Acidic protein found in SARCOPLASMIC RETICULUM that binds calcium to the extent of 700-900 nmoles/mg. It plays the role of sequestering calcium transported to the interior of the intracellular vesicle.
A network of tubules and sacs in the cytoplasm of SKELETAL MUSCLE FIBERS that assist with muscle contraction and relaxation by releasing and storing calcium ions.
The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.
Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.
A tetrameric calcium release channel in the SARCOPLASMIC RETICULUM membrane of SMOOTH MUSCLE CELLS, acting oppositely to SARCOPLASMIC RETICULUM CALCIUM-TRANSPORTING ATPASES. It is important in skeletal and cardiac excitation-contraction coupling and studied by using RYANODINE. Abnormalities are implicated in CARDIAC ARRHYTHMIAS and MUSCULAR DISEASES.
A multifunctional protein that is found primarily within membrane-bound organelles. In the ENDOPLASMIC RETICULUM it binds to specific N-linked oligosaccharides found on newly-synthesized proteins and functions as a MOLECULAR CHAPERONE that may play a role in PROTEIN FOLDING or retention and degradation of misfolded proteins. In addition calreticulin is a major storage form for CALCIUM and functions as a calcium-signaling molecule that can regulate intracellular calcium HOMEOSTASIS.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
5,5'-Nitrilodibarbituric acid ammonium derivative. Used as an indicator for complexometric titrations.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
Cation-transporting proteins that utilize the energy of ATP hydrolysis for the transport of CALCIUM. They differ from CALCIUM CHANNELS which allow calcium to pass through a membrane without the use of energy.
The muscle tissue of the HEART. It is composed of striated, involuntary muscle cells (MYOCYTES, CARDIAC) connected to form the contractile pump to generate blood flow.
Contractile tissue that produces movement in animals.
Widely distributed enzymes that carry out oxidation-reduction reactions in which one atom of the oxygen molecule is incorporated into the organic substrate; the other oxygen atom is reduced and combined with hydrogen ions to form water. They are also known as monooxygenases or hydroxylases. These reactions require two substrates as reductants for each of the two oxygen atoms. There are different classes of monooxygenases depending on the type of hydrogen-providing cosubstrate (COENZYMES) required in the mixed-function oxidation.
A subtype of striated muscle, attached by TENDONS to the SKELETON. Skeletal muscles are innervated and their movement can be consciously controlled. They are also called voluntary muscles.
Signal transduction mechanisms whereby calcium mobilization (from outside the cell or from intracellular storage pools) to the cytoplasm is triggered by external stimuli. Calcium signals are often seen to propagate as waves, oscillations, spikes, sparks, or puffs. The calcium acts as an intracellular messenger by activating calcium-responsive proteins.
Calcium-transporting ATPases that catalyze the active transport of CALCIUM into the SARCOPLASMIC RETICULUM vesicles from the CYTOPLASM. They are primarily found in MUSCLE CELLS and play a role in the relaxation of MUSCLES.
Unsaturated azacyclopropane compounds that are three-membered heterocycles of a nitrogen and two carbon atoms.
Red dye, pH indicator, and diagnostic aid for determination of renal function. It is used also for studies of the gastrointestinal and other systems.
An abnormally rapid ventricular rhythm usually in excess of 150 beats per minute. It is generated within the ventricle below the BUNDLE OF HIS, either as autonomic impulse formation or reentrant impulse conduction. Depending on the etiology, onset of ventricular tachycardia can be paroxysmal (sudden) or nonparoxysmal, its wide QRS complexes can be uniform or polymorphic, and the ventricular beating may be independent of the atrial beating (AV dissociation).
The domestic dog, Canis familiaris, comprising about 400 breeds, of the carnivore family CANIDAE. They are worldwide in distribution and live in association with people. (Walker's Mammals of the World, 5th ed, p1065)
Disorders characterized by abnormal proliferation of primary cells of the immune system or by excessive production of immunoglobulins.
A heterogeneous group of inherited MYOPATHIES, characterized by wasting and weakness of the SKELETAL MUSCLE. They are categorized by the sites of MUSCLE WEAKNESS; AGE OF ONSET; and INHERITANCE PATTERNS.
A heterogenous group of inherited muscular dystrophy that can be autosomal dominant or autosomal recessive. There are many forms (called LGMDs) involving genes encoding muscle membrane proteins such as the sarcoglycan (SARCOGLYCANS) complex that interacts with DYSTROPHIN. The disease is characterized by progressing wasting and weakness of the proximal muscles of arms and legs around the HIPS and SHOULDERS (the pelvic and shoulder girdles).
Large, multinucleate single cells, either cylindrical or prismatic in shape, that form the basic unit of SKELETAL MUSCLE. They consist of MYOFIBRILS enclosed within and attached to the SARCOLEMMA. They are derived from the fusion of skeletal myoblasts (MYOBLASTS, SKELETAL) into a syncytium, followed by differentiation.
Glycoprotein molecules on the surface of cells that react with or bind to laminin whose function allows the binding of epithelial cells to the basement membrane. The molecular weight of this high-affinity receptor is 67 kD.
Large, noncollagenous glycoprotein with antigenic properties. It is localized in the basement membrane lamina lucida and functions to bind epithelial cells to the basement membrane. Evidence suggests that the protein plays a role in tumor invasion.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Dystrophin-associated proteins that play role in the formation of a transmembrane link between laminin-2 and DYSTROPHIN. Both the alpha and the beta subtypes of dystroglycan originate via POST-TRANSLATIONAL PROTEIN PROCESSING of a single precursor protein.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The voltage differences across a membrane. For cellular membranes they are computed by subtracting the voltage measured outside the membrane from the voltage measured inside the membrane. They result from differences of inside versus outside concentration of potassium, sodium, chloride, and other ions across cells' or ORGANELLES membranes. For excitable cells, the resting membrane potentials range between -30 and -100 millivolts. Physical, chemical, or electrical stimuli can make a membrane potential more negative (hyperpolarization), or less negative (depolarization).
