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Proteintech cx43

Molecular targets in cardiac remodeling by BiVP and LBBP. Western blotting results of BNP, TGF-β, KCNIP2, SERCA2a, <t>Cx43,</t> ANKRD1 protein expression (A, C, E) in septum and LV lateral walls from NC, DHF, and BiVP and LBBP groups, and relative protein expression (B, D, F). Represented images and statistical data (G) of cardiac fibrosis detected using Masson's staining. † P < .05 between septal and lateral walls. Abbreviations as in

Cx43, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cx43/Connexin+43+Fusion+Protein/pmc13043194-73-18-19
Average 93 stars, based on 12 article reviews

cx43 - by Bioz Stars, 2026-09

93/100 stars

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1) Product Images from "Left bundle branch vs biventricular pacing: mechanistic insights from a canine model"

Article Title: Left bundle branch vs biventricular pacing: mechanistic insights from a canine model

Journal: European Heart Journal

doi: 10.1093/eurheartj/ehaf1093

Molecular targets in cardiac remodeling by BiVP and LBBP. Western blotting results of BNP, TGF-β, KCNIP2, SERCA2a, Cx43, ANKRD1 protein expression (A, C, E) in septum and LV lateral walls from NC, DHF, and BiVP and LBBP groups, and relative protein expression (B, D, F). Represented images and statistical data (G) of cardiac fibrosis detected using Masson's staining. † P < .05 between septal and lateral walls. Abbreviations as in

Figure Legend Snippet: Molecular targets in cardiac remodeling by BiVP and LBBP. Western blotting results of BNP, TGF-β, KCNIP2, SERCA2a, Cx43, ANKRD1 protein expression (A, C, E) in septum and LV lateral walls from NC, DHF, and BiVP and LBBP groups, and relative protein expression (B, D, F). Represented images and statistical data (G) of cardiac fibrosis detected using Masson's staining. † P < .05 between septal and lateral walls. Abbreviations as in

Techniques Used: Western Blot, Expressing, Staining

Overview of the key findings. This study compares the treatment efficacy of LBBP and BiVP, and relating electrocardiographic, echocardiographic and cellular (reverse) remodeling in a canine DHF model. The results show that LBBP restores electrical synchrony (QRSd) to a similar extent as BiVP, while leads to larger LV-GLS improvement than BiVP. Both LBBP and BiVP reverse the protein level of KCNIP2, SERCA2a and Cx43. Moreover, LBBP reverses abnormalities in cytoskeleton-associated proteins, TGF-β signaling, and SERCA2a expression more than BiVP, as well as enhances myocardial energy metabolism via more efficient TCA cycling and ATP production. ANKRD1, ankyrin repeat domain 1; ATP, adenosine triphosphate; BiVP, biventricular pacing; BNP, B-type natriuretic peptide; Cx43, connexin 43; DHF dyssynchronous heart failure; ECG, electrocardiogram; echo, echocardiogram; GLUD1, glutamate dehydrogenase 1; GSNOR S-nitrosoglutathione reductase; KCNIP2, potassium voltage-gated channel interacting protein 2; LBBP, left bundle branch pacing; LV-GLS, left ventricular global longitudinal strain; NC, normal control; SERCA2a, sarcoplasmic/endoplasmic reticulum Ca 2+ ATPase 2a; TCA, tricarboxylic acid; TGF-β, Transforming growth factor-β.

Figure Legend Snippet: Overview of the key findings. This study compares the treatment efficacy of LBBP and BiVP, and relating electrocardiographic, echocardiographic and cellular (reverse) remodeling in a canine DHF model. The results show that LBBP restores electrical synchrony (QRSd) to a similar extent as BiVP, while leads to larger LV-GLS improvement than BiVP. Both LBBP and BiVP reverse the protein level of KCNIP2, SERCA2a and Cx43. Moreover, LBBP reverses abnormalities in cytoskeleton-associated proteins, TGF-β signaling, and SERCA2a expression more than BiVP, as well as enhances myocardial energy metabolism via more efficient TCA cycling and ATP production. ANKRD1, ankyrin repeat domain 1; ATP, adenosine triphosphate; BiVP, biventricular pacing; BNP, B-type natriuretic peptide; Cx43, connexin 43; DHF dyssynchronous heart failure; ECG, electrocardiogram; echo, echocardiogram; GLUD1, glutamate dehydrogenase 1; GSNOR S-nitrosoglutathione reductase; KCNIP2, potassium voltage-gated channel interacting protein 2; LBBP, left bundle branch pacing; LV-GLS, left ventricular global longitudinal strain; NC, normal control; SERCA2a, sarcoplasmic/endoplasmic reticulum Ca 2+ ATPase 2a; TCA, tricarboxylic acid; TGF-β, Transforming growth factor-β.

