    Techniques Used: Western Blot, Isolation, Binding Assay, SDS Page

    cardiolipin coated beads  (Echelon Biosciences)


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    Echelon Biosciences cardiolipin coated beads
    (A) Levels of PHB1 and SLP-2 were measured in whole cell lysates by immunoblot. HSP60 was used as a loading control. (B) <t>Cardiolipin</t> content was measured in mitochondria isolated from shSCR and shPHB PC12 cells. (C) Cardiolipin binding proteins were pulled down from mitochondrial lysates using cardiolipin coated beads and separated by SDS-PAGE for immunoblotting. Uncoated beads were used to control for non-specific binding and unbound lysate was used as an input control. *p<0.05, n=3 separate experiments. (D) The data are shown as mean±SEM.
    Cardiolipin Coated Beads, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Prohibitin is a positive modulator of mitochondrial function in PC12 cells under oxidative stress"

    Article Title: Prohibitin is a positive modulator of mitochondrial function in PC12 cells under oxidative stress

    Journal: Journal of neurochemistry

    doi: 10.1111/jnc.14472

    (A) Levels of PHB1 and SLP-2 were measured in whole cell lysates by immunoblot. HSP60 was used as a loading control. (B) Cardiolipin content was measured in mitochondria isolated from shSCR and shPHB PC12 cells. (C) Cardiolipin binding proteins were pulled down from mitochondrial lysates using cardiolipin coated beads and separated by SDS-PAGE for immunoblotting. Uncoated beads were used to control for non-specific binding and unbound lysate was used as an input control. *p<0.05, n=3 separate experiments. (D) The data are shown as mean±SEM.
    Figure Legend Snippet: (A) Levels of PHB1 and SLP-2 were measured in whole cell lysates by immunoblot. HSP60 was used as a loading control. (B) Cardiolipin content was measured in mitochondria isolated from shSCR and shPHB PC12 cells. (C) Cardiolipin binding proteins were pulled down from mitochondrial lysates using cardiolipin coated beads and separated by SDS-PAGE for immunoblotting. Uncoated beads were used to control for non-specific binding and unbound lysate was used as an input control. *p<0.05, n=3 separate experiments. (D) The data are shown as mean±SEM.