Property of membranes and other structures to permit passage of light, heat, gases, liquids, metabolites, and mineral ions.
Any technique by which an unknown color is evaluated in terms of standard colors. The technique may be visual, photoelectric, or indirect by means of spectrophotometry. It is used in chemistry and physics. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Abnormally high level of calcium in the blood.
A yellow metallic element with the atomic symbol Au, atomic number 79, and atomic weight 197. It is used in jewelry, goldplating of other metals, as currency, and in dental restoration. Many of its clinical applications, such as ANTIRHEUMATIC AGENTS, are in the form of its salts.
A condition of abnormally elevated output of PARATHYROID HORMONE due to parathyroid HYPERPLASIA or PARATHYROID NEOPLASMS. It is characterized by the combination of HYPERCALCEMIA, phosphaturia, elevated renal 1,25-DIHYDROXYVITAMIN D3 synthesis, and increased BONE RESORPTION.
A condition of abnormally elevated output of PARATHYROID HORMONE (or PTH) triggering responses that increase blood CALCIUM. It is characterized by HYPERCALCEMIA and BONE RESORPTION, eventually leading to bone diseases. PRIMARY HYPERPARATHYROIDISM is caused by parathyroid HYPERPLASIA or PARATHYROID NEOPLASMS. SECONDARY HYPERPARATHYROIDISM is increased PTH secretion in response to HYPOCALCEMIA, usually caused by chronic KIDNEY DISEASES.
An interdisciplinary field in materials science, ENGINEERING, and BIOLOGY, studying the use of biological principles for synthesis or fabrication of BIOMIMETIC MATERIALS.
An antilipemic agent which lowers cholesterol, triglycerides, serum beta-lipoproteins and phospholipids. It acts by interfering with the enzymatic steps involved in the conversion of acetate to hydroxymethylglutaryl coenzyme A as well as inhibiting the activity of HYDROXYMETHYLGLUTARYL COA REDUCTASES which is the rate limiting enzyme in the biosynthesis of cholesterol.
Pricing statements presented by more than one party for the purpose of securing a contract.
The relationship between the dose of an administered drug and the response of the organism to the drug.
A methylpyrrole-carboxylate from RYANIA that disrupts the RYANODINE RECEPTOR CALCIUM RELEASE CHANNEL to modify CALCIUM release from SARCOPLASMIC RETICULUM resulting in alteration of MUSCLE CONTRACTION. It was previously used in INSECTICIDES. It is used experimentally in conjunction with THAPSIGARGIN and other inhibitors of CALCIUM ATPASE uptake of calcium into SARCOPLASMIC RETICULUM.
Voltage-dependent cell membrane glycoproteins selectively permeable to calcium ions. They are categorized as L-, T-, N-, P-, Q-, and R-types based on the activation and inactivation kinetics, ion specificity, and sensitivity to drugs and toxins. The L- and T-types are present throughout the cardiovascular and central nervous systems and the N-, P-, Q-, & R-types are located in neuronal tissue.
A glucocorticoid given orally, parenterally, by local injection, by inhalation, or applied topically in the management of various disorders in which corticosteroids are indicated. Its lack of mineralocorticoid properties makes betamethasone particularly suitable for treating cerebral edema and congenital adrenal hyperplasia. (From Martindale, The Extra Pharmacopoeia, 30th ed, p724)
A group of CORTICOSTEROIDS that affect carbohydrate metabolism (GLUCONEOGENESIS, liver glycogen deposition, elevation of BLOOD SUGAR), inhibit ADRENOCORTICOTROPIC HORMONE secretion, and possess pronounced anti-inflammatory activity. They also play a role in fat and protein metabolism, maintenance of arterial blood pressure, alteration of the connective tissue response to injury, reduction in the number of circulating lymphocytes, and functioning of the central nervous system.
An anti-inflammatory 9-fluoro-glucocorticoid.
The consequences of exposing the FETUS in utero to certain factors, such as NUTRITION PHYSIOLOGICAL PHENOMENA; PHYSIOLOGICAL STRESS; DRUGS; RADIATION; and other physical or chemical factors. These consequences are observed later in the offspring after BIRTH.
Cytoplasmic proteins that specifically bind glucocorticoids and mediate their cellular effects. The glucocorticoid receptor-glucocorticoid complex acts in the nucleus to induce transcription of DNA. Glucocorticoids were named for their actions on blood glucose concentration, but they have equally important effects on protein and fat metabolism. Cortisol is the most important example.
Skeletal muscle fibers characterized by their expression of the Type I MYOSIN HEAVY CHAIN isoforms which have low ATPase activity and effect several other functional properties - shortening velocity, power output, rate of tension redevelopment.
Skeletal muscle fibers characterized by their expression of the Type II MYOSIN HEAVY CHAIN isoforms which have high ATPase activity and effect several other functional properties - shortening velocity, power output, rate of tension redevelopment. Several fast types have been identified.
Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.
A disorder characterized by muscle twitches, cramps, and carpopedal spasm, and when severe, laryngospasm and seizures. This condition is associated with unstable depolarization of axonal membranes, primarily in the peripheral nervous system. Tetany usually results from HYPOCALCEMIA or reduced serum levels of MAGNESIUM that may be associated with HYPERVENTILATION; HYPOPARATHYROIDISM; RICKETS; UREMIA; or other conditions. (From Adams et al., Principles of Neurology, 6th ed, p1490)