Techniques Used: Expressing, Control

Milk:

Article Title: Protective effects of artesunate on the neurovascular unit by regulating PDGFRβ signaling in experimental cerebral malaria.
Article Snippet: Cerebral malaria (CM) is a severe manifestation of malaria that significantly impacts the central nervous system, and current therapeutic options are inadequate in addressing the associated neurovascular damage.. This study aimed to investigate the protective effects of artesunate on the neurovascular unit (NVU) in experimental cerebral malaria (ECM) by elucidating the underlying molecular mechanisms and signaling pathways involved.. It demonstrated artesunate significantly reduced parasitemia and improved behavioral and physiological manifestations, and protected the NVU by increasing NeuN-positive neurons and αII-Spectrin and Connexin 43 (CX43) mRNA levels, while decreasing vascular endothelial growth factor α (VEGFα) mRNA and S100β levels.

Incubation:

Article Title: Vericiguat Alleviates Atrial Electrical and Structural Remodeling in Rats with Atrial Fibrillation
Article Snippet: Proteins were then transferred to PVDF membranes (Millipore, USA) at 200 mA for 90 minutes. .. Membranes were blocked with a protein-free rapid sealing solution (PS108, Epizyme) and incubated overnight at 4°C with primary antibodies against: Collagen I (1:500, AF7001, Affinity), CaMKII (1:4000, 12666-2-AP, Proteintech), Cx43 (1:4000, 26980-1-AP, Proteintech), ATG7 (1:1000, ET1610-53, HuaAn), P62 (1:1000, A7785, ABclonal), LC3B (1:2000, ab192890, Abcam), GAPDH (1:30,000, AC001, ABclonal), and Tubulin (1:3000, 11224-1- AP; Proteintech). .. After washing with Tris-buffered saline with Tween 20, membranes were incubated with horseradish peroxidase–conjugated goat anti-rabbit IgG (1:10,000, bs-0295G-HRP, Bioss) for 1 hour at room temperature.

Article Title: Titanium Particles Activate Osteocytic Connexin 43 to Induce Oxidative Stress and Osteoclastogenesis Through the JAK-STAT Pathway.
Article Snippet: Aims: Periprosthetic osteolysis (PPO), a leading cause of aseptic loosening in joint replacement, arose from complex interactions among osteoblasts, osteoclasts, and osteocytes.. Given the pivotal role of connexin 43 (Cx43) in osteocyte communication and bone remodeling, investigating its function was essential for understanding the mechanisms of osteolysis.. Our previous studies showed that titanium (Ti) particles increased Cx43 expression in osteocytes.

Western Blot:

Article Title: Injectable hydrogels with tailored recombinant humanized collagen type I for the repair of damaged hearts by remodeling the myocardial microenvironment
Article Snippet: Bradford assay (BioRad, CA, USA) was used to detect the protein concentration [37]. .. The antibodies used in the western blot assay included VEGF, Ang-1, anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (Cell Signaling Technology, MA, USA), CX43, α-Actinin (Proteintech, Chicago, USA). .. ELISA assay: The cells (5 × 105 cells/well) were incubated with different hydrogels in 6-well plates for 72 h, and cells were collected to detect the concentration of Ang-1, VEGF, CX43, and α-Actinin (Jiangsu Jingmei Biological Technology Co., Ltd.) with ELISA kits.

