Structured Review

Millipore ryr3
RyR1 but not RyR2 or <t>RyR3</t> are expressed in fast twitch skeletal muscle. Immunoblots of extracts of Tibialis anterior muscles with antibodies to RyR1, RyR2, and RyR3. Only anti-RyR1 shows a strong band at ∼550 kDa.
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1) Product Images from "Elevated Ca2+ at the triad junction underlies dysregulation of Ca2+ signaling in dysferlin-null skeletal muscle"

Article Title: Elevated Ca2+ at the triad junction underlies dysregulation of Ca2+ signaling in dysferlin-null skeletal muscle

Journal: Frontiers in Physiology

doi: 10.3389/fphys.2022.1032447

RyR1 but not RyR2 or RyR3 are expressed in fast twitch skeletal muscle. Immunoblots of extracts of Tibialis anterior muscles with antibodies to RyR1, RyR2, and RyR3. Only anti-RyR1 shows a strong band at ∼550 kDa.
Figure Legend Snippet: RyR1 but not RyR2 or RyR3 are expressed in fast twitch skeletal muscle. Immunoblots of extracts of Tibialis anterior muscles with antibodies to RyR1, RyR2, and RyR3. Only anti-RyR1 shows a strong band at ∼550 kDa.

Techniques Used: Western Blot

2) Product Images from "Elevated Ca2+ at the triad junction underlies dysregulation of Ca2+ signaling in dysferlin-null skeletal muscle"

Article Title: Elevated Ca2+ at the triad junction underlies dysregulation of Ca2+ signaling in dysferlin-null skeletal muscle

Journal: Frontiers in Physiology

doi: 10.3389/fphys.2022.1032447

RyR1 but not RyR2 or RyR3 are expressed in fast twitch skeletal muscle. Immunoblots of extracts of Tibialis anterior muscles with antibodies to RyR1, RyR2, and RyR3. Only anti-RyR1 shows a strong band at ∼550 kDa.
Figure Legend Snippet: RyR1 but not RyR2 or RyR3 are expressed in fast twitch skeletal muscle. Immunoblots of extracts of Tibialis anterior muscles with antibodies to RyR1, RyR2, and RyR3. Only anti-RyR1 shows a strong band at ∼550 kDa.

Techniques Used: Western Blot

3) Product Images from "Elevated Ca2+ at the triad junction underlies dysregulation of Ca2+ signaling in dysferlin-null skeletal muscle"

Article Title: Elevated Ca2+ at the triad junction underlies dysregulation of Ca2+ signaling in dysferlin-null skeletal muscle

Journal: Frontiers in Physiology

doi: 10.3389/fphys.2022.1032447

RyR1 but not RyR2 or RyR3 are expressed in fast twitch skeletal muscle. Immunoblots of extracts of Tibialis anterior muscles with antibodies to RyR1, RyR2, and RyR3. Only anti-RyR1 shows a strong band at ∼550 kDa.
Figure Legend Snippet: RyR1 but not RyR2 or RyR3 are expressed in fast twitch skeletal muscle. Immunoblots of extracts of Tibialis anterior muscles with antibodies to RyR1, RyR2, and RyR3. Only anti-RyR1 shows a strong band at ∼550 kDa.

Techniques Used: Western Blot

4) Product Images from "Elevated Ca2+ at the triad junction underlies dysregulation of Ca2+ signaling in dysferlin-null skeletal muscle"

Article Title: Elevated Ca2+ at the triad junction underlies dysregulation of Ca2+ signaling in dysferlin-null skeletal muscle

Journal: Frontiers in Physiology

doi: 10.3389/fphys.2022.1032447

RyR1 but not RyR2 or RyR3 are expressed in fast twitch skeletal muscle. Immunoblots of extracts of Tibialis anterior muscles with antibodies to RyR1, RyR2, and RyR3. Only anti-RyR1 shows a strong band at ∼550 kDa.
Figure Legend Snippet: RyR1 but not RyR2 or RyR3 are expressed in fast twitch skeletal muscle. Immunoblots of extracts of Tibialis anterior muscles with antibodies to RyR1, RyR2, and RyR3. Only anti-RyR1 shows a strong band at ∼550 kDa.

Techniques Used: Western Blot

5) Product Images from "Elevated Ca2+ at the triad junction underlies dysregulation of Ca2+ signaling in dysferlin-null skeletal muscle"

Article Title: Elevated Ca2+ at the triad junction underlies dysregulation of Ca2+ signaling in dysferlin-null skeletal muscle

Journal: Frontiers in Physiology

doi: 10.3389/fphys.2022.1032447

RyR1 but not RyR2 or RyR3 are expressed in fast twitch skeletal muscle. Immunoblots of extracts of Tibialis anterior muscles with antibodies to RyR1, RyR2, and RyR3. Only anti-RyR1 shows a strong band at ∼550 kDa.
Figure Legend Snippet: RyR1 but not RyR2 or RyR3 are expressed in fast twitch skeletal muscle. Immunoblots of extracts of Tibialis anterior muscles with antibodies to RyR1, RyR2, and RyR3. Only anti-RyR1 shows a strong band at ∼550 kDa.

Techniques Used: Western Blot

6) Product Images from "Pregnancy increases Ca2+ sparks/STOCs and reduces uterine arterial myogenic tone"

Article Title: Pregnancy increases Ca2+ sparks/STOCs and reduces uterine arterial myogenic tone

Journal: Hypertension (Dallas, Tex. : 1979)

doi: 10.1161/HYPERTENSIONAHA.118.12484

Pregnancy upregulates ryanodine receptors in uterine arteries. Ryanodine receptor type 1 (RyR1), type 2 (RyR2) and type 3 (RyR3) mRNA ( A ) and protein ( B ) abundance in uterine arteries of nonpregnant (UA NP ) and pregnant (UA P ) sheep were determined with real-time RT-PCR and Western blotting. Data are means ± SEM from 4–5 animals of each group. *P
Figure Legend Snippet: Pregnancy upregulates ryanodine receptors in uterine arteries. Ryanodine receptor type 1 (RyR1), type 2 (RyR2) and type 3 (RyR3) mRNA ( A ) and protein ( B ) abundance in uterine arteries of nonpregnant (UA NP ) and pregnant (UA P ) sheep were determined with real-time RT-PCR and Western blotting. Data are means ± SEM from 4–5 animals of each group. *P