    Techniques Used: Western Blot, Isolation, Binding Assay, SDS Page

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    • biotinylated cardiolipin  (Echelon Biosciences)
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    Echelon Biosciences biotinylated cardiolipin
    Related to main . (a) Effect of <t>cardiolipin</t> on far-UV circular diagram (CD) spectra of α-Syn. Phosphate buffer, pH – 7.2, at 25 °C. In presence of cardiolipin, secondary structure of α-Syn changes from the random coil to alpha-helical form measured in pH 7.2 Phosphate buffer at 25 °C. In the absence of cardiolipin vesicles CD spectra was flat except minima at around 198 (black curve), which is characteristic spectra of a random coil. In the presence of CL vesicles at protein to lipid ratio 1:8 (red curve) and 1:16 (blue curve) a significant change occurred in the spectra, with minima at value at 222 nm and 208 nm, which is the characteristic spectra of the alpha-helical form of proteins. (b) Kinetics of amyloid formation by α-Syn (50 µM) in the presence of DMPS (curve 1 – 4) and in the presence of DMPC (curve 5 – 8). Measurements were performed at 30 °C and pH 7.4. Protein concentration was 50 µM and lipid vesicle concentration was 400 µM. ThT fluorescence was excited at 450 nm, and the emission wavelength was 482 nm. (c) Control images for .
    Biotinylated Cardiolipin, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    cardiolipin  (Echelon Biosciences)
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    Echelon Biosciences cardiolipin
    ( A ) Schematic diagrams of the full-length spartin with the MIT and the plant-related senescence domains and the MBP-spartin (421–607) construct encompassing the plant-related senescence domain. Numbers represent the amino acid residues, showing the boundaries of indicated domains. ( B ) Coomassie blue staining of affinity-purified MBP and MBP-spartin (421–607) separated on a polyacrylamide gel. The asterisk (*) indicates a degradation product of MBP-spartin (421–607). Sizes of protein standards are indicated to the left in kDa. ( C ) Detection of MBP-spartin (421–607) binding to <t>cardiolipin</t> but not to phosphatidylethanolamine or phosphatidylcholine in a lipid-protein overlay assay. MBP alone (negative control) did not associate with cardiolipin, phosphatidylethanolamine, or phosphatidylcholine.
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    cardiolipin agarose  (Echelon Biosciences)
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    Echelon Biosciences cardiolipin agarose
    ( A ) Schematic diagrams of the full-length spartin with the MIT and the plant-related senescence domains and the MBP-spartin (421–607) construct encompassing the plant-related senescence domain. Numbers represent the amino acid residues, showing the boundaries of indicated domains. ( B ) Coomassie blue staining of affinity-purified MBP and MBP-spartin (421–607) separated on a polyacrylamide gel. The asterisk (*) indicates a degradation product of MBP-spartin (421–607). Sizes of protein standards are indicated to the left in kDa. ( C ) Detection of MBP-spartin (421–607) binding to <t>cardiolipin</t> but not to phosphatidylethanolamine or phosphatidylcholine in a lipid-protein overlay assay. MBP alone (negative control) did not associate with cardiolipin, phosphatidylethanolamine, or phosphatidylcholine.
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    synthetic 16 0 ca  (Echelon Biosciences)
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    Echelon Biosciences synthetic 16 0 ca
    ( A ) Schematic diagrams of the full-length spartin with the MIT and the plant-related senescence domains and the MBP-spartin (421–607) construct encompassing the plant-related senescence domain. Numbers represent the amino acid residues, showing the boundaries of indicated domains. ( B ) Coomassie blue staining of affinity-purified MBP and MBP-spartin (421–607) separated on a polyacrylamide gel. The asterisk (*) indicates a degradation product of MBP-spartin (421–607). Sizes of protein standards are indicated to the left in kDa. ( C ) Detection of MBP-spartin (421–607) binding to <t>cardiolipin</t> but not to phosphatidylethanolamine or phosphatidylcholine in a lipid-protein overlay assay. MBP alone (negative control) did not associate with cardiolipin, phosphatidylethanolamine, or phosphatidylcholine.
    Synthetic 16 0 Ca, supplied by Echelon Biosciences, 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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    synthetic 16 0 cardiolipin  (Echelon Biosciences)
    91
    Echelon Biosciences synthetic 16 0 cardiolipin
    ( A ) Schematic diagrams of the full-length spartin with the MIT and the plant-related senescence domains and the MBP-spartin (421–607) construct encompassing the plant-related senescence domain. Numbers represent the amino acid residues, showing the boundaries of indicated domains. ( B ) Coomassie blue staining of affinity-purified MBP and MBP-spartin (421–607) separated on a polyacrylamide gel. The asterisk (*) indicates a degradation product of MBP-spartin (421–607). Sizes of protein standards are indicated to the left in kDa. ( C ) Detection of MBP-spartin (421–607) binding to <t>cardiolipin</t> but not to phosphatidylethanolamine or phosphatidylcholine in a lipid-protein overlay assay. MBP alone (negative control) did not associate with cardiolipin, phosphatidylethanolamine, or phosphatidylcholine.
    Synthetic 16 0 Cardiolipin, supplied by Echelon Biosciences, 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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    cardiolipin coated beads  (Echelon Biosciences)
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    Echelon Biosciences cardiolipin coated beads
    (A) Levels of PHB1 and SLP-2 were measured in whole cell lysates by immunoblot. HSP60 was used as a loading control. (B) <t>Cardiolipin</t> content was measured in mitochondria isolated from shSCR and shPHB PC12 cells. (C) Cardiolipin binding proteins were pulled down from mitochondrial lysates using cardiolipin coated beads and separated by SDS-PAGE for immunoblotting. Uncoated beads were used to control for non-specific binding and unbound lysate was used as an input control. *p<0.05, n=3 separate experiments. (D) The data are shown as mean±SEM.
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    mitochondrial cardiolipin  (Echelon Biosciences)
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    Echelon Biosciences mitochondrial cardiolipin
    (A) Levels of PHB1 and SLP-2 were measured in whole cell lysates by immunoblot. HSP60 was used as a loading control. (B) <t>Cardiolipin</t> content was measured in mitochondria isolated from shSCR and shPHB PC12 cells. (C) Cardiolipin binding proteins were pulled down from mitochondrial lysates using cardiolipin coated beads and separated by SDS-PAGE for immunoblotting. Uncoated beads were used to control for non-specific binding and unbound lysate was used as an input control. *p<0.05, n=3 separate experiments. (D) The data are shown as mean±SEM.
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    Related to main . (a) Effect of cardiolipin on far-UV circular diagram (CD) spectra of α-Syn. Phosphate buffer, pH – 7.2, at 25 °C. In presence of cardiolipin, secondary structure of α-Syn changes from the random coil to alpha-helical form measured in pH 7.2 Phosphate buffer at 25 °C. In the absence of cardiolipin vesicles CD spectra was flat except minima at around 198 (black curve), which is characteristic spectra of a random coil. In the presence of CL vesicles at protein to lipid ratio 1:8 (red curve) and 1:16 (blue curve) a significant change occurred in the spectra, with minima at value at 222 nm and 208 nm, which is the characteristic spectra of the alpha-helical form of proteins. (b) Kinetics of amyloid formation by α-Syn (50 µM) in the presence of DMPS (curve 1 – 4) and in the presence of DMPC (curve 5 – 8). Measurements were performed at 30 °C and pH 7.4. Protein concentration was 50 µM and lipid vesicle concentration was 400 µM. ThT fluorescence was excited at 450 nm, and the emission wavelength was 482 nm. (c) Control images for .