Article Title: Left bundle branch vs biventricular pacing: mechanistic insights from a canine model
Article Snippet: .. The levels of several key proteins were examined using western blot, including ANKRD1 (Proteintech, 11427-1-AP), BNP (Abclonal, A23996), Cx43 (Proteintech, 26980-1-AP), GSNOR (Proteintech, 66193-1-Ig), GLUD1 (Proteintech, 14299-1-AP), KCNIP2 (Abclonal, A7100), SERCA2a (Abclonal, A0098), TGF-β (Proteintech, 81746-2-RR), and GAPDH (Proteintech, 10494-1-AP). .. For immunofluorescence staining, myocardium sections were incubated overnight at 4°C with primary antibodies, including mouse anti-GSNOR (Proteintech, 66193-1-Ig), and rabbit anti-cardiac troponin T (Proteintech, 15513-1-AP).

Imaging:

Saline:

Immunohistochemical staining:

Article Title: Dioscin suppresses epithelial-mesenchymal transition in gastric cancer by upregulating Cx43 to inhibit the VEGFA/PI3K/Akt/mTOR pathway pathway.
Article Snippet: Background: Connexin 43 (Cx43) and Cx43-gap-junction-intercellular-communications (Cx43-GJs) play an important role in metastasis.. While dioscin exhibits remarkable anticancer activities in various cancers, its effect on Cx43/Cx43-GJs in gastric cancer (GC) remains poorly understood.. Purpose: This study aimed to elucidate the anti-metastatic efficacy and underlying mechanism of the plantderived compound dioscin against gastric cancer cells.

Staining:

Image Search Results

Reduction of AST PGC‐1α–CX43 axis in SPS mice was responsible for the enhanced fear retrieval. (A) Experimental steps of FACS ( n = 3/group); (B) gate strategy and sorting results; (C) representative bands and quantitative data of PGC‐1α and NRF1 proteins; (D) representative bands and quantitative data of hippocampal CX43 protein in the control group and on Days 1, 7, and 14 after SPS modeling; (E) flowchart of the experiment ( n = 6/group); (F and G) freezing time of Con+CSF and Con+GAP27 group mice in the contextual fear test (F) and the cued fear test (G); (H) ELISA for detecting the ATP levels in the hippocampal tissues of the mice in the Con+CSF and Con+GAP27 groups; (I) ELISA for detecting the ATP levels in the hippocampal tissues of the mice in the control and SPS groups. Data are presented as mean and SEM. * p < 0.05, *** p < 0.001 between groups ( t ‐test or Tukey test).

Journal: MedComm

Article Title: Peroxisome Proliferator‑Activated Receptor Gamma Coactivator‑1α Deficiency in Hippocampal Astrocytes Underlies Enhanced Fear Memory Retrieval in Male Posttraumatic Stress Disorder Model Mice

doi: 10.1002/mco2.70671

Figure Lengend Snippet: Reduction of AST PGC‐1α–CX43 axis in SPS mice was responsible for the enhanced fear retrieval. (A) Experimental steps of FACS ( n = 3/group); (B) gate strategy and sorting results; (C) representative bands and quantitative data of PGC‐1α and NRF1 proteins; (D) representative bands and quantitative data of hippocampal CX43 protein in the control group and on Days 1, 7, and 14 after SPS modeling; (E) flowchart of the experiment ( n = 6/group); (F and G) freezing time of Con+CSF and Con+GAP27 group mice in the contextual fear test (F) and the cued fear test (G); (H) ELISA for detecting the ATP levels in the hippocampal tissues of the mice in the Con+CSF and Con+GAP27 groups; (I) ELISA for detecting the ATP levels in the hippocampal tissues of the mice in the control and SPS groups. Data are presented as mean and SEM. * p < 0.05, *** p < 0.001 between groups ( t ‐test or Tukey test).

Article Snippet: Gap 27, a CX43 gap junction blocker (HY‐P0139; MCE), was intracranially administered at 0.5 μL per side with a concentration of 100 μM [ ].

Techniques: Control, Enzyme-linked Immunosorbent Assay

AST PGC‐1α knockdown enhanced fear memory and anxiety‐like behaviors and impaired AST structure. (A) Flowchart of the experiment ( n = 9/group); (B) representative images of virus‐labeled astrocytes; (C) representative bands and quantitative data of PGC‐1α and CX43; (D) freezing of mice in the contextual fear test; (E) freezing of mice in the cued fear test; (F) the percentage of time that mice spent exploring the open arm in the elevated maze test out of the total time; (G and H) the total distance and representative traces of the open field test; (I and J) the results and representative images of the Sholl analysis of astrocytes. The data are presented as mean ± standard error ( n = 3/group). (K) Representative image of S100A10 immunofluorescence staining (scale bar: 50 µm); (L) the percentage of colabeling of S100A10 and PGC‐1α ( n = 3/group). Data are presented as mean and SEM. *p < 0.05, **p < 0.01, ***p < 0.001 between groups ( t ‐test).