Techniques Used: Quantitative RT-PCR, Western Blot

7) Product Images from "Control of neuronal ryanodine receptor-mediated calcium signaling by calsenilin"

Article Title: Control of neuronal ryanodine receptor-mediated calcium signaling by calsenilin

Journal: Molecular neurobiology

doi: 10.1007/s12035-018-1080-2

Calsenilin and RyR are co-localized and have a direct protein-protein interaction in neuronal tissue Calsenilin (green) and A) RyR2 or RyR3 (red) immunoreactivity in E18 primary cultured cortical neurons B) RyR2 (red) expression in the dentate gyrus and cortical layer VI show a perinuclear staining pattern in regions adjacent to the nucleus indicative of ER staining (Merge) and a high degree of punctate co-localization in the perinuclear region (+PDM) as indicated by arrows and LUT in the last panel. C) Co-localization measurements between calsenilin and RyR2 or RyR3 for neuronal cell types (E18 primary cortical neurons and SH-SY5Y neuroblastoma cells) and 6-week-old C57BL/6 mouse brain sections (dentate gyrus, CA3, CA1, cortical layers II/III, V, VI). The Rr = Pearson’s coefficient and M1 = Mander’s coefficient describe the amount of calsenilin co-localized with the two RyR subtypes, whereas the M2 = Mander’s coefficient describes the amount of RyR2 or RyR3 co-localized with calsenilin. Statistical significance represents the SEM for each replicate; co-localization was tested with the Costes method to ensure true co-localization. D) Western blot shows the presence of calsenilin in the brain-derived ER microsomes incubated with calsenilin protein and subjected to co-immunoprecipitation separation using the RyR2 antibody; the IgG control is shown in lane “IgG”, and molecular weight standards are shown in lane “PSS”. Abbreviations: RyR, ryanodine receptor; DG, Dentate Gyrus; CA1 or CA3, Cornu Ammonis 1 or 3; Ctx, Cortex layer; IgG, Immunoglobulin G; MW, molecular weight; PSS, pre-stained standard.
Figure Legend Snippet: Calsenilin and RyR are co-localized and have a direct protein-protein interaction in neuronal tissue Calsenilin (green) and A) RyR2 or RyR3 (red) immunoreactivity in E18 primary cultured cortical neurons B) RyR2 (red) expression in the dentate gyrus and cortical layer VI show a perinuclear staining pattern in regions adjacent to the nucleus indicative of ER staining (Merge) and a high degree of punctate co-localization in the perinuclear region (+PDM) as indicated by arrows and LUT in the last panel. C) Co-localization measurements between calsenilin and RyR2 or RyR3 for neuronal cell types (E18 primary cortical neurons and SH-SY5Y neuroblastoma cells) and 6-week-old C57BL/6 mouse brain sections (dentate gyrus, CA3, CA1, cortical layers II/III, V, VI). The Rr = Pearson’s coefficient and M1 = Mander’s coefficient describe the amount of calsenilin co-localized with the two RyR subtypes, whereas the M2 = Mander’s coefficient describes the amount of RyR2 or RyR3 co-localized with calsenilin. Statistical significance represents the SEM for each replicate; co-localization was tested with the Costes method to ensure true co-localization. D) Western blot shows the presence of calsenilin in the brain-derived ER microsomes incubated with calsenilin protein and subjected to co-immunoprecipitation separation using the RyR2 antibody; the IgG control is shown in lane “IgG”, and molecular weight standards are shown in lane “PSS”. Abbreviations: RyR, ryanodine receptor; DG, Dentate Gyrus; CA1 or CA3, Cornu Ammonis 1 or 3; Ctx, Cortex layer; IgG, Immunoglobulin G; MW, molecular weight; PSS, pre-stained standard.

Techniques Used: Cell Culture, Expressing, Staining, Western Blot, Derivative Assay, Incubation, Immunoprecipitation, Molecular Weight

8) Product Images from "Control of neuronal ryanodine receptor-mediated calcium signaling by calsenilin"

Article Title: Control of neuronal ryanodine receptor-mediated calcium signaling by calsenilin

Journal: Molecular neurobiology

doi: 10.1007/s12035-018-1080-2

Calsenilin and RyR are co-localized and have a direct protein-protein interaction in neuronal tissue Calsenilin (green) and A) RyR2 or RyR3 (red) immunoreactivity in E18 primary cultured cortical neurons B) RyR2 (red) expression in the dentate gyrus and cortical layer VI show a perinuclear staining pattern in regions adjacent to the nucleus indicative of ER staining (Merge) and a high degree of punctate co-localization in the perinuclear region (+PDM) as indicated by arrows and LUT in the last panel. C) Co-localization measurements between calsenilin and RyR2 or RyR3 for neuronal cell types (E18 primary cortical neurons and SH-SY5Y neuroblastoma cells) and 6-week-old C57BL/6 mouse brain sections (dentate gyrus, CA3, CA1, cortical layers II/III, V, VI). The Rr = Pearson’s coefficient and M1 = Mander’s coefficient describe the amount of calsenilin co-localized with the two RyR subtypes, whereas the M2 = Mander’s coefficient describes the amount of RyR2 or RyR3 co-localized with calsenilin. Statistical significance represents the SEM for each replicate; co-localization was tested with the Costes method to ensure true co-localization. D) Western blot shows the presence of calsenilin in the brain-derived ER microsomes incubated with calsenilin protein and subjected to co-immunoprecipitation separation using the RyR2 antibody; the IgG control is shown in lane “IgG”, and molecular weight standards are shown in lane “PSS”. Abbreviations: RyR, ryanodine receptor; DG, Dentate Gyrus; CA1 or CA3, Cornu Ammonis 1 or 3; Ctx, Cortex layer; IgG, Immunoglobulin G; MW, molecular weight; PSS, pre-stained standard.
Figure Legend Snippet: Calsenilin and RyR are co-localized and have a direct protein-protein interaction in neuronal tissue Calsenilin (green) and A) RyR2 or RyR3 (red) immunoreactivity in E18 primary cultured cortical neurons B) RyR2 (red) expression in the dentate gyrus and cortical layer VI show a perinuclear staining pattern in regions adjacent to the nucleus indicative of ER staining (Merge) and a high degree of punctate co-localization in the perinuclear region (+PDM) as indicated by arrows and LUT in the last panel. C) Co-localization measurements between calsenilin and RyR2 or RyR3 for neuronal cell types (E18 primary cortical neurons and SH-SY5Y neuroblastoma cells) and 6-week-old C57BL/6 mouse brain sections (dentate gyrus, CA3, CA1, cortical layers II/III, V, VI). The Rr = Pearson’s coefficient and M1 = Mander’s coefficient describe the amount of calsenilin co-localized with the two RyR subtypes, whereas the M2 = Mander’s coefficient describes the amount of RyR2 or RyR3 co-localized with calsenilin. Statistical significance represents the SEM for each replicate; co-localization was tested with the Costes method to ensure true co-localization. D) Western blot shows the presence of calsenilin in the brain-derived ER microsomes incubated with calsenilin protein and subjected to co-immunoprecipitation separation using the RyR2 antibody; the IgG control is shown in lane “IgG”, and molecular weight standards are shown in lane “PSS”. Abbreviations: RyR, ryanodine receptor; DG, Dentate Gyrus; CA1 or CA3, Cornu Ammonis 1 or 3; Ctx, Cortex layer; IgG, Immunoglobulin G; MW, molecular weight; PSS, pre-stained standard.