Serial changes in sarcoplasmic reticulum gene expression in volume-overloaded cardiac hypertrophy in the rat: effect of an angiotensin II receptor antagonist. (1/309)

This study was designed to clarify whether gene expression in the cardiac sarcoplasmic reticulum [sarcoplasmic reticulum Ca2+-ATPase (SERCA), phospholamban, ryanodine receptor and calsequestrin] changes in accordance with left ventricular functional alterations in the volume-overloaded heart. Further, the effect of the angiotensin II type 1 receptor antagonist, TCV-116, on the expression of these genes was also evaluated. Left ventricular fractional shortening was significantly increased at 7 days, had returned to control levels at 21 days, and had significantly decreased at 35 days after the shunt operation, compared with sham-operated rats. The level of SERCA mRNA was significantly decreased at both 21 days and 35 days after the shunt operation. The levels of ryanodine receptor and phospholamban mRNAs were significantly decreased at 35 days in shunt-operated rats. The decrease in the SERCA mRNA level preceded the development of cardiac dysfunction. The levels of SERCA and ryanodine receptor mRNAs were correlated positively with left ventricular fractional shortening (r=0.73, P<0.0001 and r=0.61, P<0.01 respectively). Attenuation of the decrease in left ventricular fractional shortening occurred on treatment with TCV-116. After the treatment with TCV-116, the levels of SERCA and phospholamban mRNAs were restored to the respective values in sham-operated rats. Ryanodine receptor mRNA levels remained unchanged after treatment with TCV-116. These results indicate that the down-regulation of SERCA and ryanodine receptor mRNA levels may be related to cardiac dysfunction in the volume-overloaded heart. In addition, treatment with an angiotensin II receptor antagonist may restore the altered sarcoplasmic reticulum mRNA levels to control levels, and this may result in attenuation of the functional impairment in the volume-overloaded heart.  (+info)

