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Next-generation sequencing identifies pathogenic and modifier mutations in a consanguineous Chinese family with hypertrophic cardiomyopathy.
Zhang X, Xie J, Zhu S, Chen Y, Wang L, Xu B
(2017) Medicine (Baltimore) 96: e7010
MeSH Terms: Adolescent, Adult, Aged, Asian Continental Ancestry Group, Calcium Channels, L-Type, Cardiac Myosins, Cardiomyopathy, Hypertrophic, Familial, Carrier Proteins, Child, China, Consanguinity, Echocardiography, Female, Genetic Association Studies, Genetic Predisposition to Disease, Genotyping Techniques, Humans, Male, Middle Aged, Mutation, Myosin Heavy Chains, Sequence Analysis, Young Adult
Show Abstract · Added September 11, 2017
Hypertrophic cardiomyopathy (HCM) is a highly heterogeneous disease displaying considerable interfamilial and intrafamilial phenotypic variation, including disease severity, age of onset, and disease progression. This poorly understood variance raises the possibility of genetic modifier effects, particularly in MYBPC3-associated HCM.In a large consanguineous Chinese HCM family, we identified 8 members harboring the MYBPC3 c.3624delC (p.Lys1209Serfs) disease-causing mutation, but with very disparate phenotypes. Genotyping ruled out the modifying effect of previously described variants in renin-angiotensin-aldosterone system. Afterwards, we screened for modifying variants in all known causing genes and closely related genes for cardiomyopathy and channelopathy by performing targeted next-generation sequencing. For first time, we showed that a c.1598C>T (p.Ser533Leu) mutation in voltage-dependent l-type calcium channel subunit beta-2 (CACNB2) was present in all severely affected HCM patients, but not in those moderately affected or genotype-positive phenotype-negative patients. This CACNB2 p.Ser533Leu mutation is extremely conserved in evolution, and was not found in 550 healthy controls.Our results suggest that CACNB2 is a possible candidate genetic modifier of MYBPC3-associated familial HCM, but more genetic evidence and functional experiments are needed to confirm.
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23 MeSH Terms
Azithromycin Causes a Novel Proarrhythmic Syndrome.
Yang Z, Prinsen JK, Bersell KR, Shen W, Yermalitskaya L, Sidorova T, Luis PB, Hall L, Zhang W, Du L, Milne G, Tucker P, George AL, Campbell CM, Pickett RA, Shaffer CM, Chopra N, Yang T, Knollmann BC, Roden DM, Murray KT
(2017) Circ Arrhythm Electrophysiol 10:
MeSH Terms: Action Potentials, Animals, Anti-Bacterial Agents, Arrhythmias, Cardiac, Azithromycin, CHO Cells, Calcium Channel Blockers, Calcium Channels, L-Type, Cricetulus, Dose-Response Relationship, Drug, Electrocardiography, Ambulatory, Female, HEK293 Cells, Heart Rate, Humans, KCNQ1 Potassium Channel, Mice, Inbred C57BL, Myocytes, Cardiac, NAV1.5 Voltage-Gated Sodium Channel, Potassium Channel Blockers, Potassium Channels, Inwardly Rectifying, Potassium Channels, Voltage-Gated, Rabbits, Sodium Channel Blockers, Telemetry, Time Factors, Transfection, Young Adult
Show Abstract · Added July 6, 2017
BACKGROUND - The widely used macrolide antibiotic azithromycin increases risk of cardiovascular and sudden cardiac death, although the underlying mechanisms are unclear. Case reports, including the one we document here, demonstrate that azithromycin can cause rapid, polymorphic ventricular tachycardia in the absence of QT prolongation, indicating a novel proarrhythmic syndrome. We investigated the electrophysiological effects of azithromycin in vivo and in vitro using mice, cardiomyocytes, and human ion channels heterologously expressed in human embryonic kidney (HEK 293) and Chinese hamster ovary (CHO) cells.