Techniques Used: Cell Culture, Expressing, Staining, Western Blot, Derivative Assay, Incubation, Immunoprecipitation, Molecular Weight

9) Product Images from "Calcium-regulatory proteins as modulators of chemotherapy in human neuroblastoma"

Article Title: Calcium-regulatory proteins as modulators of chemotherapy in human neuroblastoma

Journal: Oncotarget

doi: 10.18632/oncotarget.15283

Confocal laser scanning microscopy demonstrates increased expression levels of IP3R3, RYR1 and S100A6 in SH-SY5Y cells following CDDP or TOPO treatment ( A ) Representative fluorescence confocal images of SH-SY5Y cells that endogenously express IP3R1, IP3R3, RYR1, RYR3 and S100A6 as detected by Fluo-488 nm conjugated antibodies (green fluorescence) using images taken in similar experimental set ups following exposure to either 1 μM CDDP or 0.01 μM TOPO for 72 h. Cell nuclei are counterstained with DAPI (blue). scale bar = 20 μm. ( B ) Quantification of fluorescence intensity (protein expression) expressed as mean corrected total cell fluorescence (CTCF) ± standard deviation (SD). Data are derived from three independent biological experiments each. Statistical significance is relative to untreated cells and considered if p
Figure Legend Snippet: Confocal laser scanning microscopy demonstrates increased expression levels of IP3R3, RYR1 and S100A6 in SH-SY5Y cells following CDDP or TOPO treatment ( A ) Representative fluorescence confocal images of SH-SY5Y cells that endogenously express IP3R1, IP3R3, RYR1, RYR3 and S100A6 as detected by Fluo-488 nm conjugated antibodies (green fluorescence) using images taken in similar experimental set ups following exposure to either 1 μM CDDP or 0.01 μM TOPO for 72 h. Cell nuclei are counterstained with DAPI (blue). scale bar = 20 μm. ( B ) Quantification of fluorescence intensity (protein expression) expressed as mean corrected total cell fluorescence (CTCF) ± standard deviation (SD). Data are derived from three independent biological experiments each. Statistical significance is relative to untreated cells and considered if p

Techniques Used: Confocal Laser Scanning Microscopy, Expressing, Fluorescence, Standard Deviation, Derivative Assay, IF-P

Treatment with CDDP or TOPO induces alterations in the mRNA expression of key [Ca 2+ ] i modulators in neuroblastoma cells Changes in mRNA expression of ITPR1, ITPR3, RYR1, RYR3 , S100A6 and COX2 were assessed via qRT-PCR in SH-SY5Y cells following 12 h, 24 h, 48 h or 72 h exposure to ( A ) 0.1 μM–10 μM CDDP or ( B ) 0.001 μM–1 μM TOPO. The expression pattern in IMR-32 cells was also assessed following exposure to 0.1 μM–10 μM CDDP ( C ). Data are expressed as fold-change (RQ), relative to the untreated control and are normalized to expression of ARF-1 mRNA as reference. Data are derived from three independent biological experiments each. Statistical significance is relative to the untreated control and considered if p
Figure Legend Snippet: Treatment with CDDP or TOPO induces alterations in the mRNA expression of key [Ca 2+ ] i modulators in neuroblastoma cells Changes in mRNA expression of ITPR1, ITPR3, RYR1, RYR3 , S100A6 and COX2 were assessed via qRT-PCR in SH-SY5Y cells following 12 h, 24 h, 48 h or 72 h exposure to ( A ) 0.1 μM–10 μM CDDP or ( B ) 0.001 μM–1 μM TOPO. The expression pattern in IMR-32 cells was also assessed following exposure to 0.1 μM–10 μM CDDP ( C ). Data are expressed as fold-change (RQ), relative to the untreated control and are normalized to expression of ARF-1 mRNA as reference. Data are derived from three independent biological experiments each. Statistical significance is relative to the untreated control and considered if p

Techniques Used: Expressing, Quantitative RT-PCR, Derivative Assay, IF-P

Changes in the expression of IP3R3, RYR3 and S100A6 at the protein level in SH-SY5Y cells following exposure to CDDP or TOPO SH-SY5Y cells were treated with either ( A ) CDDP (1 μM/10 μM) or ( B ) TOPO (0.01 μM/0.1 μM) for 72 hours and then harvested, fixed, permeabilized and incubated with primary antibodies specific for IP3R1, IP3R3, RYR1, RYR3 or S100A6 followed by incubation with a fluorescently conjugated (Alexa-488 nm) secondary antibody. The percentage of positive cells is individually presented for each protein or together for comparative analysis (expressed as a fold-change, relative to the untreated control). Data are derived from three independent biological experiments each. Statistical significance was calculated relative to untreated cells and considered if p
Figure Legend Snippet: Changes in the expression of IP3R3, RYR3 and S100A6 at the protein level in SH-SY5Y cells following exposure to CDDP or TOPO SH-SY5Y cells were treated with either ( A ) CDDP (1 μM/10 μM) or ( B ) TOPO (0.01 μM/0.1 μM) for 72 hours and then harvested, fixed, permeabilized and incubated with primary antibodies specific for IP3R1, IP3R3, RYR1, RYR3 or S100A6 followed by incubation with a fluorescently conjugated (Alexa-488 nm) secondary antibody. The percentage of positive cells is individually presented for each protein or together for comparative analysis (expressed as a fold-change, relative to the untreated control). Data are derived from three independent biological experiments each. Statistical significance was calculated relative to untreated cells and considered if p