    Journal: bioRxiv

    Article Title: Structural conversion of α-synuclein at the mitochondria induces neuronal toxicity

    doi: 10.1101/2022.06.07.494932

    Figure Lengend Snippet: Related to main . (a) Effect of cardiolipin on far-UV circular diagram (CD) spectra of α-Syn. Phosphate buffer, pH – 7.2, at 25 °C. In presence of cardiolipin, secondary structure of α-Syn changes from the random coil to alpha-helical form measured in pH 7.2 Phosphate buffer at 25 °C. In the absence of cardiolipin vesicles CD spectra was flat except minima at around 198 (black curve), which is characteristic spectra of a random coil. In the presence of CL vesicles at protein to lipid ratio 1:8 (red curve) and 1:16 (blue curve) a significant change occurred in the spectra, with minima at value at 222 nm and 208 nm, which is the characteristic spectra of the alpha-helical form of proteins. (b) Kinetics of amyloid formation by α-Syn (50 µM) in the presence of DMPS (curve 1 – 4) and in the presence of DMPC (curve 5 – 8). Measurements were performed at 30 °C and pH 7.4. Protein concentration was 50 µM and lipid vesicle concentration was 400 µM. ThT fluorescence was excited at 450 nm, and the emission wavelength was 482 nm. (c) Control images for .

    Article Snippet: Cardiolipin, 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) (Avanti polar lipids) and biotinylated cardiolipin (Echelon Biosciences) were obtained as a lyophilized powder.

