cacna1c  (Alomone Labs)


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    Structured Review

    Alomone Labs cacna1c
    Alternations of L-type calcium channel transcripts, protein, and action potential in KO smooth muscle. (A) PCR validation of alternatively started and spliced exons of <t>Cacna1c</t> in WT and KO jejunum smooth muscle at KO days 5, 10, and 15. NTC is non template control. Primer sets were designed from variant exons in the regions (e.g. E1-3, forward primer spanning a region on exon 1 and reverse primer on exon 3). (B) qPCR data showing decreased expression of Cacna1c variants starting at exon 1 and exon 2 long and short forms (E1-3, E2L-3, and E2L/S-3) at KO days 5, 10, 15, and 20. E1-3, a region spanning exons 1 and 3; E2L-3, a region spanning exon 2 long (L) form and exon 3; E2L/S-3, a region spanning exon 2 long (L) and short (S) forms and exon 3. (C) Western blot showing decreased levels of CACNA1C protein in Srf KO muscle. (D) Consensus sequence of 5’ splice donor and 3’ splice acceptor sites. (E) A topological map of CACNA1C variants. Amino acid sequence is written in small circles. Four motifs are indicated as I-IV and six transmembrane domains, S1-S6. Four pore regions are also indicated. Colors on amino acid sequence show particular regions and domains: red, missing or inserted peptides from differentially spliced exons; purple, voltage sensors in S4 transmembrane domains; green, start codons found in differentially spliced variants (*, start codons deduced from indicated exons that are differentially spliced; blue, β subunit binding domain; brown, CaM (calmodulin) binding domain; orange, PKA (protein kinase A) phosphorylation site. Alignment of alternatively spliced exons E9/10, E24/25, and E32/33 are shown. (F) Isometric force recordings from antrum and colon of WT and KO mice. Bay K8644 (1 μM) and high potassium (K + ) Krebs (36 mM and 72 mM) were applied to the tissues (indicated by bar and arrows). (G) The graph summarizes the results for 9 antral and 5 colonic WT and KO tissues. The responses to Bay K8644, 36 mM K + , and 72 mM K + were significantly decreased in KO antrums, and the responses to 36 mM K + and 72 mM K + were significantly reduced in KO colons compared to WT. * and ** represent p ≤ 0.05 and p ≤ 0.01 respectively.
    Cacna1c, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    cacna1c - by Bioz Stars, 2022-08
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    Images

    1) Product Images from "Serum response factor regulates smooth muscle contractility via myotonic dystrophy protein kinases and L-type calcium channels"

    Article Title: Serum response factor regulates smooth muscle contractility via myotonic dystrophy protein kinases and L-type calcium channels