Techniques Used: Expressing, Incubation, Derivative Assay, IF-P

10) Product Images from "Modulating ryanodine receptors with dantrolene attenuates neuronopathic phenotype in Gaucher disease mice"

Article Title: Modulating ryanodine receptors with dantrolene attenuates neuronopathic phenotype in Gaucher disease mice

Journal: Human Molecular Genetics

doi: 10.1093/hmg/ddw322

Ryrs expression in 4L;C* mouse brains. (A) Decreased mRNA expression (fold change of WT level) of three Ryrs in 4L;C* brain regions determined by RNASeq analysis ( n = 3 mice/group). (B) Immunoblot of brain lysate showed Ryr3 was expressed at normal levels at 13 days of age and significantly decreased by 44 days of age in 4L;C* brain (27% of WT level) compared to WT mice. P -values were from Student’s t-test, n = 3 mice/group, 2-4 replicates of the experiment. (C) Immunofluorescence staining of brain sections by anti-Ryr1 and anti-Ryr3 antibodies (green) showed decreased Ryr signals in 4L;C* brain including cortex and midbrain regions. Scale bar is 20 µm for all the images. (D) Co-staining of Ryr3 (green) with neural cell markers. NeuN (red) is for neurons. GFAP (red) is for astrocytes. O4 (red) is for oligodendrocytes. Ryr3 signals were detected in neurons, astrocytes and oligodendrocytes in WT midbrains. 4L;C* midbrain had low level of Ryr 3 signals in those cells compared to WT. Scale bar is 20 µm for all the images. DAPI (blue) stained cell nuclei. Images are representative from n = 3 mice for each genotype.
Figure Legend Snippet: Ryrs expression in 4L;C* mouse brains. (A) Decreased mRNA expression (fold change of WT level) of three Ryrs in 4L;C* brain regions determined by RNASeq analysis ( n = 3 mice/group). (B) Immunoblot of brain lysate showed Ryr3 was expressed at normal levels at 13 days of age and significantly decreased by 44 days of age in 4L;C* brain (27% of WT level) compared to WT mice. P -values were from Student’s t-test, n = 3 mice/group, 2-4 replicates of the experiment. (C) Immunofluorescence staining of brain sections by anti-Ryr1 and anti-Ryr3 antibodies (green) showed decreased Ryr signals in 4L;C* brain including cortex and midbrain regions. Scale bar is 20 µm for all the images. (D) Co-staining of Ryr3 (green) with neural cell markers. NeuN (red) is for neurons. GFAP (red) is for astrocytes. O4 (red) is for oligodendrocytes. Ryr3 signals were detected in neurons, astrocytes and oligodendrocytes in WT midbrains. 4L;C* midbrain had low level of Ryr 3 signals in those cells compared to WT. Scale bar is 20 µm for all the images. DAPI (blue) stained cell nuclei. Images are representative from n = 3 mice for each genotype.

Techniques Used: Expressing, Mouse Assay, Immunofluorescence, Staining

Ryr expression in dantrolene treated 4L;C* brain. (A) Immunoblot of Ryr3 in CBE-N2a cells. Ryr3 protein level was lower in CBE-N2a than N2a cells, and increased in dantrolene treated CBE-N2a cells. (B) 4L;C* cerebrum showed significantly reduced Ryr3 protein at 9% of WT level. In dantrolene treated 4L;C* cerebrum, Ryr3 protein level was significantly increased compared to untreated 4L;C*. 4L;C* panel was spliced to make panel layout consistent with other graphs. A dotted line shows splice area. (C) Immunofluorescence staining of Ryr3. 4L;C* midbrain and brain stem showed reduced Ryr3 (green) signal at 49% or 34% of WT level, respectively. In dantrolene treated 4L;C* brain, Ryr3 signal was increased to 94% in midbrain and 79% in brain stem of WT level. DAPI (blue) stained cell nuclei. Scale bar is 20 µm for all the images. ( D and E ) CAMK IV and calmodulin (CAM). 4L;C* cerebrum showed decreased level of CAMK IV (D) and increased level of CAM (E) compared to WT. Dantrolene treatment normalized expression of CAMK IV and CAM to nearly WT level. One-way ANOVA with post-hoc Tukey test ( P
Figure Legend Snippet: Ryr expression in dantrolene treated 4L;C* brain. (A) Immunoblot of Ryr3 in CBE-N2a cells. Ryr3 protein level was lower in CBE-N2a than N2a cells, and increased in dantrolene treated CBE-N2a cells. (B) 4L;C* cerebrum showed significantly reduced Ryr3 protein at 9% of WT level. In dantrolene treated 4L;C* cerebrum, Ryr3 protein level was significantly increased compared to untreated 4L;C*. 4L;C* panel was spliced to make panel layout consistent with other graphs. A dotted line shows splice area. (C) Immunofluorescence staining of Ryr3. 4L;C* midbrain and brain stem showed reduced Ryr3 (green) signal at 49% or 34% of WT level, respectively. In dantrolene treated 4L;C* brain, Ryr3 signal was increased to 94% in midbrain and 79% in brain stem of WT level. DAPI (blue) stained cell nuclei. Scale bar is 20 µm for all the images. ( D and E ) CAMK IV and calmodulin (CAM). 4L;C* cerebrum showed decreased level of CAMK IV (D) and increased level of CAM (E) compared to WT. Dantrolene treatment normalized expression of CAMK IV and CAM to nearly WT level. One-way ANOVA with post-hoc Tukey test ( P

Techniques Used: Expressing, Immunofluorescence, Staining, Chick Chorioallantoic Membrane Assay

11) Product Images from "Suppression of InsP3 Receptor-Mediated Ca2+ Signaling Alleviates Mutant Presenilin-Linked Familial Alzheimer's Disease Pathogenesis"

Article Title: Suppression of InsP3 Receptor-Mediated Ca2+ Signaling Alleviates Mutant Presenilin-Linked Familial Alzheimer's Disease Pathogenesis