Journal: MedComm

doi: 10.1002/mco2.70671

Figure Lengend Snippet: AST PGC‐1α knockdown enhanced fear memory and anxiety‐like behaviors and impaired AST structure. (A) Flowchart of the experiment ( n = 9/group); (B) representative images of virus‐labeled astrocytes; (C) representative bands and quantitative data of PGC‐1α and CX43; (D) freezing of mice in the contextual fear test; (E) freezing of mice in the cued fear test; (F) the percentage of time that mice spent exploring the open arm in the elevated maze test out of the total time; (G and H) the total distance and representative traces of the open field test; (I and J) the results and representative images of the Sholl analysis of astrocytes. The data are presented as mean ± standard error ( n = 3/group). (K) Representative image of S100A10 immunofluorescence staining (scale bar: 50 µm); (L) the percentage of colabeling of S100A10 and PGC‐1α ( n = 3/group). Data are presented as mean and SEM. *p < 0.05, **p < 0.01, ***p < 0.001 between groups ( t ‐test).

Article Snippet: Gap 27, a CX43 gap junction blocker (HY‐P0139; MCE), was intracranially administered at 0.5 μL per side with a concentration of 100 μM [ ].

Techniques: Knockdown, Virus, Labeling, Immunofluorescence, Staining

Activation of hippocampal AST or PGC‐1α reduced fear memory retrieval in SPS mice. (A) Flowchart of experiment 5 ( n = 7/group); (B) representative image of immunofluorescence of hM3Dq‐labeled AST; (C) freezing time of mice in the contextual fear test; (D) freezing time of mice in the cued fear test; (E) percentage of time that mice spent exploring the open arm in the elevated maze test out of the total time; (F) flowchart of the experiment 5 ( n = 6/group); (G) freezing time of mice in the contextual fear memory; (H) freezing time of mice in the cued fear memory; (I) percentage of time that mice spent exploring the open arm in the elevated maze test out of the total time; (J and K) representative bands of GFAP (J) and CX43 (K) along with quantitative data; (L) flowchart of the experiment 6 ( n = 7/group); (M) schematic diagram of the hM3Dq–mCherry/AAV5–PGC‐1α viral injection site and colabeling; (N) freezing time of mice in the contextual fear memory; (O) freezing time of mice in the cued fear memory. Data are presented as mean and SEM. * p < 0.05, ** p < 0.01, *** p < 0.001 between groups ( t ‐test or Tukey test).

Journal: MedComm

doi: 10.1002/mco2.70671

Figure Lengend Snippet: Activation of hippocampal AST or PGC‐1α reduced fear memory retrieval in SPS mice. (A) Flowchart of experiment 5 ( n = 7/group); (B) representative image of immunofluorescence of hM3Dq‐labeled AST; (C) freezing time of mice in the contextual fear test; (D) freezing time of mice in the cued fear test; (E) percentage of time that mice spent exploring the open arm in the elevated maze test out of the total time; (F) flowchart of the experiment 5 ( n = 6/group); (G) freezing time of mice in the contextual fear memory; (H) freezing time of mice in the cued fear memory; (I) percentage of time that mice spent exploring the open arm in the elevated maze test out of the total time; (J and K) representative bands of GFAP (J) and CX43 (K) along with quantitative data; (L) flowchart of the experiment 6 ( n = 7/group); (M) schematic diagram of the hM3Dq–mCherry/AAV5–PGC‐1α viral injection site and colabeling; (N) freezing time of mice in the contextual fear memory; (O) freezing time of mice in the cued fear memory. Data are presented as mean and SEM. * p < 0.05, ** p < 0.01, *** p < 0.001 between groups ( t ‐test or Tukey test).

Article Snippet: Gap 27, a CX43 gap junction blocker (HY‐P0139; MCE), was intracranially administered at 0.5 μL per side with a concentration of 100 μM [ ].

