ca v 3 1 channel  (Alomone Labs)

Journal: Nature Communications

Article Title: Thalamocortical bursts encode reward contingencies and drive associative learning

doi: 10.1038/s41467-026-76581-6

Figure Lengend Snippet: a Schematic of shRNA viral injection to knock down (KD) Ca V 3.1 in the VPM and POm (left panel), including a scrambled shRNA construct used as a control to account for non-specific effects of viral expression. Representative histological image (middle panel) showing shRNA expression (yellow, shRNA-mOrange) in the thalamus with DAPI counterstain (blue). Higher magnification insets (right panels) show mOrange fluorescence (yellow) and Ca V 3.1 expression (via anti-Ca V 3.1 immunofluorescence) in KD conditions. Each condition included n = 5 animals; histological quantification was performed on n = 18 brain slices from 2 scrambled shRNA control animals and n = 34 brain slices from 4 Ca V 3.1 KD animals. b Proportion of shRNA expression within anatomical boundaries of VPM and POm ( n = 34 brain slices from 4 animals). c Normalized thalamic anti-Ca V 3.1 fluorescence intensity of Ca V 3.1 KD animals ( n = 34 brain slices from 4 animals) compared to scrambled shRNA controls ( n = 18 brain slices from 2 animals) ( p = 1.1514 × 10⁻⁴). d Trial-by-trial learning curves in Ca V 3.1 KD mice compared to scrambled shRNA controls (left panel). Data is shown as cohort mean with SEM as shaded areas. Learning speed quantified as the number of trials to reach expert performance in Ca V 3.1 KD animals and scrambled shRNA controls (right panel, n = 5 mice in each group, p = 0.0317). e Schematic of systemic Z944 or DMSO (control) i.p. injection in mice. f Session-wise performance (d′) in expert animals (dashed grey line) following systemic administration of Z944 (red) compared to DMSO control sessions (grey). Lines represent the cohort means with SEM as shaded areas (4 sessions from n = 6 animals). g Same as in d for Z944-treated animals and DMSO controls ( n = 4 mice in each group, p = 0.0286). h Example reconstruction of a 4-shank Neuropixel recording in POm and VPM. i Overall burstiness (see methods) during 15 min recordings in control-DMSO, Z944 and Ca V 3.1 KD conditions. VPM and POm units were pooled, DMSO and Z944 n = 422 (same units), shRNA, n = 305 units. Statistical comparison was performed using a Kruskal–Wallis test (H(2) = 111.22, p < 0.001). j Top: raster plots of example POm units during DMSO and Z944 (left, middle, same unit) and Ca V 3.1 KD (right). Middle: Burst firing rate for wide (rewarded) and narrow (unrewarded) aperture relative to whisker touch (dashed line). Significant differences ( α = 0.05) are indicated with dashed lines. Only touch-modulated POm and VPM units were selected (same units in DMSO and Z944 conditions, n = 140, Z944, n = 140, shRNA, n = 51). Bottom: Distribution of mean burst indices for the same units as above. Statistical comparisons performed using two-tailed Wilcoxon signed-rank tests: DMSO, p = 1.1 × 10⁻⁵; Z944, p = 0.0506; shRNA, p = 0.223. n.s.: p > 0.05, *: p ≤ 0.05, **: p ≤ 0.01 and ***: p ≤ 0.001; c , d , g : two-tailed Mann–Whitney U -Test, f: two-tailed, paired t-test, i: Kruskal-Wallis with post-tests. j : two-tailed Welch’s t -test with Benjamini-Hochberg correction for multiple comparisons (middle panels); two-tailed Wilcoxon signed-rank test (lower panels). For detailed description of statistics see Supplementary Data . Source data are provided as a file.

Article Snippet: Sections containing the thalamus were processed for immunohistochemistry using an antibody against the Ca V 3.1 channel (Anti-CACNA1G (Ca V 3.1) Antibody, #ACC-021, Alomone Labs, Jerusalem 9104201, Israel), diluted 1: 200 in phosphate buffer, and counterstained with DAPI to visualize cytoarchitecture.

Techniques: shRNA, Injection, Knockdown, Construct, Control, Expressing, Fluorescence, Immunofluorescence, Comparison, Whisker Assay, Two Tailed Test, MANN-WHITNEY

Journal: Journal of Nanobiotechnology

Article Title: Protocatechualdehyde-functionalized BMSC-derived exosomes orchestrate calcium signaling in the immunoinflammatory microenvironment to promote periodontal regeneration

doi: 10.1186/s12951-026-04250-3

Figure Lengend Snippet: PA@BMSC Exo induce osteogenesis in hPDLSCs through activation of calcium signaling pathway. A ) The volcano plot of differentially expressed genes (DEGs) between control and PA@BMSC Exo groups: the up-regulated, unchanged, and down-regulated genes were doted in red, gray, and blue respectively. B ) The heatmap of DEGs. C ) The top twenty enriched signaling pathways following KEGG enrichment analysis for DEGs. D ) GSEA enrichment plots of gene set involved in calcium signaling pathway. E ) A cluster heatmap showed DEGs including CACNA1I (also known as Ca v 3.3) involved in the calcium signaling pathway. F ) Representative western blotting images of Ca v 3.3 protein. G ) Semi-quantitative statistical analysis of Ca v 3.3. Data are shown as mean ± SD ( n = 3, * P < 0.05, ** P < 0.01 and *** P < 0.001)

Article Snippet: After blocking, the membranes were incubated overnight at 4 °C with primary antibodies against the following proteins: TSG101 (1:1000, Abcam), CD9 (1:1000, Abcam), Ca v 3.3 (1:1000, Alomone Labs).