Journal: The Journal of Neuroscience

doi: 10.1523/JNEUROSCI.5441-13.2014

The Opt allele rescues elevated hippocampal RyR protein levels in M146V mice. A , Western blot analyses of hippocampal lysates from 5-week-old animals using a pan-RyR antibody ( n = 6 mice each) or antibodies specific to RyR2 ( n = 4 mice each) or RyR3 (
Figure Legend Snippet: The Opt allele rescues elevated hippocampal RyR protein levels in M146V mice. A , Western blot analyses of hippocampal lysates from 5-week-old animals using a pan-RyR antibody ( n = 6 mice each) or antibodies specific to RyR2 ( n = 4 mice each) or RyR3 (

Techniques Used: Mouse Assay, Western Blot

12) Product Images from "Increased Muscle Stress-Sensitivity Induced by Selenoprotein N Inactivation in Mouse: A Mammalian Model for SEPN1-Related Myopathy"

Article Title: Increased Muscle Stress-Sensitivity Induced by Selenoprotein N Inactivation in Mouse: A Mammalian Model for SEPN1-Related Myopathy

Journal: PLoS ONE

doi: 10.1371/journal.pone.0023094

Ultrastructural organization and triadic junctions in Sepn1 −/− adult muscles. A ) Electron microscopy image of gastrocnemius muscles from 6 month-old wild-type and mutant mice. No defect in sarcomere organization, mitochondria morphology (arrows) and triads structure (brackets) were observed in mutant (right panel), compared to wild-types (left panel). Scale bars, 1 µm (top) and 100 nm (bottom). B ) Immunostaining for DHPR (green) and RyR1 or RyR3 (red) on longitudinal sections of quadriceps from 2 month-old mice, revealing normal localization of both receptors in mutant mice compared to controls. Nuclei are revealed by DAPI staining. Boxed regions in the merged images are magnified as inserts (right) showing intracellular co-localization (yellow). Scale bar is 10 µm. C ) Skeletal muscle microsomes extracts from Sepn1 +/+ or Sepn1 −/− littermates were immunoblotted for Ryanodine Receptor type 1 (RyR1), Ryanodine Receptor type 3 (RyR3), Dihydropyridine Receptor (DHPR), Selenoprotein N (SelN) and triadin isoform Trisk 95 (Trisk 95).
Figure Legend Snippet: Ultrastructural organization and triadic junctions in Sepn1 −/− adult muscles. A ) Electron microscopy image of gastrocnemius muscles from 6 month-old wild-type and mutant mice. No defect in sarcomere organization, mitochondria morphology (arrows) and triads structure (brackets) were observed in mutant (right panel), compared to wild-types (left panel). Scale bars, 1 µm (top) and 100 nm (bottom). B ) Immunostaining for DHPR (green) and RyR1 or RyR3 (red) on longitudinal sections of quadriceps from 2 month-old mice, revealing normal localization of both receptors in mutant mice compared to controls. Nuclei are revealed by DAPI staining. Boxed regions in the merged images are magnified as inserts (right) showing intracellular co-localization (yellow). Scale bar is 10 µm. C ) Skeletal muscle microsomes extracts from Sepn1 +/+ or Sepn1 −/− littermates were immunoblotted for Ryanodine Receptor type 1 (RyR1), Ryanodine Receptor type 3 (RyR3), Dihydropyridine Receptor (DHPR), Selenoprotein N (SelN) and triadin isoform Trisk 95 (Trisk 95).

Techniques Used: Electron Microscopy, Mutagenesis, Mouse Assay, Immunostaining, Staining

13) Product Images from "Maturation and long-term hypoxia alters Ca2+-induced Ca2+ release in sheep cerebrovascular sympathetic neurons"

Article Title: Maturation and long-term hypoxia alters Ca2+-induced Ca2+ release in sheep cerebrovascular sympathetic neurons

Journal: Journal of Applied Physiology

doi: 10.1152/japplphysiol.00363.2009

Representative electrical field stimulation (EFS)-evoked intracellular Ca 2+  concentration ([Ca 2+ ] i ) transients in fetal normoxic superior cervical ganglia (SCG) cells showing the application of  EFS protocol 1  ( A ) and  protocol 2  ( B ).  A :  protocol 1 . A priming stimulus of square wave EFS (50 pulses at 5 Hz, 1-ms duration, 300 mA) was used to ensure filling of smooth endoplasmic reticulum Ca 2+  stores. This was followed by a set of graded pulses (3–27 pulses at 3 Hz, 1-ms duration, 300 mA). Ryanodine was added during the last supermaximal transient with a subsequent equilibration period of 30 min. To ensure maximal blockade of ryanodine receptors (RyRs), caffeine was applied and failed to evoke a [Ca 2+ ] i  transient.  B :  protocol 2 . Control stimulations were as described in  A  followed by the addition of caffeine, as indicated by the large transient that returned to baseline [Ca 2+ ] i . EFS was then repeated 10 min after the formation of the caffeine-evoked [Ca 2+ ] i  transient. All electrical stimulations were followed by at least 2 min for recovery.
Figure Legend Snippet: Representative electrical field stimulation (EFS)-evoked intracellular Ca 2+ concentration ([Ca 2+ ] i ) transients in fetal normoxic superior cervical ganglia (SCG) cells showing the application of EFS protocol 1 ( A ) and protocol 2 ( B ). A : protocol 1 . A priming stimulus of square wave EFS (50 pulses at 5 Hz, 1-ms duration, 300 mA) was used to ensure filling of smooth endoplasmic reticulum Ca 2+ stores. This was followed by a set of graded pulses (3–27 pulses at 3 Hz, 1-ms duration, 300 mA). Ryanodine was added during the last supermaximal transient with a subsequent equilibration period of 30 min. To ensure maximal blockade of ryanodine receptors (RyRs), caffeine was applied and failed to evoke a [Ca 2+ ] i transient. B : protocol 2 . Control stimulations were as described in A followed by the addition of caffeine, as indicated by the large transient that returned to baseline [Ca 2+ ] i . EFS was then repeated 10 min after the formation of the caffeine-evoked [Ca 2+ ] i transient. All electrical stimulations were followed by at least 2 min for recovery.