METHODS AND RESULTS - In conscious telemetered mice, acute intraperitoneal and oral administration of azithromycin caused effects consistent with multi-ion channel block, with significant sinus slowing and increased PR, QRS, QT, and QTc intervals, as seen with azithromycin overdose. Similarly, in HL-1 cardiomyocytes, the drug slowed sinus automaticity, reduced phase 0 upstroke slope, and prolonged action potential duration. Acute exposure to azithromycin reduced peak SCN5A currents in HEK cells (IC=110±3 μmol/L) and Na current in mouse ventricular myocytes. However, with chronic (24 hour) exposure, azithromycin caused a ≈2-fold increase in both peak and late SCN5A currents, with findings confirmed for I in cardiomyocytes. Mild block occurred for K currents representing I (CHO cells expressing hERG; IC=219±21 μmol/L) and I (CHO cells expressing KCNQ1+KCNE1; IC=184±12 μmol/L), whereas azithromycin suppressed L-type Ca currents (rabbit ventricular myocytes, IC=66.5±4 μmol/L) and I (HEK cells expressing Kir2.1, IC=44±3 μmol/L).
CONCLUSIONS - Chronic exposure to azithromycin increases cardiac Na current to promote intracellular Na loading, providing a potential mechanistic basis for the novel form of proarrhythmia seen with this macrolide antibiotic.
© 2017 American Heart Association, Inc.
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28 MeSH Terms
Densin-180 Controls the Trafficking and Signaling of L-Type Voltage-Gated Ca1.2 Ca Channels at Excitatory Synapses.
Wang S, Stanika RI, Wang X, Hagen J, Kennedy MB, Obermair GJ, Colbran RJ, Lee A
(2017) J Neurosci 37: 4679-4691
MeSH Terms: Animals, Calcium Channels, L-Type, Calcium Signaling, Cerebral Cortex, Excitatory Postsynaptic Potentials, Ion Channel Gating, Male, Mice, Mice, Inbred C57BL, Mice, Knockout, Neurons, Protein Transport, Sialoglycoproteins, Signal Transduction, Synapses
Show Abstract · Added April 26, 2017
Voltage-gated Ca1.2 and Ca1.3 (L-type) Ca channels regulate neuronal excitability, synaptic plasticity, and learning and memory. Densin-180 (densin) is an excitatory synaptic protein that promotes Ca-dependent facilitation of voltage-gated Ca1.3 Ca channels in transfected cells. Mice lacking densin (densin KO) exhibit defects in synaptic plasticity, spatial memory, and increased anxiety-related behaviors-phenotypes that more closely match those in mice lacking Ca1.2 than Ca1.3. Therefore, we investigated the functional impact of densin on Ca1.2. We report that densin is an essential regulator of Ca1.2 in neurons, but has distinct modulatory effects compared with its regulation of Ca1.3. Densin binds to the N-terminal domain of Ca1.2, but not that of Ca1.3, and increases Ca1.2 currents in transfected cells and in neurons. In transfected cells, densin accelerates the forward trafficking of Ca1.2 channels without affecting their endocytosis. Consistent with a role for densin in increasing the number of postsynaptic Ca1.2 channels, overexpression of densin increases the clustering of Ca1.2 in dendrites of hippocampal neurons in culture. Compared with wild-type mice, the cell surface levels of Ca1.2 in the brain, as well as Ca1.2 current density and signaling to the nucleus, are reduced in neurons from densin KO mice. We conclude that densin is an essential regulator of neuronal Ca1 channels and ensures efficient Ca1.2 Ca signaling at excitatory synapses. The number and localization of voltage-gated Ca Ca channels are crucial determinants of neuronal excitability and synaptic transmission. We report that the protein densin-180 is highly enriched at excitatory synapses in the brain and enhances the cell surface trafficking and postsynaptic localization of Ca1.2 L-type Ca channels in neurons. This interaction promotes coupling of Ca1.2 channels to activity-dependent gene transcription. Our results reveal a mechanism that may contribute to the roles of Ca1.2 in regulating cognition and mood.
Copyright © 2017 the authors 0270-6474/17/374679-13$15.00/0.
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15 MeSH Terms
Ablation Is Associated With Increased Nitro-Oxidative Stress During Ischemia-Reperfusion Injury: Implications for Human Ischemic Cardiomyopathy.
