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pi 4 5 p 2 dic8 phosphatidylinositol 4 5 bisphosphate dic8 echelon bioscience  (Echelon Biosciences)


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    Structured Review

    Echelon Biosciences pi 4 5 p 2 dic8 phosphatidylinositol 4 5 bisphosphate dic8 echelon bioscience
    PIP 2 enhances HsNCX1 activity. (A) Representative outward currents recorded from oocytes expressing the human NCX1 before and after application of long-chain brain PIP 2 . Currents were activated by replacing cytosolic Cs + with Na + . Application of 10 µM brain PIP 2 enhanced HsNCX1 current and abolished the Na + -dependent inactivation irreversibly. Perfusion time of PIP 2 is indicated above traces while lines below traces indicate solution exchange. Arrows mark the peak and steady currents used to measure the fold of increase upon PIP 2 application. The fold of current increase was calculated by comparing the peak or steady-state current before and after PIP 2 application. (B) Representative outward currents recorded before and after application of short-chain PIP 2 <t>diC8</t> (10 µM). PIP 2 diC8 was perfused from the cytosolic side before HsNCX1 activation (in the presence of Cs + for 30 s) and during transport (in the presence of Na + ). Both peak and steady-state currents of HsNCX1 are enhanced by PIP 2 diC8 and the effect is reversible. The Na + -dependent inactivation remains in the presence of PIP 2 diC8.
    Pi 4 5 P 2 Dic8 Phosphatidylinositol 4 5 Bisphosphate Dic8 Echelon Bioscience, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Structural mechanisms of PIP 2 activation and SEA0400 inhibition in human cardiac sodium-calcium exchanger NCX1"

    Article Title: Structural mechanisms of PIP 2 activation and SEA0400 inhibition in human cardiac sodium-calcium exchanger NCX1

    Journal: bioRxiv

    doi: 10.1101/2024.12.05.627058

    PIP 2 enhances HsNCX1 activity. (A) Representative outward currents recorded from oocytes expressing the human NCX1 before and after application of long-chain brain PIP 2 . Currents were activated by replacing cytosolic Cs + with Na + . Application of 10 µM brain PIP 2 enhanced HsNCX1 current and abolished the Na + -dependent inactivation irreversibly. Perfusion time of PIP 2 is indicated above traces while lines below traces indicate solution exchange. Arrows mark the peak and steady currents used to measure the fold of increase upon PIP 2 application. The fold of current increase was calculated by comparing the peak or steady-state current before and after PIP 2 application. (B) Representative outward currents recorded before and after application of short-chain PIP 2 diC8 (10 µM). PIP 2 diC8 was perfused from the cytosolic side before HsNCX1 activation (in the presence of Cs + for 30 s) and during transport (in the presence of Na + ). Both peak and steady-state currents of HsNCX1 are enhanced by PIP 2 diC8 and the effect is reversible. The Na + -dependent inactivation remains in the presence of PIP 2 diC8.
    Figure Legend Snippet: PIP 2 enhances HsNCX1 activity. (A) Representative outward currents recorded from oocytes expressing the human NCX1 before and after application of long-chain brain PIP 2 . Currents were activated by replacing cytosolic Cs + with Na + . Application of 10 µM brain PIP 2 enhanced HsNCX1 current and abolished the Na + -dependent inactivation irreversibly. Perfusion time of PIP 2 is indicated above traces while lines below traces indicate solution exchange. Arrows mark the peak and steady currents used to measure the fold of increase upon PIP 2 application. The fold of current increase was calculated by comparing the peak or steady-state current before and after PIP 2 application. (B) Representative outward currents recorded before and after application of short-chain PIP 2 diC8 (10 µM). PIP 2 diC8 was perfused from the cytosolic side before HsNCX1 activation (in the presence of Cs + for 30 s) and during transport (in the presence of Na + ). Both peak and steady-state currents of HsNCX1 are enhanced by PIP 2 diC8 and the effect is reversible. The Na + -dependent inactivation remains in the presence of PIP 2 diC8.