Down-regulation of L-type calcium channel and sarcoplasmic reticular Ca(2+)-ATPase mRNA in human atrial fibrillation without significant change in the mRNA of ryanodine receptor, calsequestrin and phospholamban: an insight into the mechanism of atrial electrical remodeling. (2/309)

OBJECTIVES: We investigated the gene expression of calcium-handling genes including L-type calcium channel, sarcoplasmic reticular calcium adenosine triphosphatase (Ca(2+)-ATPase), ryanodine receptor, calsequestrin and phospholamban in human atrial fibrillation. BACKGROUND: Recent studies have demonstrated that atrial electrical remodeling in atrial fibrillation is associated with intracellular calcium overload. However, the changes of calcium-handling proteins remain unclear. METHODS: A total of 34 patients undergoing open heart surgery were included. Atrial tissue was obtained from the right atrial free wall, right atrial appendage, left atrial free wall and left atrial appendage, respectively. The messenger ribonucleic acid (mRNA) amount of the genes was measured by reverse transcription-polymerase chain reaction and normalized to the mRNA levels of glyceraldehyde 3-phosphate dehydrogenase. RESULTS: The mRNA of L-type calcium channel and of Ca(2+)-ATPase was significantly decreased in patients with persistent atrial fibrillation for more than 3 months (0.36+/-0.26 vs. 0.90+/-0.88 for L-type calcium channel; 0.69+/-0.42 vs. 1.21+/-0.68 for Ca(2+)-ATPase; both p < 0.05, all data in arbitrary unit). We further demonstrated that there was no spatial dispersion of the gene expression among the four atrial tissue sampling sites. Age, gender and underlying cardiac disease had no significant effects on the gene expression. In contrast, the mRNA levels of ryanodine receptor, calsequestrin and phospholamban showed no significant change in atrial fibrillation. CONCLUSIONS: L-type calcium channel and the sarcoplasmic reticular Ca(2+)-ATPase gene were down-regulated in atrial fibrillation. These changes may be a consequence of, as well as a contributory factor for, atrial fibrillation.  (+info)