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0171262

    Alternations of L-type calcium channel transcripts, protein, and action potential in KO smooth muscle. (A) PCR validation of alternatively started and spliced exons of Cacna1c in WT and KO jejunum smooth muscle at KO days 5, 10, and 15. NTC is non template control. Primer sets were designed from variant exons in the regions (e.g. E1-3, forward primer spanning a region on exon 1 and reverse primer on exon 3). (B) qPCR data showing decreased expression of Cacna1c variants starting at exon 1 and exon 2 long and short forms (E1-3, E2L-3, and E2L/S-3) at KO days 5, 10, 15, and 20. E1-3, a region spanning exons 1 and 3; E2L-3, a region spanning exon 2 long (L) form and exon 3; E2L/S-3, a region spanning exon 2 long (L) and short (S) forms and exon 3. (C) Western blot showing decreased levels of CACNA1C protein in Srf KO muscle. (D) Consensus sequence of 5’ splice donor and 3’ splice acceptor sites. (E) A topological map of CACNA1C variants. Amino acid sequence is written in small circles. Four motifs are indicated as I-IV and six transmembrane domains, S1-S6. Four pore regions are also indicated. Colors on amino acid sequence show particular regions and domains: red, missing or inserted peptides from differentially spliced exons; purple, voltage sensors in S4 transmembrane domains; green, start codons found in differentially spliced variants (*, start codons deduced from indicated exons that are differentially spliced; blue, β subunit binding domain; brown, CaM (calmodulin) binding domain; orange, PKA (protein kinase A) phosphorylation site. Alignment of alternatively spliced exons E9/10, E24/25, and E32/33 are shown. (F) Isometric force recordings from antrum and colon of WT and KO mice. Bay K8644 (1 μM) and high potassium (K + ) Krebs (36 mM and 72 mM) were applied to the tissues (indicated by bar and arrows). (G) The graph summarizes the results for 9 antral and 5 colonic WT and KO tissues. The responses to Bay K8644, 36 mM K + , and 72 mM K + were significantly decreased in KO antrums, and the responses to 36 mM K + and 72 mM K + were significantly reduced in KO colons compared to WT. * and ** represent p ≤ 0.05 and p ≤ 0.01 respectively.
    Figure Legend Snippet: Alternations of L-type calcium channel transcripts, protein, and action potential in KO smooth muscle. (A) PCR validation of alternatively started and spliced exons of Cacna1c in WT and KO jejunum smooth muscle at KO days 5, 10, and 15. NTC is non template control. Primer sets were designed from variant exons in the regions (e.g. E1-3, forward primer spanning a region on exon 1 and reverse primer on exon 3). (B) qPCR data showing decreased expression of Cacna1c variants starting at exon 1 and exon 2 long and short forms (E1-3, E2L-3, and E2L/S-3) at KO days 5, 10, 15, and 20. E1-3, a region spanning exons 1 and 3; E2L-3, a region spanning exon 2 long (L) form and exon 3; E2L/S-3, a region spanning exon 2 long (L) and short (S) forms and exon 3. (C) Western blot showing decreased levels of CACNA1C protein in Srf KO muscle. (D) Consensus sequence of 5’ splice donor and 3’ splice acceptor sites. (E) A topological map of CACNA1C variants. Amino acid sequence is written in small circles. Four motifs are indicated as I-IV and six transmembrane domains, S1-S6. Four pore regions are also indicated. Colors on amino acid sequence show particular regions and domains: red, missing or inserted peptides from differentially spliced exons; purple, voltage sensors in S4 transmembrane domains; green, start codons found in differentially spliced variants (*, start codons deduced from indicated exons that are differentially spliced; blue, β subunit binding domain; brown, CaM (calmodulin) binding domain; orange, PKA (protein kinase A) phosphorylation site. Alignment of alternatively spliced exons E9/10, E24/25, and E32/33 are shown. (F) Isometric force recordings from antrum and colon of WT and KO mice. Bay K8644 (1 μM) and high potassium (K + ) Krebs (36 mM and 72 mM) were applied to the tissues (indicated by bar and arrows). (G) The graph summarizes the results for 9 antral and 5 colonic WT and KO tissues. The responses to Bay K8644, 36 mM K + , and 72 mM K + were significantly decreased in KO antrums, and the responses to 36 mM K + and 72 mM K + were significantly reduced in KO colons compared to WT. * and ** represent p ≤ 0.05 and p ≤ 0.01 respectively.

    Techniques Used: Polymerase Chain Reaction, Variant Assay, Real-time Polymerase Chain Reaction, Expressing, Western Blot, Sequencing, Binding Assay, Chick Chorioallantoic Membrane Assay, Mouse Assay

    Model showing the possible molecular pathways by which SRF regulates contractility via DMPK and CACNA1C in SMC.
    Figure Legend Snippet: Model showing the possible molecular pathways by which SRF regulates contractility via DMPK and CACNA1C in SMC.