Techniques: Activation Assay, Immunofluorescence, Labeling, Injection

( A ) A schematic representation of the gap junction assembly from connexin 43 (Cx) monomers to hemichannels and to the gap junction plaque between two cells. Intra- (IL) and extracellular (EL) loops are labeled. The transmembrane (TM) helices are numbered 1 to 4. ( B ) One-nm-thick slice through a cryo-ET reconstruction of a cell-cell junction. Areas harboring Cx43 channels (green), 80 S ribosomes (cyan), and microtubules (pink) have been indicated. A mitochondrion has been labeled (M). Scale bars, 100 nm. ( C ) Close-up of the area indicated in (B). Side views of Cx43 GJCs bridging two plasma membranes are indicated with arrowheads. Scale bar, 10 nm. ( D ) Close-up from a different cryo-ET reconstruction showing top views of the Cx43 GJCs. Scale bar, 10 nm. ( E ) Results of template matching for Cx43 GJCs, 80 S ribosomes, and microtubule segments are shown after plotting the templates back onto the cryo-ET tomogram (illustrated with a 1-nm-thick slice in the background). The gap junction is depicted as a transparent surface (green) fitted to the Cx43 channel positions for visual clarity. ( F ) Histogram of pairwise distances between 80 S ribosomes and microtubule segments (MTs) to the Cx43 GJCs, calculated from multiple cryo-ET reconstructions ( n = 26). The 15-nm-wide zone occupied by Cx43 channels is indicated in green. The 22-nm-wide ribosome exclusion zone (REZ) is indicated in gray.

Journal: Science Advances

Article Title: In situ structure of the human gap junction

doi: 10.1126/sciadv.aea4183

Figure Lengend Snippet: ( A ) A schematic representation of the gap junction assembly from connexin 43 (Cx) monomers to hemichannels and to the gap junction plaque between two cells. Intra- (IL) and extracellular (EL) loops are labeled. The transmembrane (TM) helices are numbered 1 to 4. ( B ) One-nm-thick slice through a cryo-ET reconstruction of a cell-cell junction. Areas harboring Cx43 channels (green), 80 S ribosomes (cyan), and microtubules (pink) have been indicated. A mitochondrion has been labeled (M). Scale bars, 100 nm. ( C ) Close-up of the area indicated in (B). Side views of Cx43 GJCs bridging two plasma membranes are indicated with arrowheads. Scale bar, 10 nm. ( D ) Close-up from a different cryo-ET reconstruction showing top views of the Cx43 GJCs. Scale bar, 10 nm. ( E ) Results of template matching for Cx43 GJCs, 80 S ribosomes, and microtubule segments are shown after plotting the templates back onto the cryo-ET tomogram (illustrated with a 1-nm-thick slice in the background). The gap junction is depicted as a transparent surface (green) fitted to the Cx43 channel positions for visual clarity. ( F ) Histogram of pairwise distances between 80 S ribosomes and microtubule segments (MTs) to the Cx43 GJCs, calculated from multiple cryo-ET reconstructions ( n = 26). The 15-nm-wide zone occupied by Cx43 channels is indicated in green. The 22-nm-wide ribosome exclusion zone (REZ) is indicated in gray.

Article Snippet: The cryo-ET map of the Cx43 lattice has been deposited in the Electron Microscopy DataBank (EMDB) with the deposition ID EMD-54024.

Techniques: Labeling, Tomography, Clinical Proteomics

( A ) Slice through a subtomogram average of the Cx43 lattice is shown. One channel is indicated (arrowhead). Scale bar, 10 nm for (A) to (C). ( B ) Slice through the subtomogram average, along the solid line in (A). ( C ) Slice along the dashed line in (A). Channels are indicated in (B) and (C) (arrowheads). ( D ) Isosurface of a subtomogram average. A low-pass filter to 20-Å resolution has been applied to improve the interpretability of the lateral layers. Cx43 atomic models (PDB: 7Z22, residues 17 to 105 and 151 to 235) are shown in green. Two hemichannels forming a full channel are indicated (arrowheads). The convex (+) and concave (−) sides of the lattice are indicated in (B) to (D). ( E ) Density distribution as a function of distance from the lattice midpoint is shown. Density is in arbitrary units. The inner (IL) and outer (OL) leaflets of the two lipid bilayers are marked. The regions corresponding to intracellular density bridging Cx43 hexamers, denoted as lateral-contact layers (LCLs), are labeled. An additional layer of density on the concave side of the gap junction is indicated with an asterisk. ( F to H ) Isosurface renderings are shown from the top (+ to – direction) for the extracellular region (gap), inner leaflet (IL1), and intracellular densities (OL1). ( I ) Rendering of the CG MD simulation setup. The connexins are green, the POPC lipids are blue (head groups in a darker shade), and cholesterol is magenta. The solvent water is rendered as a transparent cube. The inset shows the area indicated. ( J and K ) Number of POPC lipids (J) and cholesterol molecules (K) around the centermost gap junction hemichannel is plotted as a function of the simulation time for both the membranes (+ and – sides).