Reduced sodium pump alpha1, alpha3, and beta1-isoform protein levels and Na+,K+-ATPase activity but unchanged Na+-Ca2+ exchanger protein levels in human heart failure. (3/309)

BACKGROUND: Cardiac glycosides initiate an increase in force of contraction by inhibiting the sarcolemmal sodium pump (Na+, K+-ATPase), thereby decreasing Ca2+ extrusion by the Na+-Ca2+ exchanger, which increases the cellular content of Ca2+. In patients with heart failure the sensitivity toward cardiac glycosides is enhanced. METHODS AND RESULTS: Because the inotropic effect of cardiac glycosides may be a function of the sodium pump and Na+-Ca2+ exchanger (NCE) expression levels, the present study aimed to investigate protein expression of both transporters (immunoblot with specific antibodies against the sodium pump catalytic alpha1-, alpha2-, alpha3-, and glycoprotein beta1-isoforms and against NCE) in left ventricle from failing (heart transplantations, New York Heart Association class IV, n=21) compared with nonfailing (donor hearts, NF, n=22) human myocardium. The density of 3H-ouabain-binding sites (Bmax) and the Na+,K+-ATPase activity were also measured. In NYHA class IV, protein levels of Na+,K+-ATPase alpha1- (0.62+/-0.06 of control), alpha3- (0.70+/-0.09), and beta1- (0.61+/-0.04) but not alpha2-isoforms were significantly reduced (P<0.01), whereas levels of NCE (0.92+/-0.13 of control) and calsequestrin (0.98+/-0.06) remained unchanged. Both Na+,K+-ATPase activity (NF: 1.9+/-0.29; NYHA class IV: 1.1+/-0.17 micromol ATP/min per milligram of protein) and the 3H-ouabain binding sites (Bmax NF: 15.9+/-1.9 pmol/mg protein; NYHA class IV: 9.7+/-1.5) were reduced in NYHA class IV and correlated significantly to each other (r2=0. 73; P<0.0001), as did beta1-subunit expression. In left ventricular papillary muscle strips from NYHA class IV compared with nonfailing tissue the Na+-channel modulator BDF 9198 exerted an increase in force of contraction with unchanged effectiveness but enhanced potency. CONCLUSIONS: The enhanced sensitivity of failing human myocardium toward cardiac glycosides may be, at least in part, attributed to a reduced protein expression and activity of the sarcolemmal Na+,K+-ATPase without a change in Na+-Ca2+ exchanger protein expression.  (+info)

Analysis of calsequestrin gene expression using green fluorescent protein in Caenorhabditis elegans. (4/309)

The calsequestrin gene of Caenorhabditis elegans is expressed in body-wall muscle cells during muscle development. In order to study the body-wall muscle specific regulation of the calsequestrin gene expression, approximately 2 kb upstream sequences of the calsequestrin gene were analyzed. Transcriptional fusion constructs utilizing green fluorescent protein as a reporter gene were made and microinjected to produce germ-line transformed transgenic C. elegans. The expression of green fluorescent protein was observed in the body-wall muscles of live transgenic animals under fluorescence microscopy. Deletion analyses of upstream sequences have revealed a putative promoter sequence and a regulatory element which appeared to enhance reporter gene expression. Both sequence elements are juxtaposed to constitute a 260 bp regulatory region approximately 260 bp upstream from the putative translational initiation codon. Several possible binding sites for transcription factors were identified including the sites for YY1 and NF-W2, a muscle specific zinc finger transcription factor, and an ubiquitous enhancer binding protein, respectively. Interestingly, this region also contains a 20 bp sequence element identical to those found in the mouse dystrophin gene, which suggests a possible role of this regulatory region in muscle specific gene regulation.  (+info)

Subunit expression of the cardiac L-type calcium channel is differentially regulated in diastolic heart failure of the cardiac allograft. (5/309)