    Techniques: Protein Concentration, Concentration Assay, Fluorescence

    (ai – iv) 50 µM A53T monomer led to a dramatically fast increase in ThT fluorescence in the presence of 40 % or 100 % cardiolipin as compared to WT monomer. (bi) TEM images show that in the presence of cardiolipin, fibrils of α-Syn have different morphology. A total 200 fibrils were analyzed for each group by Image J software . (bii) Quantitative histogram of fibril width shows large distribution of width in the presence of cardiolipin, which is expected for a hierarchical self-assembly model of amyloid formation. (c) TIRFM analysis shows co-localization of cardiolipin and α-Syn fibrils (ThT positive). 0.5 µM α -Syn amyloid fibrils and in the presence of 4 µM cardiolipin vesicles (containing 2 mol % of biotinylated lipid) in the presence of 1 nM streptavidin-AF647 and 5 µµM ThT. Images were recorded for 50 frames from the red channel (AF647 emission) with 641 nm illumination, followed by green channel (ThT emission) with 405 nm illumination. Note . Data are represented as mean ± SEM; n = 3 independent experiments. See also .

    Journal: bioRxiv

    Article Title: Structural conversion of α-synuclein at the mitochondria induces neuronal toxicity

    doi: 10.1101/2022.06.07.494932

    Figure Lengend Snippet: (ai – iv) 50 µM A53T monomer led to a dramatically fast increase in ThT fluorescence in the presence of 40 % or 100 % cardiolipin as compared to WT monomer. (bi) TEM images show that in the presence of cardiolipin, fibrils of α-Syn have different morphology. A total 200 fibrils were analyzed for each group by Image J software . (bii) Quantitative histogram of fibril width shows large distribution of width in the presence of cardiolipin, which is expected for a hierarchical self-assembly model of amyloid formation. (c) TIRFM analysis shows co-localization of cardiolipin and α-Syn fibrils (ThT positive). 0.5 µM α -Syn amyloid fibrils and in the presence of 4 µM cardiolipin vesicles (containing 2 mol % of biotinylated lipid) in the presence of 1 nM streptavidin-AF647 and 5 µµM ThT. Images were recorded for 50 frames from the red channel (AF647 emission) with 641 nm illumination, followed by green channel (ThT emission) with 405 nm illumination. Note . Data are represented as mean ± SEM; n = 3 independent experiments. See also .

    Article Snippet: Cardiolipin, 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) (Avanti polar lipids) and biotinylated cardiolipin (Echelon Biosciences) were obtained as a lyophilized powder.

    Techniques: Fluorescence, Software

    (ai) Representative images showing both FRET intensity and FRET efficiency of A53T are reduced by treatment with Mito-TEMPO. (aii & iii) Mito-TEMPO treated cells show reduced A53T FRET intensity (A53T alone vs Mito-T (Mito-TEMPO): p = 0.024, A53T alone vs Trolox: p = 0.021) and efficiency (A53T alone vs Mito-T: p = 0.011, A53T alone vs Trolox: p = 0.039). (aiv) Application of Trolox to cells reduces FRET intensity signal through reducing uptake of donor (A53T alone vs Trolox: p = 0.020). (bi & ii) Cell death induced by 48-hour incubation of A53T ( p = 0.027), but by WT nor A30P/E46K. (ci & ii) A53T induced cell death was rescued by treatment either with Trolox (A53T alone vs Trolox: p = 0.018) or Mito-TEMPO (A53T alone vs Mito-T: p < 0.0001). (d) Graphical illustration demonstrating how α-Syn monomers form aggregates inside neurons and induce cell toxicity; The intracellular monomeric population begins to self-assemble first into a population of amorphous loosely ordered oligomeric species, and progresses to form highly ordered oligomeric species. Aggregates form with a dense central core of highly ordered oligomer surrounded by a rim of loosely packed oligomers, and occur in multiple hotspots throughout the cell body including the nucleus, Golgi and mitochondria. Mitochondria are a crucial site of aggregation: cardiolipin triggers oligomerization of A53T α-Syn. A53T α-Syn induces over-production of mROS promoting oligomerization of α-Syn. A53T α-Syn oligomerization promotes early opening of mPTP leading to cell death. Note . 100 μM Trolox, 0.5 μM Mito-TEMPO were pre-treated 30 min prior to α-Syn application. Data are presented as mean ± SEM. n = 3 – 5 number of wells. Total number of cells = 180 – 491. All experiments were independently repeated 2 – 3 times. *p<0.05, **p<0.001, ***p<0.0001.