Zhang B, Novitskaya T, Wheeler DG, Xu Z, Chepurko E, Huttinger R, He H, Varadharaj S, Zweier JL, Song Y, Xu M, Harrell FE, Su YR, Absi T, Kohr MJ, Ziolo MT, Roden DM, Shaffer CM, Galindo CL, Wells QS, Gumina RJ
(2017) Circ Heart Fail 10:
MeSH Terms: Adult, Animals, Calcium Channels, L-Type, Calcium Signaling, Calcium-Binding Proteins, Cardiomyopathies, Case-Control Studies, Disease Models, Animal, Female, Genetic Predisposition to Disease, Humans, Male, Mice, Inbred C57BL, Mice, Knockout, Middle Aged, Myocardial Infarction, Myocardial Reperfusion Injury, Myocardium, Oxidative Stress, Phenotype, Potassium Channels, Inwardly Rectifying, Reactive Nitrogen Species, Reactive Oxygen Species, Sarcoplasmic Reticulum Calcium-Transporting ATPases, Tyrosine, Ventricular Dysfunction, Left, Ventricular Function, Left, Ventricular Pressure
Show Abstract · Added April 6, 2017
BACKGROUND - Despite increased secondary cardiovascular events in patients with ischemic cardiomyopathy (ICM), the expression of innate cardiac protective molecules in the hearts of patients with ICM is incompletely characterized. Therefore, we used a nonbiased RNAseq approach to determine whether differences in cardiac protective molecules occur with ICM.
METHODS AND RESULTS - RNAseq analysis of human control and ICM left ventricular samples demonstrated a significant decrease in expression with ICM. encodes the Kir6.2 subunit of the cardioprotective K channel. Using wild-type mice and -deficient (-null) mice, we examined the effect of expression on cardiac function during ischemia-reperfusion injury. Reactive oxygen species generation increased in -null hearts above that found in wild-type mice hearts after ischemia-reperfusion injury. Continuous left ventricular pressure measurement during ischemia and reperfusion demonstrated a more compromised diastolic function in -null compared with wild-type mice during reperfusion. Analysis of key calcium-regulating proteins revealed significant differences in -null mice. Despite impaired relaxation, -null hearts increased phospholamban Ser16 phosphorylation, a modification that results in the dissociation of phospholamban from sarcoendoplasmic reticulum Ca, thereby increasing sarcoendoplasmic reticulum Ca-mediated calcium reuptake. However, -null mice also had increased 3-nitrotyrosine modification of the sarcoendoplasmic reticulum Ca-ATPase, a modification that irreversibly impairs sarcoendoplasmic reticulum Ca function, thereby contributing to diastolic dysfunction.
CONCLUSIONS - expression is decreased in human ICM. Lack of expression increases peroxynitrite-mediated modification of the key calcium-handling protein sarcoendoplasmic reticulum Ca-ATPase after myocardial ischemia-reperfusion injury, contributing to impaired diastolic function. These data suggest a mechanism for ischemia-induced diastolic dysfunction in patients with ICM.
© 2017 American Heart Association, Inc.
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28 MeSH Terms
Discovery of gene-gene interactions across multiple independent data sets of late onset Alzheimer disease from the Alzheimer Disease Genetics Consortium.
Hohman TJ, Bush WS, Jiang L, Brown-Gentry KD, Torstenson ES, Dudek SM, Mukherjee S, Naj A, Kunkle BW, Ritchie MD, Martin ER, Schellenberg GD, Mayeux R, Farrer LA, Pericak-Vance MA, Haines JL, Thornton-Wells TA, Alzheimer's Disease Genetics Consortium
(2016) Neurobiol Aging 38: 141-150
MeSH Terms: ATP Binding Cassette Transporter, Subfamily B, Alzheimer Disease, Cadherins, Calcium Channels, L-Type, Datasets as Topic, Disease Progression, Epistasis, Genetic, Female, Genetic Association Studies, Humans, Male, Models, Genetic, Phosphatidylethanolamine Binding Protein, Polymorphism, Single Nucleotide, Receptors, Adrenergic, alpha-1, Receptors, N-Methyl-D-Aspartate, Risk, Ryanodine Receptor Calcium Release Channel, Saposins, Sirtuin 1
Show Abstract · Added April 10, 2018
Late-onset Alzheimer disease (AD) has a complex genetic etiology, involving locus heterogeneity, polygenic inheritance, and gene-gene interactions; however, the investigation of interactions in recent genome-wide association studies has been limited. We used a biological knowledge-driven approach to evaluate gene-gene interactions for consistency across 13 data sets from the Alzheimer Disease Genetics Consortium. Fifteen single nucleotide polymorphism (SNP)-SNP pairs within 3 gene-gene combinations were identified: SIRT1 × ABCB1, PSAP × PEBP4, and GRIN2B × ADRA1A. In addition, we extend a previously identified interaction from an endophenotype analysis between RYR3 × CACNA1C. Finally, post hoc gene expression analyses of the implicated SNPs further implicate SIRT1 and ABCB1, and implicate CDH23 which was most recently identified as an AD risk locus in an epigenetic analysis of AD. The observed interactions in this article highlight ways in which genotypic variation related to disease may depend on the genetic context in which it occurs. Further, our results highlight the utility of evaluating genetic interactions to explain additional variance in AD risk and identify novel molecular mechanisms of AD pathogenesis.
