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    synthetic phosphoinositides  (Echelon Biosciences)


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    Echelon Biosciences synthetic phosphoinositides
    (A) Binding of tTG to recycling endosomes. The amounts of purified 125 I-tTG bound at 4°C to recycling endosomes immunoisolated from NIH3T3 cells lacking tTG were determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (B) The role of <t>phosphoinositides</t> in the tTG interaction with recycling endosomes. Binding of 50 nM purified tTG to recycling endosomes was tested in the presence of 100 µM free phosphoinositides. Bound tTG and endosomal Rab11A/Rab11B and transferrin receptor (TfR) were detected by immuno-blotting. The relative amounts of vesicle-bound tTG were quantified and compared to that in the sample without phosphoinositides in four independent experiments. Bars depict means ± SEM, *p<0.05. (C) The putative phospholipid-binding sequence and site within the fourth domain of tTG. (D) Comparative analysis of tTG binding to phosphoinositides. 125 I-tTG binding to synthetic liposomes (PolyPIPosomes™) containing indicated phiosphoinositides was determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (E) Association of tTG with phosphoinositides in cells. tTG was immunoprecipitated from extracts of WI-38 fibroblasts and the immune complexes were probed by immunoblotting for PI(3)P or PI(4)P. (F) The phospholipid-binding site in tTG is required for membrane targeting and externalization of the protein. K598A,K600A,R601A,K602A mutations (m-plbs) were generated within the phospholipid-binding site of tTG. NIH3T3 fibroblasts transfected with wild type tTG (wt) or its mutant deficient in phosphoinositide binding (m-plbs) were left untreated or treated with 10 mM neomycin for 24 h before induction of these proteins for 4 h. The contents of wt and m-plbs tTG in the recycling endosomes and cytosol were defined by immunoblotting ( left panels ). Cell surface and total levels of wt and m-plbs tTG were defined by surface biotinylation, isolation of surface protein fractions, and immunoblotting ( right panels ). The relative contents of wt and m-plbs tTG in the recycling endosomes and on the cell surface were quantified and compared to those for untreated cells expressing wt protein. Shown are representative of three independent experiments. Bars depict means ± SEM, **p<0.005. See also . (G) A proposed mechanism of unconventional tTG secretion. The de novo synthesized intracellular (cytoplasmic) tTG ( hexagons ) does not follow the classical, ER/Golgi-dependent secretion pathway, but is exported via a four-step unconventional secretion process mediated by recycling endosomes ( dotted arrows ). Solid arrows mark the major intracellular recycling route through the PNRC utilized by β1 integrins. See further comments in the text.
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    1) Product Images from "Unconventional Secretion of Tissue Transglutaminase Involves Phospholipid-Dependent Delivery into Recycling Endosomes"

    Article Title: Unconventional Secretion of Tissue Transglutaminase Involves Phospholipid-Dependent Delivery into Recycling Endosomes