Techniques Used: Concentration Assay, Mass Spectrometry

14) Product Images from "Hypernitrosylated ryanodine receptor/calcium release channels are leaky in dystrophic muscle"

Article Title: Hypernitrosylated ryanodine receptor/calcium release channels are leaky in dystrophic muscle

Journal: Nature medicine

doi: 10.1038/nm.1916

iNOS co-immunoprecipitates and co-localizes with RyR1 and S-nitrosylation of RyR1 depletes the channel of calstabin1 ( a ) In vitro S-nitrosylation of skeletal SR microsomes with NO donors Nor-3 or Noc-12 results in depletion of calstabin1 from immunoprecipitated RyR1. ( b ) Immunoblot of expression of three NOS isoforms (iNOS, eNOS, and nNOS) from WT and mdx whole muscle lysates at the indicated ages. ( c ) Co-immunoprecipitation of RyR1 and iNOS. 50 μg of mdx EDL lysate was used as positive control. RyR1 and iNOS separately immunoprecipitated from 250 μg of mdx muscle lysate and probed for RyR1 and iNOS. Antibody against RyR was pre-incubated with 100-fold excess antigenic peptide prior to immunoprecipitation (blocked IP RyR). ( d ) Immunoprecipitation-immunoblotting of RyR1 and eNOS from mdx lysate. IgG control immunoprecipitation shown at right. ( e ) RyR1 was immunoprecipitated from WT and mdx EDL lysates at indicated ages and immunoblotted for RyR1 and iNOS. (f) Immunohistochemistry showing co-localization of RyR1 and iNOS in murine skeletal muscle (EDL) from mdx but not WT mice. Scale bar in lower right panel applies to all six panels.
Figure Legend Snippet: iNOS co-immunoprecipitates and co-localizes with RyR1 and S-nitrosylation of RyR1 depletes the channel of calstabin1 ( a ) In vitro S-nitrosylation of skeletal SR microsomes with NO donors Nor-3 or Noc-12 results in depletion of calstabin1 from immunoprecipitated RyR1. ( b ) Immunoblot of expression of three NOS isoforms (iNOS, eNOS, and nNOS) from WT and mdx whole muscle lysates at the indicated ages. ( c ) Co-immunoprecipitation of RyR1 and iNOS. 50 μg of mdx EDL lysate was used as positive control. RyR1 and iNOS separately immunoprecipitated from 250 μg of mdx muscle lysate and probed for RyR1 and iNOS. Antibody against RyR was pre-incubated with 100-fold excess antigenic peptide prior to immunoprecipitation (blocked IP RyR). ( d ) Immunoprecipitation-immunoblotting of RyR1 and eNOS from mdx lysate. IgG control immunoprecipitation shown at right. ( e ) RyR1 was immunoprecipitated from WT and mdx EDL lysates at indicated ages and immunoblotted for RyR1 and iNOS. (f) Immunohistochemistry showing co-localization of RyR1 and iNOS in murine skeletal muscle (EDL) from mdx but not WT mice. Scale bar in lower right panel applies to all six panels.

Techniques Used: In Vitro, Immunoprecipitation, Expressing, Positive Control, Incubation, Immunohistochemistry, Mouse Assay

RyR1 is S-nitrosylated and depleted of calstabin1 in mdx mice ( a ) RyR1 was immunoprecipitated from EDL muscle of mdx mice and WT littermates at 7, 21, 35, and 180 days after birth and immunoblotted for RyR1, RyR1 PKA phosphorylated at Ser2844 (RyR1-pS2844), S-nitrosylation of cysteine residues on RyR1 (Cys-NO), and calstabin1 bound to RyR1. Positive and negative control (IgG) immunoprecipitation are shown for 7 day WT hearts. Blots are representative of three independent experiments. ( b ) Quantification of RyR1 PKA phosphorylation, RyR1 S-nitrosylation, and bound calstabin1 relative to total RyR1. Data presented as mean ± S.E.M. *, P
Figure Legend Snippet: RyR1 is S-nitrosylated and depleted of calstabin1 in mdx mice ( a ) RyR1 was immunoprecipitated from EDL muscle of mdx mice and WT littermates at 7, 21, 35, and 180 days after birth and immunoblotted for RyR1, RyR1 PKA phosphorylated at Ser2844 (RyR1-pS2844), S-nitrosylation of cysteine residues on RyR1 (Cys-NO), and calstabin1 bound to RyR1. Positive and negative control (IgG) immunoprecipitation are shown for 7 day WT hearts. Blots are representative of three independent experiments. ( b ) Quantification of RyR1 PKA phosphorylation, RyR1 S-nitrosylation, and bound calstabin1 relative to total RyR1. Data presented as mean ± S.E.M. *, P

Techniques Used: Mouse Assay, Immunoprecipitation, Negative Control

Preventing calstabin1 depletion from the RyR1 complex with S107 improves grip strength and reduces muscle damage ( a ) We determined forelimb grip strength in sedentary mice after two weeks of treatment with S107 administered via an osmotic pump as described in the methods. ( mdx -S107, n = 14, black diamond), vehicle ( mdx -vehicle, n = 14, grey triangle), WT ( n = 9, open square) mice. Data are presented as a scatter plot of absolute grip strength (ponds) versus body weight (BW, g). Least square fit lines are overlaid. ( b ) Grip strength normalized to BW. *, P
Figure Legend Snippet: Preventing calstabin1 depletion from the RyR1 complex with S107 improves grip strength and reduces muscle damage ( a ) We determined forelimb grip strength in sedentary mice after two weeks of treatment with S107 administered via an osmotic pump as described in the methods. ( mdx -S107, n = 14, black diamond), vehicle ( mdx -vehicle, n = 14, grey triangle), WT ( n = 9, open square) mice. Data are presented as a scatter plot of absolute grip strength (ponds) versus body weight (BW, g). Least square fit lines are overlaid. ( b ) Grip strength normalized to BW. *, P

Techniques Used: Mouse Assay

Preventing RyR1 leak with S107 reduces Ca 2+ leak, enhances muscle force, and voluntary exercise in mdx mice ( a ) Isometric and eccentric force production in EDL muscle in situ in anesthetized mice ( Supplementary Methods , online). Typical recording from an mdx mouse EDL muscle (bottom graph) indicating a decline in force production during tetanus following mechanical stress (arrow). ( b ) Effect of oral S107 on decrease in force production in mdx mice (S107, 0.25 mg ml −1 , in the drinking water for 10 days prior to testing, n = 5 for each group). Spontaneous Ca 2+ sparks recorded in EDL muscles from: WT ( c ), vehicle treated mdx ( d ), and S107 treated mdx mice ( e ). Representative ΔF/F0 images (top) and fluorescence time courses (bottom) at different triads (colored arrow heads). ( f ) Spark frequency ( n = 5 mice for each condition, 3–4 fibers per muscle). Data are mean ± SEM (* P
Figure Legend Snippet: Preventing RyR1 leak with S107 reduces Ca 2+ leak, enhances muscle force, and voluntary exercise in mdx mice ( a ) Isometric and eccentric force production in EDL muscle in situ in anesthetized mice ( Supplementary Methods , online). Typical recording from an mdx mouse EDL muscle (bottom graph) indicating a decline in force production during tetanus following mechanical stress (arrow). ( b ) Effect of oral S107 on decrease in force production in mdx mice (S107, 0.25 mg ml −1 , in the drinking water for 10 days prior to testing, n = 5 for each group). Spontaneous Ca 2+ sparks recorded in EDL muscles from: WT ( c ), vehicle treated mdx ( d ), and S107 treated mdx mice ( e ). Representative ΔF/F0 images (top) and fluorescence time courses (bottom) at different triads (colored arrow heads). ( f ) Spark frequency ( n = 5 mice for each condition, 3–4 fibers per muscle). Data are mean ± SEM (* P