Copyright © 2016 Elsevier Inc. All rights reserved.
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20 MeSH Terms
Differential CaMKII regulation by voltage-gated calcium channels in the striatum.
Pasek JG, Wang X, Colbran RJ
(2015) Mol Cell Neurosci 68: 234-43
MeSH Terms: 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester, Animals, Calcium, Calcium Channel Agonists, Calcium Channel Blockers, Calcium Channels, L-Type, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Chelating Agents, Corpus Striatum, Egtazic Acid, Enzyme Inhibitors, Gene Expression Regulation, In Vitro Techniques, Male, Mice, Mice, Inbred C57BL, Pyrroles, Receptors, Glutamate, Signal Transduction, Spider Venoms
Show Abstract · Added February 15, 2016
Calcium signaling regulates synaptic plasticity and many other functions in striatal medium spiny neurons to modulate basal ganglia function. Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is a major calcium-dependent signaling protein that couples calcium entry to diverse cellular changes. CaMKII activation results in autophosphorylation at Thr286 and sustained calcium-independent CaMKII activity after calcium signals dissipate. However, little is known about the mechanisms regulating striatal CaMKII. To address this, mouse brain slices were treated with pharmacological modulators of calcium channels and punches of dorsal striatum were immunoblotted for CaMKII Thr286 autophosphorylation as an index of CaMKII activation. KCl depolarization increased levels of CaMKII autophosphorylation ~2-fold; this increase was blocked by an LTCC antagonist and was mimicked by treatment with pharmacological LTCC activators. The chelation of extracellular calcium robustly decreased basal CaMKII autophosphorylation within 5min and increased levels of total CaMKII in cytosolic fractions, in addition to decreasing the phosphorylation of CaMKII sites in the GluN2B subunit of NMDA receptors and the GluA1 subunit of AMPA receptors. We also found that the maintenance of basal levels of CaMKII autophosphorylation requires low-voltage gated T-type calcium channels, but not LTCCs or R-type calcium channels. Our findings indicate that CaMKII activity is dynamically regulated by multiple calcium channels in the striatum thus coupling calcium entry to key downstream substrates.
Copyright © 2015 Elsevier Inc. All rights reserved.
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20 MeSH Terms
Overnutrition induces β-cell differentiation through prolonged activation of β-cells in zebrafish larvae.