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0019414

    (A) Binding of tTG to recycling endosomes. The amounts of purified 125 I-tTG bound at 4°C to recycling endosomes immunoisolated from NIH3T3 cells lacking tTG were determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (B) The role of phosphoinositides in the tTG interaction with recycling endosomes. Binding of 50 nM purified tTG to recycling endosomes was tested in the presence of 100 µM free phosphoinositides. Bound tTG and endosomal Rab11A/Rab11B and transferrin receptor (TfR) were detected by immuno-blotting. The relative amounts of vesicle-bound tTG were quantified and compared to that in the sample without phosphoinositides in four independent experiments. Bars depict means ± SEM, *p<0.05. (C) The putative phospholipid-binding sequence and site within the fourth domain of tTG. (D) Comparative analysis of tTG binding to phosphoinositides. 125 I-tTG binding to synthetic liposomes (PolyPIPosomes™) containing indicated phiosphoinositides was determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (E) Association of tTG with phosphoinositides in cells. tTG was immunoprecipitated from extracts of WI-38 fibroblasts and the immune complexes were probed by immunoblotting for PI(3)P or PI(4)P. (F) The phospholipid-binding site in tTG is required for membrane targeting and externalization of the protein. K598A,K600A,R601A,K602A mutations (m-plbs) were generated within the phospholipid-binding site of tTG. NIH3T3 fibroblasts transfected with wild type tTG (wt) or its mutant deficient in phosphoinositide binding (m-plbs) were left untreated or treated with 10 mM neomycin for 24 h before induction of these proteins for 4 h. The contents of wt and m-plbs tTG in the recycling endosomes and cytosol were defined by immunoblotting ( left panels ). Cell surface and total levels of wt and m-plbs tTG were defined by surface biotinylation, isolation of surface protein fractions, and immunoblotting ( right panels ). The relative contents of wt and m-plbs tTG in the recycling endosomes and on the cell surface were quantified and compared to those for untreated cells expressing wt protein. Shown are representative of three independent experiments. Bars depict means ± SEM, **p<0.005. See also . (G) A proposed mechanism of unconventional tTG secretion. The de novo synthesized intracellular (cytoplasmic) tTG ( hexagons ) does not follow the classical, ER/Golgi-dependent secretion pathway, but is exported via a four-step unconventional secretion process mediated by recycling endosomes ( dotted arrows ). Solid arrows mark the major intracellular recycling route through the PNRC utilized by β1 integrins. See further comments in the text.
    Figure Legend Snippet: (A) Binding of tTG to recycling endosomes. The amounts of purified 125 I-tTG bound at 4°C to recycling endosomes immunoisolated from NIH3T3 cells lacking tTG were determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (B) The role of phosphoinositides in the tTG interaction with recycling endosomes. Binding of 50 nM purified tTG to recycling endosomes was tested in the presence of 100 µM free phosphoinositides. Bound tTG and endosomal Rab11A/Rab11B and transferrin receptor (TfR) were detected by immuno-blotting. The relative amounts of vesicle-bound tTG were quantified and compared to that in the sample without phosphoinositides in four independent experiments. Bars depict means ± SEM, *p<0.05. (C) The putative phospholipid-binding sequence and site within the fourth domain of tTG. (D) Comparative analysis of tTG binding to phosphoinositides. 125 I-tTG binding to synthetic liposomes (PolyPIPosomes™) containing indicated phiosphoinositides was determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (E) Association of tTG with phosphoinositides in cells. tTG was immunoprecipitated from extracts of WI-38 fibroblasts and the immune complexes were probed by immunoblotting for PI(3)P or PI(4)P. (F) The phospholipid-binding site in tTG is required for membrane targeting and externalization of the protein. K598A,K600A,R601A,K602A mutations (m-plbs) were generated within the phospholipid-binding site of tTG. NIH3T3 fibroblasts transfected with wild type tTG (wt) or its mutant deficient in phosphoinositide binding (m-plbs) were left untreated or treated with 10 mM neomycin for 24 h before induction of these proteins for 4 h. The contents of wt and m-plbs tTG in the recycling endosomes and cytosol were defined by immunoblotting ( left panels ). Cell surface and total levels of wt and m-plbs tTG were defined by surface biotinylation, isolation of surface protein fractions, and immunoblotting ( right panels ). The relative contents of wt and m-plbs tTG in the recycling endosomes and on the cell surface were quantified and compared to those for untreated cells expressing wt protein. Shown are representative of three independent experiments. Bars depict means ± SEM, **p<0.005. See also . (G) A proposed mechanism of unconventional tTG secretion. The de novo synthesized intracellular (cytoplasmic) tTG ( hexagons ) does not follow the classical, ER/Golgi-dependent secretion pathway, but is exported via a four-step unconventional secretion process mediated by recycling endosomes ( dotted arrows ). Solid arrows mark the major intracellular recycling route through the PNRC utilized by β1 integrins. See further comments in the text.