Techniques Used: Mouse Assay, In Situ, Fluorescence

15) Product Images from "Hypernitrosylated ryanodine receptor/calcium release channels are leaky in dystrophic muscle"

Article Title: Hypernitrosylated ryanodine receptor/calcium release channels are leaky in dystrophic muscle

Journal: Nature medicine

doi: 10.1038/nm.1916

iNOS co-immunoprecipitates and co-localizes with RyR1 and S-nitrosylation of RyR1 depletes the channel of calstabin1 ( a ) In vitro S-nitrosylation of skeletal SR microsomes with NO donors Nor-3 or Noc-12 results in depletion of calstabin1 from immunoprecipitated RyR1. ( b ) Immunoblot of expression of three NOS isoforms (iNOS, eNOS, and nNOS) from WT and mdx whole muscle lysates at the indicated ages. ( c ) Co-immunoprecipitation of RyR1 and iNOS. 50 μg of mdx EDL lysate was used as positive control. RyR1 and iNOS separately immunoprecipitated from 250 μg of mdx muscle lysate and probed for RyR1 and iNOS. Antibody against RyR was pre-incubated with 100-fold excess antigenic peptide prior to immunoprecipitation (blocked IP RyR). ( d ) Immunoprecipitation-immunoblotting of RyR1 and eNOS from mdx lysate. IgG control immunoprecipitation shown at right. ( e ) RyR1 was immunoprecipitated from WT and mdx EDL lysates at indicated ages and immunoblotted for RyR1 and iNOS. (f) Immunohistochemistry showing co-localization of RyR1 and iNOS in murine skeletal muscle (EDL) from mdx but not WT mice. Scale bar in lower right panel applies to all six panels.
Figure Legend Snippet: iNOS co-immunoprecipitates and co-localizes with RyR1 and S-nitrosylation of RyR1 depletes the channel of calstabin1 ( a ) In vitro S-nitrosylation of skeletal SR microsomes with NO donors Nor-3 or Noc-12 results in depletion of calstabin1 from immunoprecipitated RyR1. ( b ) Immunoblot of expression of three NOS isoforms (iNOS, eNOS, and nNOS) from WT and mdx whole muscle lysates at the indicated ages. ( c ) Co-immunoprecipitation of RyR1 and iNOS. 50 μg of mdx EDL lysate was used as positive control. RyR1 and iNOS separately immunoprecipitated from 250 μg of mdx muscle lysate and probed for RyR1 and iNOS. Antibody against RyR was pre-incubated with 100-fold excess antigenic peptide prior to immunoprecipitation (blocked IP RyR). ( d ) Immunoprecipitation-immunoblotting of RyR1 and eNOS from mdx lysate. IgG control immunoprecipitation shown at right. ( e ) RyR1 was immunoprecipitated from WT and mdx EDL lysates at indicated ages and immunoblotted for RyR1 and iNOS. (f) Immunohistochemistry showing co-localization of RyR1 and iNOS in murine skeletal muscle (EDL) from mdx but not WT mice. Scale bar in lower right panel applies to all six panels.

Techniques Used: In Vitro, Immunoprecipitation, Expressing, Positive Control, Incubation, Immunohistochemistry, Mouse Assay

RyR1 is S-nitrosylated and depleted of calstabin1 in mdx mice ( a ) RyR1 was immunoprecipitated from EDL muscle of mdx mice and WT littermates at 7, 21, 35, and 180 days after birth and immunoblotted for RyR1, RyR1 PKA phosphorylated at Ser2844 (RyR1-pS2844), S-nitrosylation of cysteine residues on RyR1 (Cys-NO), and calstabin1 bound to RyR1. Positive and negative control (IgG) immunoprecipitation are shown for 7 day WT hearts. Blots are representative of three independent experiments. ( b ) Quantification of RyR1 PKA phosphorylation, RyR1 S-nitrosylation, and bound calstabin1 relative to total RyR1. Data presented as mean ± S.E.M. *, P
Figure Legend Snippet: RyR1 is S-nitrosylated and depleted of calstabin1 in mdx mice ( a ) RyR1 was immunoprecipitated from EDL muscle of mdx mice and WT littermates at 7, 21, 35, and 180 days after birth and immunoblotted for RyR1, RyR1 PKA phosphorylated at Ser2844 (RyR1-pS2844), S-nitrosylation of cysteine residues on RyR1 (Cys-NO), and calstabin1 bound to RyR1. Positive and negative control (IgG) immunoprecipitation are shown for 7 day WT hearts. Blots are representative of three independent experiments. ( b ) Quantification of RyR1 PKA phosphorylation, RyR1 S-nitrosylation, and bound calstabin1 relative to total RyR1. Data presented as mean ± S.E.M. *, P

Techniques Used: Mouse Assay, Immunoprecipitation, Negative Control

Preventing calstabin1 depletion from the RyR1 complex with S107 improves grip strength and reduces muscle damage ( a ) We determined forelimb grip strength in sedentary mice after two weeks of treatment with S107 administered via an osmotic pump as described in the methods. ( mdx -S107, n = 14, black diamond), vehicle ( mdx -vehicle, n = 14, grey triangle), WT ( n = 9, open square) mice. Data are presented as a scatter plot of absolute grip strength (ponds) versus body weight (BW, g). Least square fit lines are overlaid. ( b ) Grip strength normalized to BW. *, P
Figure Legend Snippet: Preventing calstabin1 depletion from the RyR1 complex with S107 improves grip strength and reduces muscle damage ( a ) We determined forelimb grip strength in sedentary mice after two weeks of treatment with S107 administered via an osmotic pump as described in the methods. ( mdx -S107, n = 14, black diamond), vehicle ( mdx -vehicle, n = 14, grey triangle), WT ( n = 9, open square) mice. Data are presented as a scatter plot of absolute grip strength (ponds) versus body weight (BW, g). Least square fit lines are overlaid. ( b ) Grip strength normalized to BW. *, P