    Journal: bioRxiv

    Article Title: Structural conversion of α-synuclein at the mitochondria induces neuronal toxicity

    doi: 10.1101/2022.06.07.494932

    Figure Lengend Snippet: (ai) Representative images showing both FRET intensity and FRET efficiency of A53T are reduced by treatment with Mito-TEMPO. (aii & iii) Mito-TEMPO treated cells show reduced A53T FRET intensity (A53T alone vs Mito-T (Mito-TEMPO): p = 0.024, A53T alone vs Trolox: p = 0.021) and efficiency (A53T alone vs Mito-T: p = 0.011, A53T alone vs Trolox: p = 0.039). (aiv) Application of Trolox to cells reduces FRET intensity signal through reducing uptake of donor (A53T alone vs Trolox: p = 0.020). (bi & ii) Cell death induced by 48-hour incubation of A53T ( p = 0.027), but by WT nor A30P/E46K. (ci & ii) A53T induced cell death was rescued by treatment either with Trolox (A53T alone vs Trolox: p = 0.018) or Mito-TEMPO (A53T alone vs Mito-T: p < 0.0001). (d) Graphical illustration demonstrating how α-Syn monomers form aggregates inside neurons and induce cell toxicity; The intracellular monomeric population begins to self-assemble first into a population of amorphous loosely ordered oligomeric species, and progresses to form highly ordered oligomeric species. Aggregates form with a dense central core of highly ordered oligomer surrounded by a rim of loosely packed oligomers, and occur in multiple hotspots throughout the cell body including the nucleus, Golgi and mitochondria. Mitochondria are a crucial site of aggregation: cardiolipin triggers oligomerization of A53T α-Syn. A53T α-Syn induces over-production of mROS promoting oligomerization of α-Syn. A53T α-Syn oligomerization promotes early opening of mPTP leading to cell death. Note . 100 μM Trolox, 0.5 μM Mito-TEMPO were pre-treated 30 min prior to α-Syn application. Data are presented as mean ± SEM. n = 3 – 5 number of wells. Total number of cells = 180 – 491. All experiments were independently repeated 2 – 3 times. *p<0.05, **p<0.001, ***p<0.0001.

    Article Snippet: Cardiolipin, 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) (Avanti polar lipids) and biotinylated cardiolipin (Echelon Biosciences) were obtained as a lyophilized powder.

    Techniques: Incubation

    ( A ) Schematic diagrams of the full-length spartin with the MIT and the plant-related senescence domains and the MBP-spartin (421–607) construct encompassing the plant-related senescence domain. Numbers represent the amino acid residues, showing the boundaries of indicated domains. ( B ) Coomassie blue staining of affinity-purified MBP and MBP-spartin (421–607) separated on a polyacrylamide gel. The asterisk (*) indicates a degradation product of MBP-spartin (421–607). Sizes of protein standards are indicated to the left in kDa. ( C ) Detection of MBP-spartin (421–607) binding to cardiolipin but not to phosphatidylethanolamine or phosphatidylcholine in a lipid-protein overlay assay. MBP alone (negative control) did not associate with cardiolipin, phosphatidylethanolamine, or phosphatidylcholine.

    Journal: PLoS ONE

    Article Title: SPG20 Protein Spartin Associates with Cardiolipin via Its Plant-Related Senescence Domain and Regulates Mitochondrial Ca 2+ Homeostasis

    doi: 10.1371/journal.pone.0019290

    Figure Lengend Snippet: ( A ) Schematic diagrams of the full-length spartin with the MIT and the plant-related senescence domains and the MBP-spartin (421–607) construct encompassing the plant-related senescence domain. Numbers represent the amino acid residues, showing the boundaries of indicated domains. ( B ) Coomassie blue staining of affinity-purified MBP and MBP-spartin (421–607) separated on a polyacrylamide gel. The asterisk (*) indicates a degradation product of MBP-spartin (421–607). Sizes of protein standards are indicated to the left in kDa. ( C ) Detection of MBP-spartin (421–607) binding to cardiolipin but not to phosphatidylethanolamine or phosphatidylcholine in a lipid-protein overlay assay. MBP alone (negative control) did not associate with cardiolipin, phosphatidylethanolamine, or phosphatidylcholine.