    Techniques Used: Binding Assay, Purification, Sequencing, Immunoprecipitation, Western Blot, Generated, Transfection, Mutagenesis, Isolation, Expressing, Synthesized

    synthetic ptdins 4 5 p2 complexes  (Echelon Biosciences)


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    synthetic short chain octanoyl phosphoinositides  (Echelon Biosciences)


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    synthetic phosphoinositides dic16  (Echelon Biosciences)


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    synthetic phosphoinositides dic16  (Echelon Biosciences)


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    long chain di c16 synthetic phosphoinositides  (Echelon Biosciences)


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    synthetic phosphoinositides  (Echelon Biosciences)


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    Lipid-binding properties of the Nwk F-BAR domain. (A–D) Liposome sedimentation assays. Purified Nwk 1-428 was incubated with liposomes of the indicated lipid composition and pelleted. Representative Coomassie staining of supernatant (S) and pellet (P) fractions is shown. –, no liposome controls. Quantification is a result of three independent experiments. Data are represented as mean ± SEM. * p < 0.05, ** p < 0.01, *** p < 0.001. (A) Liposomes composed of 85% phosphatidylcholine (PC), 15% phosphatidylethanolamine (PE), and PS as indicated (with a corresponding decrease in PC). Purified Nwk 1-428 cosediments with liposomes containing high concentrations of PS. (B) Liposomes composed of 70% PC, 15% PE, 10% PS, and 5% of the indicated phosphoinositide. Purified Nwk 1-428 cosedimentation with liposomes is enhanced by <t>phosphoinositides.</t> (C, D) Cosedimentation assays with liposomes composed of 70% PC, 15% PE, 10% PS, and 5% PI(4,5)P 2 . (C) Liposomes were incubated with purified Nwk 1-428 and increasing concentrations of NaCl. (D) Purified Nwk 1-428 , Synd 1-300 , and Mim 1-265 were cosedimented with liposomes of increasing diameter. Representative Coomassie staining shown for Nwk 1-428 . Cosedimentation is not strongly sensitive to liposome size.
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    1) Product Images from "Formation of membrane ridges and scallops by the F-BAR protein Nervous Wreck"

    Article Title: Formation of membrane ridges and scallops by the F-BAR protein Nervous Wreck

    Journal: Molecular Biology of the Cell

    doi: 10.1091/mbc.E13-05-0271

    Lipid-binding properties of the Nwk F-BAR domain. (A–D) Liposome sedimentation assays. Purified Nwk 1-428 was incubated with liposomes of the indicated lipid composition and pelleted. Representative Coomassie staining of supernatant (S) and pellet (P) fractions is shown. –, no liposome controls. Quantification is a result of three independent experiments. Data are represented as mean ± SEM. * p < 0.05, ** p < 0.01, *** p < 0.001. (A) Liposomes composed of 85% phosphatidylcholine (PC), 15% phosphatidylethanolamine (PE), and PS as indicated (with a corresponding decrease in PC). Purified Nwk 1-428 cosediments with liposomes containing high concentrations of PS. (B) Liposomes composed of 70% PC, 15% PE, 10% PS, and 5% of the indicated phosphoinositide. Purified Nwk 1-428 cosedimentation with liposomes is enhanced by phosphoinositides. (C, D) Cosedimentation assays with liposomes composed of 70% PC, 15% PE, 10% PS, and 5% PI(4,5)P 2 . (C) Liposomes were incubated with purified Nwk 1-428 and increasing concentrations of NaCl. (D) Purified Nwk 1-428 , Synd 1-300 , and Mim 1-265 were cosedimented with liposomes of increasing diameter. Representative Coomassie staining shown for Nwk 1-428 . Cosedimentation is not strongly sensitive to liposome size.
    Figure Legend Snippet: Lipid-binding properties of the Nwk F-BAR domain. (A–D) Liposome sedimentation assays. Purified Nwk 1-428 was incubated with liposomes of the indicated lipid composition and pelleted. Representative Coomassie staining of supernatant (S) and pellet (P) fractions is shown. –, no liposome controls. Quantification is a result of three independent experiments. Data are represented as mean ± SEM. * p < 0.05, ** p < 0.01, *** p < 0.001. (A) Liposomes composed of 85% phosphatidylcholine (PC), 15% phosphatidylethanolamine (PE), and PS as indicated (with a corresponding decrease in PC). Purified Nwk 1-428 cosediments with liposomes containing high concentrations of PS. (B) Liposomes composed of 70% PC, 15% PE, 10% PS, and 5% of the indicated phosphoinositide. Purified Nwk 1-428 cosedimentation with liposomes is enhanced by phosphoinositides. (C, D) Cosedimentation assays with liposomes composed of 70% PC, 15% PE, 10% PS, and 5% PI(4,5)P 2 . (C) Liposomes were incubated with purified Nwk 1-428 and increasing concentrations of NaCl. (D) Purified Nwk 1-428 , Synd 1-300 , and Mim 1-265 were cosedimented with liposomes of increasing diameter. Representative Coomassie staining shown for Nwk 1-428 . Cosedimentation is not strongly sensitive to liposome size.