BACKGROUND: Left ventricular diastolic dysfunction is a major cause of cardiac allograft failure. Multimeric L-type calcium channels (alpha1-, alpha2/delta-, and beta-subunits) are essential for excitation/contraction coupling in the heart. Their gene expression was studied in allografts that developed diastolic heart failure. METHODS AND RESULTS: mRNA levels of calcium channel subunits were measured by competitive reverse transcriptase-polymerase chain reaction in microbiopsy samples from the interventricular septum. Size and tissue variabilities between biopsy samples were assessed by determination of cardiac calsequestrin mRNA levels. In the cardiac allografts studied, mRNA levels in microbiopsy samples were considered to represent left ventricular gene expression, because septal and left ventricular gene expression in Northern blots was equivalent, and left ventricles contracted homogeneously. Biopsy samples (n=72) were taken from allografts with normal left ventricular end-diastolic pressure (LVEDP; 8 to 13 mm Hg; n=30), moderately elevated LVEDP (14 to 18 mm Hg; n=26), and elevated LVEDP (19 to 28 mm Hg; n=16). Increased LVEDP was related to slowed diastolic relaxation determined by the time constant tau (r2=0.86), whereas systolic performance (dP/dt; ejection fraction) was preserved. With increasing LVEDP, mRNA levels of the pore-forming alpha1c-subunit (n=15) and of the regulatory alpha2/delta-subunit (n=17) remained unchanged but decreased exponentially (r2=-0.83) for the regulatory beta-subunit (n=40). Compared with cardiac allografts with normal LVEDP (n=15), beta-subunit mRNA level was reduced by 75% at elevated LVEDP (n=9; P=0.012). In an explanted, diastolically failing cardiac allograft, beta-subunit expression was reduced correspondingly by 72% and 76% on the mRNA level in septal and left ventricular myocardium and by 80% on the protein level. CONCLUSIONS: The downregulated expression of the calcium channel beta-subunit might contribute to altered calcium handling in diastolically failing cardiac allografts.  (+info)

Defective beta-adrenergic receptor signaling precedes the development of dilated cardiomyopathy in transgenic mice with calsequestrin overexpression. (6/309)

Calsequestrin is a high capacity Ca(2+)-binding protein in the junctional sarcoplasmic reticulum that forms a quaternary complex with junctin, triadin, and the ryanodine receptor. Transgenic mice with cardiac-targeted calsequestrin overexpression show marked suppression of Ca(2+)-induced Ca(2+) release, myocyte hypertrophy, and premature death by 16 weeks of age (Jones, L. R., Suzuki, Y. J., Wang, W., Kobayashi, Y. M., Ramesh, V., Franzini-Armstrong, C., Cleemann, L., and Morad, M. (1998) J. Clin. Invest. 101, 1385-1393). To investigate whether alterations in intracellular Ca(2+) trigger changes in the beta-adrenergic receptor pathway, we studied calsequestrin overexpressing transgenic mice at 7 and 14 weeks of age. As assessed by echocardiography, calsequestrin mice at 7 weeks showed mild left ventricular enlargement, mild decreased fractional shortening with increased wall thickness. By 14 weeks, the phenotype progressed to marked left ventricular enlargement and severely depressed systolic function. Cardiac catheterization in calsequestrin mice revealed markedly impaired beta-adrenergic receptor responsiveness in both 7- and 14- week mice. Biochemical analysis in 7- and 14-week mice showed a significant decrease in total beta-adrenergic receptor density, adenylyl cyclase activity, and the percent high affinity agonist binding, which was associated with increased beta-adrenergic receptor kinase 1 levels. Taken together, these data indicate that alterations in beta-adrenergic receptor signaling precede the development of overt heart failure in this mouse model of progressive cardiomyopathy.  (+info)

Characterization of the binding and phosphorylation of cardiac calsequestrin by epsilon protein kinase C. (7/309)