Journal: Science Advances

Article Title: In situ structure of the human gap junction

doi: 10.1126/sciadv.aea4183

Figure Lengend Snippet: ( A ) Slice through a subtomogram average of the Cx43 lattice is shown. One channel is indicated (arrowhead). Scale bar, 10 nm for (A) to (C). ( B ) Slice through the subtomogram average, along the solid line in (A). ( C ) Slice along the dashed line in (A). Channels are indicated in (B) and (C) (arrowheads). ( D ) Isosurface of a subtomogram average. A low-pass filter to 20-Å resolution has been applied to improve the interpretability of the lateral layers. Cx43 atomic models (PDB: 7Z22, residues 17 to 105 and 151 to 235) are shown in green. Two hemichannels forming a full channel are indicated (arrowheads). The convex (+) and concave (−) sides of the lattice are indicated in (B) to (D). ( E ) Density distribution as a function of distance from the lattice midpoint is shown. Density is in arbitrary units. The inner (IL) and outer (OL) leaflets of the two lipid bilayers are marked. The regions corresponding to intracellular density bridging Cx43 hexamers, denoted as lateral-contact layers (LCLs), are labeled. An additional layer of density on the concave side of the gap junction is indicated with an asterisk. ( F to H ) Isosurface renderings are shown from the top (+ to – direction) for the extracellular region (gap), inner leaflet (IL1), and intracellular densities (OL1). ( I ) Rendering of the CG MD simulation setup. The connexins are green, the POPC lipids are blue (head groups in a darker shade), and cholesterol is magenta. The solvent water is rendered as a transparent cube. The inset shows the area indicated. ( J and K ) Number of POPC lipids (J) and cholesterol molecules (K) around the centermost gap junction hemichannel is plotted as a function of the simulation time for both the membranes (+ and – sides).

Article Snippet: The cryo-ET map of the Cx43 lattice has been deposited in the Electron Microscopy DataBank (EMDB) with the deposition ID EMD-54024.

Techniques: Labeling, Solvent

( A to C ) Isosurface renderings of the cryo-ET subtomogram average at 14-Å resolution segmented with a cylindrical mask are shown as gray transparent surfaces, together with a partial atomic model of the Cx43 channel (PDB: 7Z22, residues 17 to 105 and 151 to 235). The inset indicates the level of the cross sections taken from the middle of the top bilayer (A), the middle of the extracellular loops (B), and the middle of the bottom bilayer (C). The TM helices are numbered 1 to 4 for one Cx monomer in both hemichannels. The convex (+) and concave (−) sides of the gap junction are indicated. ( D ) Close-up of the hemichannel cryo-ET map (this study) and a single-particle cryo-EM structure of the Cx43 hemichannel (EMD-14475), low-pass filtered to the same resolution (14 Å) for comparison. At this resolution, the N-terminal helices (residues 1 to 16, purple) closing the channel are visible in the cryo-EM density. The dashed lines indicate the position of the two membrane leaflets in both structures. ( E and F ) Close-ups of the intracellular areas indicated in the inset (dashed rectangles) are shown. In both, a stalk-like density can be seen, connecting the density below it (stem) and the density above it [lateral contacts layer (LCL)].