Li M, Maddison LA, Page-McCaw P, Chen W
(2014) Am J Physiol Endocrinol Metab 306: E799-807
MeSH Terms: Animals, Animals, Genetically Modified, Calcium Channels, L-Type, Cell Count, Cell Differentiation, Disease Models, Animal, Embryo, Nonmammalian, Glucokinase, Insulin-Secreting Cells, KATP Channels, Larva, Membrane Potentials, Overnutrition, Potassium Channels, Inwardly Rectifying, Zebrafish
Show Abstract · Added April 24, 2014
Insulin from islet β-cells maintains glucose homeostasis by stimulating peripheral tissues to remove glucose from circulation. Persistent elevation of insulin demand increases β-cell number through self-replication or differentiation (neogenesis) as part of a compensatory response. However, it is not well understood how a persistent increase in insulin demand is detected. We have previously demonstrated that a persistent increase in insulin demand by overnutrition induces compensatory β-cell differentiation in zebrafish. Here, we use a series of pharmacological and genetic analyses to show that prolonged stimulation of existing β-cells is necessary and sufficient for this compensatory response. In the absence of feeding, tonic, but not intermittent, pharmacological activation of β-cell secretion was sufficient to induce β-cell differentiation. Conversely, drugs that block β-cell secretion, including an ATP-sensitive potassium (K ATP) channel agonist and an L-type Ca(2+) channel blocker, suppressed overnutrition-induced β-cell differentiation. Genetic experiments specifically targeting β-cells confirm existing β-cells as the overnutrition sensor. First, inducible expression of a constitutively active K ATP channel in β-cells suppressed the overnutrition effect. Second, inducible expression of a dominant-negative K ATP mutant induced β-cell differentiation independent of nutrients. Third, sensitizing β-cell metabolism by transgenic expression of a hyperactive glucokinase potentiated differentiation. Finally, ablation of the existing β-cells abolished the differentiation response. Taken together, these data establish that overnutrition induces β-cell differentiation in larval zebrafish through prolonged activation of β-cells. These findings demonstrate an essential role for existing β-cells in sensing overnutrition and compensating for their own insufficiency by recruiting additional β-cells.
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15 MeSH Terms
Genetic interactions found between calcium channel genes modulate amyloid load measured by positron emission tomography.
Koran ME, Hohman TJ, Thornton-Wells TA
(2014) Hum Genet 133: 85-93
MeSH Terms: Aged, Aged, 80 and over, Alzheimer Disease, Amyloid beta-Peptides, Apolipoprotein E4, Brain, Calcium Channels, L-Type, Chromosome Mapping, Epistasis, Genetic, Female, Genotype, Homeostasis, Humans, Male, Polymorphism, Single Nucleotide, Positron-Emission Tomography, Reproducibility of Results, Ryanodine Receptor Calcium Release Channel
Show Abstract · Added December 10, 2014
Late-onset Alzheimer's disease (LOAD) is known to have a complex, oligogenic etiology, with considerable genetic heterogeneity. We investigated the influence of genetic interactions between genes in the Alzheimer's disease (AD) pathway on amyloid-beta (Aβ) deposition as measured by PiB or AV-45 ligand positron emission tomography (PET) to aid in understanding LOAD's genetic etiology. Subsets of the Alzheimer's Disease Neuroimaging Initiative (ADNI) cohorts were used for discovery and for two independent validation analyses. A significant interaction between RYR3 and CACNA1C was confirmed in all three of the independent ADNI datasets. Both genes encode calcium channels expressed in the brain. The results shown here support previous animal studies implicating interactions between these calcium channels in amyloidogenesis and suggest that the pathological cascade of this disease may be modified by interactions in the amyloid-calcium axis. Future work focusing on the mechanisms of such relationships may inform targets for clinical intervention.
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18 MeSH Terms
Inhibition of the late sodium current slows t-tubule disruption during the progression of hypertensive heart disease in the rat.
Aistrup GL, Gupta DK, Kelly JE, O'Toole MJ, Nahhas A, Chirayil N, Misener S, Beussink L, Singh N, Ng J, Reddy M, Mongkolrattanothai T, El-Bizri N, Rajamani S, Shryock JC, Belardinelli L, Shah SJ, Wasserstrom JA
(2013) Am J Physiol Heart Circ Physiol 305: H1068-79
MeSH Terms: Acetanilides, Animals, Calcium Channels, L-Type, Calcium Signaling, Disease Models, Animal, Disease Progression, Dose-Response Relationship, Drug, Heart Failure, Hypertension, Hypertrophy, Left Ventricular, Male, Myocytes, Cardiac, NAV1.5 Voltage-Gated Sodium Channel, Piperazines, Ranolazine, Rats, Rats, Inbred SHR, Ryanodine Receptor Calcium Release Channel, Sarcoplasmic Reticulum Calcium-Transporting ATPases, Sodium, Sodium Channel Blockers, Sodium Channels, Sodium-Calcium Exchanger, Time Factors, Ultrasonography