    Techniques Used: Binding Assay, Sedimentation, Purification, Incubation, Staining

    synthetic phosphoinositides  (Echelon Biosciences)


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    (A) Binding of tTG to recycling endosomes. The amounts of purified 125 I-tTG bound at 4°C to recycling endosomes immunoisolated from NIH3T3 cells lacking tTG were determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (B) The role of <t>phosphoinositides</t> in the tTG interaction with recycling endosomes. Binding of 50 nM purified tTG to recycling endosomes was tested in the presence of 100 µM free phosphoinositides. Bound tTG and endosomal Rab11A/Rab11B and transferrin receptor (TfR) were detected by immuno-blotting. The relative amounts of vesicle-bound tTG were quantified and compared to that in the sample without phosphoinositides in four independent experiments. Bars depict means ± SEM, *p<0.05. (C) The putative phospholipid-binding sequence and site within the fourth domain of tTG. (D) Comparative analysis of tTG binding to phosphoinositides. 125 I-tTG binding to synthetic liposomes (PolyPIPosomes™) containing indicated phiosphoinositides was determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (E) Association of tTG with phosphoinositides in cells. tTG was immunoprecipitated from extracts of WI-38 fibroblasts and the immune complexes were probed by immunoblotting for PI(3)P or PI(4)P. (F) The phospholipid-binding site in tTG is required for membrane targeting and externalization of the protein. K598A,K600A,R601A,K602A mutations (m-plbs) were generated within the phospholipid-binding site of tTG. NIH3T3 fibroblasts transfected with wild type tTG (wt) or its mutant deficient in phosphoinositide binding (m-plbs) were left untreated or treated with 10 mM neomycin for 24 h before induction of these proteins for 4 h. The contents of wt and m-plbs tTG in the recycling endosomes and cytosol were defined by immunoblotting ( left panels ). Cell surface and total levels of wt and m-plbs tTG were defined by surface biotinylation, isolation of surface protein fractions, and immunoblotting ( right panels ). The relative contents of wt and m-plbs tTG in the recycling endosomes and on the cell surface were quantified and compared to those for untreated cells expressing wt protein. Shown are representative of three independent experiments. Bars depict means ± SEM, **p<0.005. See also . (G) A proposed mechanism of unconventional tTG secretion. The de novo synthesized intracellular (cytoplasmic) tTG ( hexagons ) does not follow the classical, ER/Golgi-dependent secretion pathway, but is exported via a four-step unconventional secretion process mediated by recycling endosomes ( dotted arrows ). Solid arrows mark the major intracellular recycling route through the PNRC utilized by β1 integrins. See further comments in the text.
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    (A) Binding of tTG to recycling endosomes. The amounts of purified 125 I-tTG bound at 4°C to recycling endosomes immunoisolated from NIH3T3 cells lacking tTG were determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (B) The role of <t>phosphoinositides</t> in the tTG interaction with recycling endosomes. Binding of 50 nM purified tTG to recycling endosomes was tested in the presence of 100 µM free phosphoinositides. Bound tTG and endosomal Rab11A/Rab11B and transferrin receptor (TfR) were detected by immuno-blotting. The relative amounts of vesicle-bound tTG were quantified and compared to that in the sample without phosphoinositides in four independent experiments. Bars depict means ± SEM, *p<0.05. (C) The putative phospholipid-binding sequence and site within the fourth domain of tTG. (D) Comparative analysis of tTG binding to phosphoinositides. 125 I-tTG binding to synthetic liposomes (PolyPIPosomes™) containing indicated phiosphoinositides was determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (E) Association of tTG with phosphoinositides in cells. tTG was immunoprecipitated from extracts of WI-38 fibroblasts and the immune complexes were probed by immunoblotting for PI(3)P or PI(4)P. (F) The phospholipid-binding site in tTG is required for membrane targeting and externalization of the protein. K598A,K600A,R601A,K602A mutations (m-plbs) were generated within the phospholipid-binding site of tTG. NIH3T3 fibroblasts transfected with wild type tTG (wt) or its mutant deficient in phosphoinositide binding (m-plbs) were left untreated or treated with 10 mM neomycin for 24 h before induction of these proteins for 4 h. The contents of wt and m-plbs tTG in the recycling endosomes and cytosol were defined by immunoblotting ( left panels ). Cell surface and total levels of wt and m-plbs tTG were defined by surface biotinylation, isolation of surface protein fractions, and immunoblotting ( right panels ). The relative contents of wt and m-plbs tTG in the recycling endosomes and on the cell surface were quantified and compared to those for untreated cells expressing wt protein. Shown are representative of three independent experiments. Bars depict means ± SEM, **p<0.005. See also . (G) A proposed mechanism of unconventional tTG secretion. The de novo synthesized intracellular (cytoplasmic) tTG ( hexagons ) does not follow the classical, ER/Golgi-dependent secretion pathway, but is exported via a four-step unconventional secretion process mediated by recycling endosomes ( dotted arrows ). Solid arrows mark the major intracellular recycling route through the PNRC utilized by β1 integrins. See further comments in the text.
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    Echelon Biosciences synthetic phosphoinositides dic16