Techniques Used: Mouse Assay

Preventing RyR1 leak with S107 reduces Ca 2+ leak, enhances muscle force, and voluntary exercise in mdx mice ( a ) Isometric and eccentric force production in EDL muscle in situ in anesthetized mice ( Supplementary Methods , online). Typical recording from an mdx mouse EDL muscle (bottom graph) indicating a decline in force production during tetanus following mechanical stress (arrow). ( b ) Effect of oral S107 on decrease in force production in mdx mice (S107, 0.25 mg ml −1 , in the drinking water for 10 days prior to testing, n = 5 for each group). Spontaneous Ca 2+ sparks recorded in EDL muscles from: WT ( c ), vehicle treated mdx ( d ), and S107 treated mdx mice ( e ). Representative ΔF/F0 images (top) and fluorescence time courses (bottom) at different triads (colored arrow heads). ( f ) Spark frequency ( n = 5 mice for each condition, 3–4 fibers per muscle). Data are mean ± SEM (* P
Figure Legend Snippet: Preventing RyR1 leak with S107 reduces Ca 2+ leak, enhances muscle force, and voluntary exercise in mdx mice ( a ) Isometric and eccentric force production in EDL muscle in situ in anesthetized mice ( Supplementary Methods , online). Typical recording from an mdx mouse EDL muscle (bottom graph) indicating a decline in force production during tetanus following mechanical stress (arrow). ( b ) Effect of oral S107 on decrease in force production in mdx mice (S107, 0.25 mg ml −1 , in the drinking water for 10 days prior to testing, n = 5 for each group). Spontaneous Ca 2+ sparks recorded in EDL muscles from: WT ( c ), vehicle treated mdx ( d ), and S107 treated mdx mice ( e ). Representative ΔF/F0 images (top) and fluorescence time courses (bottom) at different triads (colored arrow heads). ( f ) Spark frequency ( n = 5 mice for each condition, 3–4 fibers per muscle). Data are mean ± SEM (* P

Techniques Used: Mouse Assay, In Situ, Fluorescence

16) Product Images from "Advancing age alters the expression of the ryanodine receptor 3 isoform in adult rat superior cervical ganglia"

Article Title: Advancing age alters the expression of the ryanodine receptor 3 isoform in adult rat superior cervical ganglia

Journal:

doi: 10.1152/japplphysiol.00167.2006

Validation of RyR2 and RyR3 antibody specificity, and saturation curve analysis for RyR2 and RyR3 ELISA. (A) 25 μg of total rat SCG protein were subjected to SDS-PAGE, transferred to PVDF membrane and probed with RyR2 or RyR3 antibodies. The ryanodine
Figure Legend Snippet: Validation of RyR2 and RyR3 antibody specificity, and saturation curve analysis for RyR2 and RyR3 ELISA. (A) 25 μg of total rat SCG protein were subjected to SDS-PAGE, transferred to PVDF membrane and probed with RyR2 or RyR3 antibodies. The ryanodine

Techniques Used: Enzyme-linked Immunosorbent Assay, SDS Page

Transcriptional profiling of ryr2 and ryr3 with advancing age
Figure Legend Snippet: Transcriptional profiling of ryr2 and ryr3 with advancing age

Techniques Used:

Phosphorylation of total ryanodine receptors do not change with age. 25 μg of total SCG protein from 6, 12 and 24 month old animals were separated and the RyRs were analyzed for phosphate groups stained with the Pro-Q Diamond phosphoprotein stain
Figure Legend Snippet: Phosphorylation of total ryanodine receptors do not change with age. 25 μg of total SCG protein from 6, 12 and 24 month old animals were separated and the RyRs were analyzed for phosphate groups stained with the Pro-Q Diamond phosphoprotein stain

Techniques Used: Staining

Ryanodine receptor expression levels with advancing age
Figure Legend Snippet: Ryanodine receptor expression levels with advancing age

Techniques Used: Expressing

The ryr1 transcript is not the predominant ryr isoform in adult SCG. 75 ng of DNase treated total RNA isolated from rat SCG ganglia or rat brain was subjected to reverse transcriptase-PCR (RT-PCR) using ryr1 -specific oligonucleotides. RT-PCR products
Figure Legend Snippet: The ryr1 transcript is not the predominant ryr isoform in adult SCG. 75 ng of DNase treated total RNA isolated from rat SCG ganglia or rat brain was subjected to reverse transcriptase-PCR (RT-PCR) using ryr1 -specific oligonucleotides. RT-PCR products

Techniques Used: Isolation, Polymerase Chain Reaction, Reverse Transcription Polymerase Chain Reaction

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    Millipore mouse monoclonal anti ryr1
    Mouse Monoclonal Anti Ryr1, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Millipore ryr3
    RyR1 but not RyR2 or <t>RyR3</t> are expressed in fast twitch skeletal muscle. Immunoblots of extracts of Tibialis anterior muscles with antibodies to RyR1, RyR2, and RyR3. Only anti-RyR1 shows a strong band at ∼550 kDa.
    Ryr3, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    RyR1 but not RyR2 or RyR3 are expressed in fast twitch skeletal muscle. Immunoblots of extracts of Tibialis anterior muscles with antibodies to RyR1, RyR2, and RyR3. Only anti-RyR1 shows a strong band at ∼550 kDa.

    Journal: Frontiers in Physiology

    Article Title: Elevated Ca2+ at the triad junction underlies dysregulation of Ca2+ signaling in dysferlin-null skeletal muscle

    doi: 10.3389/fphys.2022.1032447

    Figure Lengend Snippet: RyR1 but not RyR2 or RyR3 are expressed in fast twitch skeletal muscle. Immunoblots of extracts of Tibialis anterior muscles with antibodies to RyR1, RyR2, and RyR3. Only anti-RyR1 shows a strong band at ∼550 kDa.

    Article Snippet: Thus, RyR2 and RyR3 are unlikely to contribute significantly to abnormal Ca2+ signaling in dysferlinopathic muscle.

    Techniques: Western Blot