    Techniques Used: Activity Assay, Expressing, Activation Assay

    PIP 2 binding in NCX1. (A) Structure of the TM and β-hub regions of PIP 2 diC8-bound NCX1 with a zoomed-in view of the lipid binding site. (B) Structural comparison between apo (grey) and PIP 2 diC8-bound (color) NCX1. (C) Zoomed-in view of the structural comparison (boxed area in (B)). The two major conformational changes occur in the boxed regions with the two areas SEA0400 binding site and the schematic diagram detailing the interactions between NCX1 residues and SEA0400. (D) Zoomed-in views of the two conformational changes between apo (left in grey) and PIP 2 diC8-bound (right in color) state. Top: conformational change 1 at the C-terminus of TM5. Bottom: conformational change 2 at the interface between XIP and CBD2.
    Figure Legend Snippet: PIP 2 binding in NCX1. (A) Structure of the TM and β-hub regions of PIP 2 diC8-bound NCX1 with a zoomed-in view of the lipid binding site. (B) Structural comparison between apo (grey) and PIP 2 diC8-bound (color) NCX1. (C) Zoomed-in view of the structural comparison (boxed area in (B)). The two major conformational changes occur in the boxed regions with the two areas SEA0400 binding site and the schematic diagram detailing the interactions between NCX1 residues and SEA0400. (D) Zoomed-in views of the two conformational changes between apo (left in grey) and PIP 2 diC8-bound (right in color) state. Top: conformational change 1 at the C-terminus of TM5. Bottom: conformational change 2 at the interface between XIP and CBD2.

    Techniques Used: Binding Assay, Comparison



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    PIP 2 enhances HsNCX1 activity. (A) Representative outward currents recorded from oocytes expressing the human NCX1 before and after application of long-chain brain PIP 2 . Currents were activated by replacing cytosolic Cs + with Na + . Application of 10 µM brain PIP 2 enhanced HsNCX1 current and abolished the Na + -dependent inactivation irreversibly. Perfusion time of PIP 2 is indicated above traces while lines below traces indicate solution exchange. Arrows mark the peak and steady currents used to measure the fold of increase upon PIP 2 application. The fold of current increase was calculated by comparing the peak or steady-state current before and after PIP 2 application. (B) Representative outward currents recorded before and after application of short-chain PIP 2 <t>diC8</t> (10 µM). PIP 2 diC8 was perfused from the cytosolic side before HsNCX1 activation (in the presence of Cs + for 30 s) and during transport (in the presence of Na + ). Both peak and steady-state currents of HsNCX1 are enhanced by PIP 2 diC8 and the effect is reversible. The Na + -dependent inactivation remains in the presence of PIP 2 diC8.
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    Image Search Results


    PIP 2 enhances HsNCX1 activity. (A) Representative outward currents recorded from oocytes expressing the human NCX1 before and after application of long-chain brain PIP 2 . Currents were activated by replacing cytosolic Cs + with Na + . Application of 10 µM brain PIP 2 enhanced HsNCX1 current and abolished the Na + -dependent inactivation irreversibly. Perfusion time of PIP 2 is indicated above traces while lines below traces indicate solution exchange. Arrows mark the peak and steady currents used to measure the fold of increase upon PIP 2 application. The fold of current increase was calculated by comparing the peak or steady-state current before and after PIP 2 application. (B) Representative outward currents recorded before and after application of short-chain PIP 2 diC8 (10 µM). PIP 2 diC8 was perfused from the cytosolic side before HsNCX1 activation (in the presence of Cs + for 30 s) and during transport (in the presence of Na + ). Both peak and steady-state currents of HsNCX1 are enhanced by PIP 2 diC8 and the effect is reversible. The Na + -dependent inactivation remains in the presence of PIP 2 diC8.