    (A) Binding of tTG to recycling endosomes. The amounts of purified 125 I-tTG bound at 4°C to recycling endosomes immunoisolated from NIH3T3 cells lacking tTG were determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (B) The role of <t>phosphoinositides</t> in the tTG interaction with recycling endosomes. Binding of 50 nM purified tTG to recycling endosomes was tested in the presence of 100 µM free phosphoinositides. Bound tTG and endosomal Rab11A/Rab11B and transferrin receptor (TfR) were detected by immuno-blotting. The relative amounts of vesicle-bound tTG were quantified and compared to that in the sample without phosphoinositides in four independent experiments. Bars depict means ± SEM, *p<0.05. (C) The putative phospholipid-binding sequence and site within the fourth domain of tTG. (D) Comparative analysis of tTG binding to phosphoinositides. 125 I-tTG binding to synthetic liposomes (PolyPIPosomes™) containing indicated phiosphoinositides was determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (E) Association of tTG with phosphoinositides in cells. tTG was immunoprecipitated from extracts of WI-38 fibroblasts and the immune complexes were probed by immunoblotting for PI(3)P or PI(4)P. (F) The phospholipid-binding site in tTG is required for membrane targeting and externalization of the protein. K598A,K600A,R601A,K602A mutations (m-plbs) were generated within the phospholipid-binding site of tTG. NIH3T3 fibroblasts transfected with wild type tTG (wt) or its mutant deficient in phosphoinositide binding (m-plbs) were left untreated or treated with 10 mM neomycin for 24 h before induction of these proteins for 4 h. The contents of wt and m-plbs tTG in the recycling endosomes and cytosol were defined by immunoblotting ( left panels ). Cell surface and total levels of wt and m-plbs tTG were defined by surface biotinylation, isolation of surface protein fractions, and immunoblotting ( right panels ). The relative contents of wt and m-plbs tTG in the recycling endosomes and on the cell surface were quantified and compared to those for untreated cells expressing wt protein. Shown are representative of three independent experiments. Bars depict means ± SEM, **p<0.005. See also . (G) A proposed mechanism of unconventional tTG secretion. The de novo synthesized intracellular (cytoplasmic) tTG ( hexagons ) does not follow the classical, ER/Golgi-dependent secretion pathway, but is exported via a four-step unconventional secretion process mediated by recycling endosomes ( dotted arrows ). Solid arrows mark the major intracellular recycling route through the PNRC utilized by β1 integrins. See further comments in the text.
    Synthetic Phosphoinositides Dic16, 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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    86
    Echelon Biosciences long chain di c16 synthetic phosphoinositides
    (A) Binding of tTG to recycling endosomes. The amounts of purified 125 I-tTG bound at 4°C to recycling endosomes immunoisolated from NIH3T3 cells lacking tTG were determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (B) The role of <t>phosphoinositides</t> in the tTG interaction with recycling endosomes. Binding of 50 nM purified tTG to recycling endosomes was tested in the presence of 100 µM free phosphoinositides. Bound tTG and endosomal Rab11A/Rab11B and transferrin receptor (TfR) were detected by immuno-blotting. The relative amounts of vesicle-bound tTG were quantified and compared to that in the sample without phosphoinositides in four independent experiments. Bars depict means ± SEM, *p<0.05. (C) The putative phospholipid-binding sequence and site within the fourth domain of tTG. (D) Comparative analysis of tTG binding to phosphoinositides. 125 I-tTG binding to synthetic liposomes (PolyPIPosomes™) containing indicated phiosphoinositides was determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (E) Association of tTG with phosphoinositides in cells. tTG was immunoprecipitated from extracts of WI-38 fibroblasts and the immune complexes were probed by immunoblotting for PI(3)P or PI(4)P. (F) The phospholipid-binding site in tTG is required for membrane targeting and externalization of the protein. K598A,K600A,R601A,K602A mutations (m-plbs) were generated within the phospholipid-binding site of tTG. NIH3T3 fibroblasts transfected with wild type tTG (wt) or its mutant deficient in phosphoinositide binding (m-plbs) were left untreated or treated with 10 mM neomycin for 24 h before induction of these proteins for 4 h. The contents of wt and m-plbs tTG in the recycling endosomes and cytosol were defined by immunoblotting ( left panels ). Cell surface and total levels of wt and m-plbs tTG were defined by surface biotinylation, isolation of surface protein fractions, and immunoblotting ( right panels ). The relative contents of wt and m-plbs tTG in the recycling endosomes and on the cell surface were quantified and compared to those for untreated cells expressing wt protein. Shown are representative of three independent experiments. Bars depict means ± SEM, **p<0.005. See also . (G) A proposed mechanism of unconventional tTG secretion. The de novo synthesized intracellular (cytoplasmic) tTG ( hexagons ) does not follow the classical, ER/Golgi-dependent secretion pathway, but is exported via a four-step unconventional secretion process mediated by recycling endosomes ( dotted arrows ). Solid arrows mark the major intracellular recycling route through the PNRC utilized by β1 integrins. See further comments in the text.
    Long Chain Di C16 Synthetic Phosphoinositides, 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
    https://www.bioz.com/result/long chain di c16 synthetic phosphoinositides/product/Echelon Biosciences
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    Image Search Results