Techniques: Activation Assay, Control, Protein-Protein interactions, Western Blot

Journal: Journal of Nanobiotechnology

Article Title: Protocatechualdehyde-functionalized BMSC-derived exosomes orchestrate calcium signaling in the immunoinflammatory microenvironment to promote periodontal regeneration

doi: 10.1186/s12951-026-04250-3

Figure Lengend Snippet: PA@BMSC Exo upregulates Ca v 3.3 and calcium influx in hPDLSCs and periodontal tissue. A ) Representative immunofluorescence staining in hPDLSCs with Ca v 3.3 (green fluorescence) at day 2. B ) The investigation of intracellular Ca 2+ concentration stained by Fluo-4 AM probe. C ) Representative immunofluorescence staining of the periodontal tissue with Ca v 3.3 (green fluorescence) at day 14 ( n = 3)

Article Snippet: After blocking, the membranes were incubated overnight at 4 °C with primary antibodies against the following proteins: TSG101 (1:1000, Abcam), CD9 (1:1000, Abcam), Ca v 3.3 (1:1000, Alomone Labs).

Techniques: Immunofluorescence, Staining, Fluorescence, Concentration Assay

Journal: Molecular Metabolism

Article Title: α-Parvin promotes glucose uptake and metabolism in skeletal muscle with minimal influence on hepatic insulin sensitivity

doi: 10.1016/j.molmet.2026.102322

Figure Lengend Snippet: α-Parvin regulates skeletal muscle actin remodeling and GLUT4 membrane recruitment. A ) RhoA and Rac1 activity assays were determined in the basal and insulin-stimulated state in gastrocnemius muscle. B) Immunoblotting for total and phosphorylated cofilin was determined in gastrocnemius muscle in basal and insulin-stimulated conditions. The phosphorylated cofilin densitometry was normalized to total cofilin. C ) Sections of gastrocnemius muscle were collected from the mice indicated and fixed in a solution of 10% formalin paraformaldehyde in phosphate buffered saline or snap frozen in isopentane at liquid nitrogen temperature and affixed to cork blocks with OCT. Fixed tissues were embedded in paraffin and sectioned and frozen tissues were cryo-sectioned and mounted. Antibodies against Cav3, GLUT4, and AF-647–phalloidin (F-actin) were used to determine GLUT4 cellular localization. Confocal muscle images were collected with confocal microscopy at super-resolution using a Zeiss LSM 980 confocal microscope equipped with an inverted Axio Observer 7 and Airyscan 2 detector. D ) Airyscan super-resolution images were acquired under identical settings for all groups and images. Acquisition and 2D Airyscan processing of acquired images was done using ZEN Blue software (Carl Zeiss). Line Scan profiles of fluorescence intensity along an annotated line was performed using the plot profile function in Fiji/ImageJ. E ) Gastrocnemius muscle tissue was fractionated to separate cytosolic and plasma membrane fractions for immunoblotting. Purity of fractions were determined by the plasma membrane protein Na/K Atpase. N = 4 to 6 mice per group. Panel A and B, Two-way ANOVA with genotype and insulin as factors was run to test for between group differences. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001, ∗∗∗∗p < 0.0001. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Article Snippet: Antibodies against Cav3 (Santa Cruz #sc55518), GLUT4 (Abcam #ab33780), α-Parvin (Cell Signaling (CST) #4026), HKII (Abcam # ab227198), VDAC1 (MilliporeSigma #SAB5201374) were used and F-actin was visualized using AF-647–phalloidin (Thermo, #A22287).

Techniques: Membrane, Activity Assay, Western Blot, Saline, Confocal Microscopy, Microscopy, Software, Fluorescence, Clinical Proteomics

Journal: Nature Communications

Article Title: Endothelin-3 and T-type Ca 2+ channels drive enteric neural crest cell calcium activity, contractility and migration

doi: 10.1038/s41467-025-68121-5

Figure Lengend Snippet: All experiments in ( a – c ) are performed at E11.5 at the ileo-cecal junction. Error bars are ±SD. a CA change relative to control before drug application for EDTA (2 mM, n = 6), GdCl3 (100 µM, n = 6), 2-APB (100 µM, n = 5), ryanodine (10 µM, n = 5). b CA change for nifedipine (Nif, 10 µM, n = 5), ruthenium red (RuR, 100 µM, n = 6), Z944 at 1 µM ( n = 7), 10 µM ( n = 7), 50 µM ( n = 9), ascorbic acid (AA, 1 mM, n = 13) and SAK3 at 1 µM ( n = 6), 10 µM ( n = 6). c CA change for NPPB (100 µM, n = 11), NFA (50 µM, n = 9) and DIDS (500 µM, n = 5). Two-tailed p -values for (a-c) are calculated from the Student t-test. Sox10 and CaV3.1 ( d ), CaV3.2 ( e ) and CaV3.3 ( f ) IHCs of ENCCs migrating from an intestinal explant on a substrate. All three T-type Ca 2+ channels are expressed by ENCCs, but not by the surrounding mesenchymal cells. The small bright green dots are AF647 µ-beads fluorescing in the same range as the T-type Ca 2+ channel secondary antibody. They were added in the overlying collagen gel for another experiment (see Fig. ).

Article Snippet: After fixation, blocking and permeation, samples were incubated for 1 day in 1:200 mouse Anti-SOX10 and 1:100 rabbit anti CaV3.1 (Alomone Labs #ACC-021) or 1:100 rabbit anti CaV3.2 (Alomone Labs #ACC-025) or 1:100 rabbit anti CaV3.3 (Alomone Labs #ACC-009) for 24 h, washed 3 times, incubated in secondary 1:500 anti-mouse Cy3 and 1:500 anti-rabbit AF647 antibody for another day, washed and imaged.

Techniques: Control, Two Tailed Test