    Article Snippet: The nitrocellulose membrane with spotted lipids, including cardiolipin and a solvent blank control, were purchased from Echelon Biosciences (Salt Lake City, UT).

    Techniques: Construct, Staining, Affinity Purification, Binding Assay, Overlay Assay, Negative Control

    (A) Levels of PHB1 and SLP-2 were measured in whole cell lysates by immunoblot. HSP60 was used as a loading control. (B) Cardiolipin content was measured in mitochondria isolated from shSCR and shPHB PC12 cells. (C) Cardiolipin binding proteins were pulled down from mitochondrial lysates using cardiolipin coated beads and separated by SDS-PAGE for immunoblotting. Uncoated beads were used to control for non-specific binding and unbound lysate was used as an input control. *p<0.05, n=3 separate experiments. (D) The data are shown as mean±SEM.

    Journal: Journal of neurochemistry

    Article Title: Prohibitin is a positive modulator of mitochondrial function in PC12 cells under oxidative stress

    doi: 10.1111/jnc.14472

    Figure Lengend Snippet: (A) Levels of PHB1 and SLP-2 were measured in whole cell lysates by immunoblot. HSP60 was used as a loading control. (B) Cardiolipin content was measured in mitochondria isolated from shSCR and shPHB PC12 cells. (C) Cardiolipin binding proteins were pulled down from mitochondrial lysates using cardiolipin coated beads and separated by SDS-PAGE for immunoblotting. Uncoated beads were used to control for non-specific binding and unbound lysate was used as an input control. *p<0.05, n=3 separate experiments. (D) The data are shown as mean±SEM.

    Article Snippet: Cardlolipin Binding Assay Mitochondrial cardiolipin-binding proteins were pulled down using cardiolipin coated beads (P-BCLP, Echelon Biosciences, Salt Lake City, UT).

    Techniques: Western Blot, Isolation, Binding Assay, SDS Page

    (A) Levels of PHB1 and SLP-2 were measured in whole cell lysates by immunoblot. HSP60 was used as a loading control. (B) Cardiolipin content was measured in mitochondria isolated from shSCR and shPHB PC12 cells. (C) Cardiolipin binding proteins were pulled down from mitochondrial lysates using cardiolipin coated beads and separated by SDS-PAGE for immunoblotting. Uncoated beads were used to control for non-specific binding and unbound lysate was used as an input control. *p<0.05, n=3 separate experiments. (D) The data are shown as mean±SEM.

    Journal: Journal of neurochemistry

    Article Title: Prohibitin is a positive modulator of mitochondrial function in PC12 cells under oxidative stress

    doi: 10.1111/jnc.14472

    Figure Lengend Snippet: (A) Levels of PHB1 and SLP-2 were measured in whole cell lysates by immunoblot. HSP60 was used as a loading control. (B) Cardiolipin content was measured in mitochondria isolated from shSCR and shPHB PC12 cells. (C) Cardiolipin binding proteins were pulled down from mitochondrial lysates using cardiolipin coated beads and separated by SDS-PAGE for immunoblotting. Uncoated beads were used to control for non-specific binding and unbound lysate was used as an input control. *p<0.05, n=3 separate experiments. (D) The data are shown as mean±SEM.

    Article Snippet: Mitochondrial cardiolipin-binding proteins were pulled down using cardiolipin coated beads (P-BCLP, Echelon Biosciences, Salt Lake City, UT).

    Techniques: Western Blot, Isolation, Binding Assay, SDS Page