    Journal: bioRxiv

    Article Title: Structural mechanisms of PIP 2 activation and SEA0400 inhibition in human cardiac sodium-calcium exchanger NCX1

    doi: 10.1101/2024.12.05.627058

    Figure Lengend Snippet: PIP 2 enhances HsNCX1 activity. (A) Representative outward currents recorded from oocytes expressing the human NCX1 before and after application of long-chain brain PIP 2 . Currents were activated by replacing cytosolic Cs + with Na + . Application of 10 µM brain PIP 2 enhanced HsNCX1 current and abolished the Na + -dependent inactivation irreversibly. Perfusion time of PIP 2 is indicated above traces while lines below traces indicate solution exchange. Arrows mark the peak and steady currents used to measure the fold of increase upon PIP 2 application. The fold of current increase was calculated by comparing the peak or steady-state current before and after PIP 2 application. (B) Representative outward currents recorded before and after application of short-chain PIP 2 diC8 (10 µM). PIP 2 diC8 was perfused from the cytosolic side before HsNCX1 activation (in the presence of Cs + for 30 s) and during transport (in the presence of Na + ). Both peak and steady-state currents of HsNCX1 are enhanced by PIP 2 diC8 and the effect is reversible. The Na + -dependent inactivation remains in the presence of PIP 2 diC8.

    Article Snippet: PI(4,5)P 2 diC8 (Phosphatidylinositol 4,5-bisphosphate diC8, Echelon Bioscience) and brain PI(4,5)P 2 (L-α-phosphatidylinositol-4,5-bisphosphate, Brain, Porcine, Avanti Polar Lipids) were dissolved in water and kept as stock at -20 °C.

    Techniques: Activity Assay, Expressing, Activation Assay

    PIP 2 binding in NCX1. (A) Structure of the TM and β-hub regions of PIP 2 diC8-bound NCX1 with a zoomed-in view of the lipid binding site. (B) Structural comparison between apo (grey) and PIP 2 diC8-bound (color) NCX1. (C) Zoomed-in view of the structural comparison (boxed area in (B)). The two major conformational changes occur in the boxed regions with the two areas SEA0400 binding site and the schematic diagram detailing the interactions between NCX1 residues and SEA0400. (D) Zoomed-in views of the two conformational changes between apo (left in grey) and PIP 2 diC8-bound (right in color) state. Top: conformational change 1 at the C-terminus of TM5. Bottom: conformational change 2 at the interface between XIP and CBD2.

    Journal: bioRxiv

    Article Title: Structural mechanisms of PIP 2 activation and SEA0400 inhibition in human cardiac sodium-calcium exchanger NCX1

    doi: 10.1101/2024.12.05.627058

    Figure Lengend Snippet: PIP 2 binding in NCX1. (A) Structure of the TM and β-hub regions of PIP 2 diC8-bound NCX1 with a zoomed-in view of the lipid binding site. (B) Structural comparison between apo (grey) and PIP 2 diC8-bound (color) NCX1. (C) Zoomed-in view of the structural comparison (boxed area in (B)). The two major conformational changes occur in the boxed regions with the two areas SEA0400 binding site and the schematic diagram detailing the interactions between NCX1 residues and SEA0400. (D) Zoomed-in views of the two conformational changes between apo (left in grey) and PIP 2 diC8-bound (right in color) state. Top: conformational change 1 at the C-terminus of TM5. Bottom: conformational change 2 at the interface between XIP and CBD2.

    Article Snippet: PI(4,5)P 2 diC8 (Phosphatidylinositol 4,5-bisphosphate diC8, Echelon Bioscience) and brain PI(4,5)P 2 (L-α-phosphatidylinositol-4,5-bisphosphate, Brain, Porcine, Avanti Polar Lipids) were dissolved in water and kept as stock at -20 °C.

    Techniques: Binding Assay, Comparison