Show Abstract · Added February 28, 2014
The treatment of heart failure (HF) is challenging and morbidity and mortality are high. The goal of this study was to determine if inhibition of the late Na(+) current with ranolazine during early hypertensive heart disease might slow or stop disease progression. Spontaneously hypertensive rats (aged 7 mo) were subjected to echocardiographic study and then fed either control chow (CON) or chow containing 0.5% ranolazine (RAN) for 3 mo. Animals were then restudied, and each heart was removed for measurements of t-tubule organization and Ca(2+) transients using confocal microscopy of the intact heart. RAN halted left ventricular hypertrophy as determined from both echocardiographic and cell dimension (length but not width) measurements. RAN reduced the number of myocytes with t-tubule disruption and the proportion of myocytes with defects in intracellular Ca(2+) cycling. RAN also prevented the slowing of the rate of restitution of Ca(2+) release and the increased vulnerability to rate-induced Ca(2+) alternans. Differences between CON- and RAN-treated animals were not a result of different expression levels of voltage-dependent Ca(2+) channel 1.2, sarco(endo)plasmic reticulum Ca(2+)-ATPase 2a, ryanodine receptor type 2, Na(+)/Ca(2+) exchanger-1, or voltage-gated Na(+) channel 1.5. Furthermore, myocytes with defective Ca(2+) transients in CON rats showed improved Ca(2+) cycling immediately upon acute exposure to RAN. Increased late Na(+) current likely plays a role in the progression of cardiac hypertrophy, a key pathological step in the development of HF. Early, chronic inhibition of this current slows both hypertrophy and development of ultrastructural and physiological defects associated with the progression to HF.
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25 MeSH Terms
L-type calcium channels play a critical role in maintaining lens transparency by regulating phosphorylation of aquaporin-0 and myosin light chain and expression of connexins.
Maddala R, Nagendran T, de Ridder GG, Schey KL, Rao PV
(2013) PLoS One 8: e64676
MeSH Terms: Animals, Aquaporins, Calcium Channel Blockers, Calcium Channels, L-Type, Connexins, Eye Proteins, Felodipine, Female, Gene Expression, Immunoblotting, Lens, Crystalline, Male, Mice, Mice, Inbred C57BL, Myosin Light Chains, Nifedipine, Phosphorylation, Reverse Transcriptase Polymerase Chain Reaction, beta-Crystallin B Chain
Show Abstract · Added May 27, 2014
Homeostasis of intracellular calcium is crucial for lens cytoarchitecture and transparency, however, the identity of specific channel proteins regulating calcium influx within the lens is not completely understood. Here we examined the expression and distribution profiles of L-type calcium channels (LTCCs) and explored their role in morphological integrity and transparency of the mouse lens, using cDNA microarray, RT-PCR, immunoblot, pharmacological inhibitors and immunofluorescence analyses. The results revealed that Ca (V) 1.2 and 1.3 channels are expressed and distributed in both the epithelium and cortical fiber cells in mouse lens. Inhibition of LTCCs with felodipine or nifedipine induces progressive cortical cataract formation with time, in association with decreased lens weight in ex-vivo mouse lenses. Histological analyses of felodipine treated lenses revealed extensive disorganization and swelling of cortical fiber cells resembling the phenotype reported for altered aquaporin-0 activity without detectable cytotoxic effects. Analysis of both soluble and membrane rich fractions from felodipine treated lenses by SDS-PAGE in conjunction with mass spectrometry and immunoblot analyses revealed decreases in β-B1-crystallin, Hsp-90, spectrin and filensin. Significantly, loss of transparency in the felodipine treated lenses was preceded by an increase in aquaporin-0 serine-235 phosphorylation and levels of connexin-50, together with decreases in myosin light chain phosphorylation and the levels of 14-3-3ε, a phosphoprotein-binding regulatory protein. Felodipine treatment led to a significant increase in gene expression of connexin-50 and 46 in the mouse lens. Additionally, felodipine inhibition of LTCCs in primary cultures of mouse lens epithelial cells resulted in decreased intracellular calcium, and decreased actin stress fibers and myosin light chain phosphorylation, without detectable cytotoxic response. Taken together, these observations reveal a crucial role for LTCCs in regulation of expression, activity and stability of aquaporin-0, connexins, cytoskeletal proteins, and the mechanical properties of lens, all of which have a vital role in maintaining lens function and cytoarchitecture.
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19 MeSH Terms