    (A) Binding of tTG to recycling endosomes. The amounts of purified 125 I-tTG bound at 4°C to recycling endosomes immunoisolated from NIH3T3 cells lacking tTG were determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (B) The role of phosphoinositides in the tTG interaction with recycling endosomes. Binding of 50 nM purified tTG to recycling endosomes was tested in the presence of 100 µM free phosphoinositides. Bound tTG and endosomal Rab11A/Rab11B and transferrin receptor (TfR) were detected by immuno-blotting. The relative amounts of vesicle-bound tTG were quantified and compared to that in the sample without phosphoinositides in four independent experiments. Bars depict means ± SEM, *p<0.05. (C) The putative phospholipid-binding sequence and site within the fourth domain of tTG. (D) Comparative analysis of tTG binding to phosphoinositides. 125 I-tTG binding to synthetic liposomes (PolyPIPosomes™) containing indicated phiosphoinositides was determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (E) Association of tTG with phosphoinositides in cells. tTG was immunoprecipitated from extracts of WI-38 fibroblasts and the immune complexes were probed by immunoblotting for PI(3)P or PI(4)P. (F) The phospholipid-binding site in tTG is required for membrane targeting and externalization of the protein. K598A,K600A,R601A,K602A mutations (m-plbs) were generated within the phospholipid-binding site of tTG. NIH3T3 fibroblasts transfected with wild type tTG (wt) or its mutant deficient in phosphoinositide binding (m-plbs) were left untreated or treated with 10 mM neomycin for 24 h before induction of these proteins for 4 h. The contents of wt and m-plbs tTG in the recycling endosomes and cytosol were defined by immunoblotting ( left panels ). Cell surface and total levels of wt and m-plbs tTG were defined by surface biotinylation, isolation of surface protein fractions, and immunoblotting ( right panels ). The relative contents of wt and m-plbs tTG in the recycling endosomes and on the cell surface were quantified and compared to those for untreated cells expressing wt protein. Shown are representative of three independent experiments. Bars depict means ± SEM, **p<0.005. See also . (G) A proposed mechanism of unconventional tTG secretion. The de novo synthesized intracellular (cytoplasmic) tTG ( hexagons ) does not follow the classical, ER/Golgi-dependent secretion pathway, but is exported via a four-step unconventional secretion process mediated by recycling endosomes ( dotted arrows ). Solid arrows mark the major intracellular recycling route through the PNRC utilized by β1 integrins. See further comments in the text.