    Techniques Used:

    Identification of a predominant subtype and alternative transcriptional variants of L-type calcium channels expressed in SMC. (A) Expression levels of L-type calcium channel subtypes in SMC of jejunum and colon. (B) Expression levels of Cacna1c variants in SMC and tissue of jejunum and colon. (C) A genomic map of Cacna1c variants. Five variable regions (V1-5) are indicated. Exons are numbered 1–48. (D) Magnified view of variable regions showing alternatively started or spliced exons (indicated as exon numbers). Seven exons containing alternative transcriptional start sequence are shown by a star (*). Long (L) and short (S) exons that are differentially started or spliced are indicated.
    Figure Legend Snippet: Identification of a predominant subtype and alternative transcriptional variants of L-type calcium channels expressed in SMC. (A) Expression levels of L-type calcium channel subtypes in SMC of jejunum and colon. (B) Expression levels of Cacna1c variants in SMC and tissue of jejunum and colon. (C) A genomic map of Cacna1c variants. Five variable regions (V1-5) are indicated. Exons are numbered 1–48. (D) Magnified view of variable regions showing alternatively started or spliced exons (indicated as exon numbers). Seven exons containing alternative transcriptional start sequence are shown by a star (*). Long (L) and short (S) exons that are differentially started or spliced are indicated.

    Techniques Used: Expressing, Sequencing

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    Alomone Labs cav1 2
    Effect of colchicine on the protein expression of calcium (Ca 2+ ) regulatory proteins and potassium channel proteins. ( A ) Representative immunoblotting and average data of sarcoplasmic reticulum Ca 2+ ATPase (SERCA2a), <t>Cav1.2,</t> Ca 2+ /calmodulin‐dependent protein kinase II (CaMKII), PLB, Ser16‐ and Thr17‐phosphorylated PLB (PLB‐Ser16 and PLB‐Thr17) from control and colchicine (3 nM)‐treated HL‐1 cells. ( n = 9) ( B ) Representative immunoblotting and average data of RyR type 2, phosphorylation of RyR at S2808 and S2814 (RyR‐2808 and RyR‐2814), the Na + –Ca 2+ exchanger (NCX), Kv1.4, Kv1.5 and Kv4.2 from control and colchicine (3 nM)‐treated HL‐1 cells ( n = 7). * P
    Cav1 2, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Effect of colchicine on the protein expression of calcium (Ca 2+ ) regulatory proteins and potassium channel proteins. ( A ) Representative immunoblotting and average data of sarcoplasmic reticulum Ca 2+ ATPase (SERCA2a), Cav1.2, Ca 2+ /calmodulin‐dependent protein kinase II (CaMKII), PLB, Ser16‐ and Thr17‐phosphorylated PLB (PLB‐Ser16 and PLB‐Thr17) from control and colchicine (3 nM)‐treated HL‐1 cells. ( n = 9) ( B ) Representative immunoblotting and average data of RyR type 2, phosphorylation of RyR at S2808 and S2814 (RyR‐2808 and RyR‐2814), the Na + –Ca 2+ exchanger (NCX), Kv1.4, Kv1.5 and Kv4.2 from control and colchicine (3 nM)‐treated HL‐1 cells ( n = 7). * P

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Colchicine modulates calcium homeostasis and electrical property of HL‐1 cells

    doi: 10.1111/jcmm.12818

    Figure Lengend Snippet: Effect of colchicine on the protein expression of calcium (Ca 2+ ) regulatory proteins and potassium channel proteins. ( A ) Representative immunoblotting and average data of sarcoplasmic reticulum Ca 2+ ATPase (SERCA2a), Cav1.2, Ca 2+ /calmodulin‐dependent protein kinase II (CaMKII), PLB, Ser16‐ and Thr17‐phosphorylated PLB (PLB‐Ser16 and PLB‐Thr17) from control and colchicine (3 nM)‐treated HL‐1 cells. ( n = 9) ( B ) Representative immunoblotting and average data of RyR type 2, phosphorylation of RyR at S2808 and S2814 (RyR‐2808 and RyR‐2814), the Na + –Ca 2+ exchanger (NCX), Kv1.4, Kv1.5 and Kv4.2 from control and colchicine (3 nM)‐treated HL‐1 cells ( n = 7). * P

    Article Snippet: Effects of colchicine on Ca2+ regulatory proteins and Kv channel subunits The expression of SERCA2a and Cav1.2 in the colchicine (3 nM)‐treated HL‐1 cells was lower by 14% and 11% than in the controls.