Journal: Science Advances

Article Title: In situ structure of the human gap junction

doi: 10.1126/sciadv.aea4183

Figure Lengend Snippet: ( A to C ) Isosurface renderings of the cryo-ET subtomogram average at 14-Å resolution segmented with a cylindrical mask are shown as gray transparent surfaces, together with a partial atomic model of the Cx43 channel (PDB: 7Z22, residues 17 to 105 and 151 to 235). The inset indicates the level of the cross sections taken from the middle of the top bilayer (A), the middle of the extracellular loops (B), and the middle of the bottom bilayer (C). The TM helices are numbered 1 to 4 for one Cx monomer in both hemichannels. The convex (+) and concave (−) sides of the gap junction are indicated. ( D ) Close-up of the hemichannel cryo-ET map (this study) and a single-particle cryo-EM structure of the Cx43 hemichannel (EMD-14475), low-pass filtered to the same resolution (14 Å) for comparison. At this resolution, the N-terminal helices (residues 1 to 16, purple) closing the channel are visible in the cryo-EM density. The dashed lines indicate the position of the two membrane leaflets in both structures. ( E and F ) Close-ups of the intracellular areas indicated in the inset (dashed rectangles) are shown. In both, a stalk-like density can be seen, connecting the density below it (stem) and the density above it [lateral contacts layer (LCL)].

Article Snippet: The cryo-ET map of the Cx43 lattice has been deposited in the Electron Microscopy DataBank (EMDB) with the deposition ID EMD-54024.

Techniques: Tomography, Single Particle, Cryo-EM Sample Prep, Comparison, Membrane

Journal: European Heart Journal

Article Title: Left bundle branch vs biventricular pacing: mechanistic insights from a canine model

doi: 10.1093/eurheartj/ehaf1093

Figure Lengend Snippet: Molecular targets in cardiac remodeling by BiVP and LBBP. Western blotting results of BNP, TGF-β, KCNIP2, SERCA2a, Cx43, ANKRD1 protein expression (A, C, E) in septum and LV lateral walls from NC, DHF, and BiVP and LBBP groups, and relative protein expression (B, D, F). Represented images and statistical data (G) of cardiac fibrosis detected using Masson's staining. † P < .05 between septal and lateral walls. Abbreviations as in

Article Snippet: The levels of several key proteins were examined using western blot, including ANKRD1 (Proteintech, 11427-1-AP), BNP (Abclonal, A23996), Cx43 (Proteintech, 26980-1-AP), GSNOR (Proteintech, 66193-1-Ig), GLUD1 (Proteintech, 14299-1-AP), KCNIP2 (Abclonal, A7100), SERCA2a (Abclonal, A0098), TGF-β (Proteintech, 81746-2-RR), and GAPDH (Proteintech, 10494-1-AP).

Techniques: Western Blot, Expressing, Staining

Journal: European Heart Journal

Article Title: Left bundle branch vs biventricular pacing: mechanistic insights from a canine model

doi: 10.1093/eurheartj/ehaf1093

Figure Lengend Snippet: Overview of the key findings. This study compares the treatment efficacy of LBBP and BiVP, and relating electrocardiographic, echocardiographic and cellular (reverse) remodeling in a canine DHF model. The results show that LBBP restores electrical synchrony (QRSd) to a similar extent as BiVP, while leads to larger LV-GLS improvement than BiVP. Both LBBP and BiVP reverse the protein level of KCNIP2, SERCA2a and Cx43. Moreover, LBBP reverses abnormalities in cytoskeleton-associated proteins, TGF-β signaling, and SERCA2a expression more than BiVP, as well as enhances myocardial energy metabolism via more efficient TCA cycling and ATP production. ANKRD1, ankyrin repeat domain 1; ATP, adenosine triphosphate; BiVP, biventricular pacing; BNP, B-type natriuretic peptide; Cx43, connexin 43; DHF dyssynchronous heart failure; ECG, electrocardiogram; echo, echocardiogram; GLUD1, glutamate dehydrogenase 1; GSNOR S-nitrosoglutathione reductase; KCNIP2, potassium voltage-gated channel interacting protein 2; LBBP, left bundle branch pacing; LV-GLS, left ventricular global longitudinal strain; NC, normal control; SERCA2a, sarcoplasmic/endoplasmic reticulum Ca 2+ ATPase 2a; TCA, tricarboxylic acid; TGF-β, Transforming growth factor-β.

Techniques: Expressing, Control

Review

cx43 (Proteintech)

Structured Review

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1) Product Images from "Left bundle branch vs biventricular pacing: mechanistic insights from a canine model"

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