    Journal: PLoS ONE

    Article Title: Unconventional Secretion of Tissue Transglutaminase Involves Phospholipid-Dependent Delivery into Recycling Endosomes

    doi: 10.1371/journal.pone.0019414

    Figure Lengend Snippet: (A) Binding of tTG to recycling endosomes. The amounts of purified 125 I-tTG bound at 4°C to recycling endosomes immunoisolated from NIH3T3 cells lacking tTG were determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (B) The role of phosphoinositides in the tTG interaction with recycling endosomes. Binding of 50 nM purified tTG to recycling endosomes was tested in the presence of 100 µM free phosphoinositides. Bound tTG and endosomal Rab11A/Rab11B and transferrin receptor (TfR) were detected by immuno-blotting. The relative amounts of vesicle-bound tTG were quantified and compared to that in the sample without phosphoinositides in four independent experiments. Bars depict means ± SEM, *p<0.05. (C) The putative phospholipid-binding sequence and site within the fourth domain of tTG. (D) Comparative analysis of tTG binding to phosphoinositides. 125 I-tTG binding to synthetic liposomes (PolyPIPosomes™) containing indicated phiosphoinositides was determined in a gamma counter with all measurements performed in triplicates. Shown are means ± SEM for three independent experiments. (E) Association of tTG with phosphoinositides in cells. tTG was immunoprecipitated from extracts of WI-38 fibroblasts and the immune complexes were probed by immunoblotting for PI(3)P or PI(4)P. (F) The phospholipid-binding site in tTG is required for membrane targeting and externalization of the protein. K598A,K600A,R601A,K602A mutations (m-plbs) were generated within the phospholipid-binding site of tTG. NIH3T3 fibroblasts transfected with wild type tTG (wt) or its mutant deficient in phosphoinositide binding (m-plbs) were left untreated or treated with 10 mM neomycin for 24 h before induction of these proteins for 4 h. The contents of wt and m-plbs tTG in the recycling endosomes and cytosol were defined by immunoblotting ( left panels ). Cell surface and total levels of wt and m-plbs tTG were defined by surface biotinylation, isolation of surface protein fractions, and immunoblotting ( right panels ). The relative contents of wt and m-plbs tTG in the recycling endosomes and on the cell surface were quantified and compared to those for untreated cells expressing wt protein. Shown are representative of three independent experiments. Bars depict means ± SEM, **p<0.005. See also . (G) A proposed mechanism of unconventional tTG secretion. The de novo synthesized intracellular (cytoplasmic) tTG ( hexagons ) does not follow the classical, ER/Golgi-dependent secretion pathway, but is exported via a four-step unconventional secretion process mediated by recycling endosomes ( dotted arrows ). Solid arrows mark the major intracellular recycling route through the PNRC utilized by β1 integrins. See further comments in the text.

    Article Snippet: Membrane lipid strips (#P6002); PIP strips (#P6001), PolyPIPosomes (#YP000; #YP003; #YP004; #YP005; #YP034; #YP035; #YP045; #YP039), and purified synthetic phosphoinositides were from Echelon Biosciences.

    Techniques: Binding Assay, Purification, Sequencing, Immunoprecipitation, Western Blot, Generated, Transfection, Mutagenesis, Isolation, Expressing, Synthesized