    Techniques: Expressing

    Treatment effects of metformin on the mRNA and protein levels of Cav1.2 in diabetic mice. (A) Relative levels of CACNA1C with metformin in diabetic mice detected by real-time PCR, n=6. (B) Relative levels of Cav1.2 in the Ctrl group, DM group, and the metformin-treatment group detected by western blot, n=6. (C) Representative confocal images of α-Actinin (left) or CaV1.2 (middle) in the Ctrl group, DM group, and the metformin-treatment group. (D) Relative levels of Cav1.2 in the Ctrl group, DM group, and the metformin-treatment group by immunofluorescences, n=9. Values represent mean ± SEM, *P

    Journal: Frontiers in Pharmacology

    Article Title: Metformin Shortens Prolonged QT Interval in Diabetic Mice by Inhibiting L-Type Calcium Current: A Possible Therapeutic Approach

    doi: 10.3389/fphar.2020.00614

    Figure Lengend Snippet: Treatment effects of metformin on the mRNA and protein levels of Cav1.2 in diabetic mice. (A) Relative levels of CACNA1C with metformin in diabetic mice detected by real-time PCR, n=6. (B) Relative levels of Cav1.2 in the Ctrl group, DM group, and the metformin-treatment group detected by western blot, n=6. (C) Representative confocal images of α-Actinin (left) or CaV1.2 (middle) in the Ctrl group, DM group, and the metformin-treatment group. (D) Relative levels of Cav1.2 in the Ctrl group, DM group, and the metformin-treatment group by immunofluorescences, n=9. Values represent mean ± SEM, *P

    Article Snippet: The molecular mechanism underlying the reduced expression of Cav1.2 with metformin treatment may involve the restoration of the physicochemical properties of the protein.

    Techniques: Mouse Assay, Real-time Polymerase Chain Reaction, Western Blot

    Treatment effects of metformin on the mRNA and protein levels of Cav1.2 in primary cultured neonatal mice cardiomyocytes. (A) Relative levels of CACNA1C with metformin of primary cardiomyocytes in NC group, HG group and metformin-treatment group detected by real-time PCR, n=6. (B) Relative levels of Cav1.2 of primary cardiomyocytes in NC group, HG group and metformin-treatment group detected by western blot, n=6. (C) Representative confocal images of α-Actinin (left) or CaV1.2 (middle) of primary cardiomyocytes in NC group, HG group and metformin-treatment group. (D) Relative levels of Cav1.2 of primary cardiomyocytes in NC group, HG group and metformin-treatment group detected by immunofluorescences, n=9. Values represent mean ± SEM, *P

    Journal: Frontiers in Pharmacology

    Article Title: Metformin Shortens Prolonged QT Interval in Diabetic Mice by Inhibiting L-Type Calcium Current: A Possible Therapeutic Approach

    doi: 10.3389/fphar.2020.00614

    Figure Lengend Snippet: Treatment effects of metformin on the mRNA and protein levels of Cav1.2 in primary cultured neonatal mice cardiomyocytes. (A) Relative levels of CACNA1C with metformin of primary cardiomyocytes in NC group, HG group and metformin-treatment group detected by real-time PCR, n=6. (B) Relative levels of Cav1.2 of primary cardiomyocytes in NC group, HG group and metformin-treatment group detected by western blot, n=6. (C) Representative confocal images of α-Actinin (left) or CaV1.2 (middle) of primary cardiomyocytes in NC group, HG group and metformin-treatment group. (D) Relative levels of Cav1.2 of primary cardiomyocytes in NC group, HG group and metformin-treatment group detected by immunofluorescences, n=9. Values represent mean ± SEM, *P

    Article Snippet: The molecular mechanism underlying the reduced expression of Cav1.2 with metformin treatment may involve the restoration of the physicochemical properties of the protein.

    Techniques: Cell Culture, Mouse Assay, Real-time Polymerase Chain Reaction, Western Blot