In this study, we report the cloning of the rat cardiac isoform of calsequestrin on the basis of its interaction with an epsilonprotein kinase C-unique sequence (epsilonV1) derived form the epsilonprotein kinase C regulatory domain. Calsequestrin binds activated epsilonprotein kinase C holoenzyme better than the inactive enzyme and nearly three times better than other protein kinase C isozymes. The interaction between epsilonprotein kinase C and calsequestrin is mediated by sequences in both the regulatory and kinase domains of the epsilonprotein kinase C. Finally, we show that calsequestrin is an epsilonprotein kinase C substrate in vitro and protein kinase C phosphorylation of calsequestrin leads to a decreased binding of epsilonprotein kinase C to calsequestrin.  (+info)

Heterogeneous transmural gene expression of calcium-handling proteins and natriuretic peptides in the failing human heart. (8/309)

OBJECTIVE: Human heart failure is associated with a disturbed intracellular calcium (Ca2+) homeostasis. In this regard, ventricular wall stress is considered to be a determinant for expression of sarcoplasmic reticulum Ca(2+)-ATPase (SERCA2a). In the present study, we analyzed the transmural protein and/or mRNA levels of SERCA2a, other Ca(2+)-handling proteins, and of atrial and brain natriuretic peptides (ANP and BNP) in the human heart. METHODS: Subepicardial (epi), midmyocardial (mid), and subendocardial (endo) sections of the left ventricular free wall from end-stage failing (n = 17) and nonfailing (n = 5) human hearts were analyzed by Western blot for immunoreactive protein levels of SERCA2a, phospholamban (PLN), and calsequestrin (CS). Subepi- and subendocardial sections were analyzed by Northern blot for steady-state mRNA levels of SERCA2a, Na(+)-Ca2+ exchanger (NCX1), ANP, and BNP. RESULTS: SERCA2a protein and mRNA levels were reduced by 40 +/- 5% (P < 0.01) and 25 +/- 7% (P < 0.05) in endo compared to epi in the failing heart and by 27 +/- 14% and 16 +/- 12% (non-significant) in the nonfailing heart, respectively. PLN protein levels were reduced by 23 +/- 6% (P < 0.05) in endo compared to epi in the failing heart and by 17 +/- 25% (non-significant) in the nonfailing heart, whereas CS protein levels and NCX1 mRNA levels were similar across the left ventricular wall. Strikingly, in the failing heart, both BNP and ANP mRNA levels were upregulated predominantly in endo. CONCLUSIONS: In the failing human heart, SERCA2a and PLN, as well as natriuretic peptides but not CS and NCX1 are differentially expressed across the left ventricular wall, implicating (1) different susceptibility of subendocardium and subepicardium to factors affecting expression of these proteins and (2) differences in regulation of the distinct calcium-cycling proteins.  (+info)

Overexpression of the conserved Ca2+-binding proteins calreticulin and calsequestrin impairs cardiac function, leading to premature death. Calreticulin is vital for embryonic development, but also impairs glucocorticoid action. Glucocorticoid overexposure during late fetal life causes intra-uterine growth retardation and programmed hypertension in adulthood. To determine whether intra-uterine growth retardation or programmed hypertension was associated with altered calreticulin or calsequestrin expression, effects of prenatal glucocorticoid overexposure (maternal dexamethasone treatment on days 15-21 of pregnancy) were examined during fetal life and postnatal development until adulthood (24 weeks). Dexamethasone (100 or 200μg/kg of maternal body weight) was administered via osmotic pump. Calreticulin was detected as a 55kDa band and calsequestrin as 55 and 63kDa bands in 21 day fetal hearts. Only the 55kDa calsequestrin band was detected postnatally. Prenatal glucocorticoid overexposure at the ...
Calsequestrin is the principal calcium-binding protein present in the sarcoplasmic reticulum of cardiac and skeletal muscle [(PUBMED:3379055)]. It is a highly acidic protein that is able to bind over 40 calcium ions and acts as an internal calcium store in muscle. Sequence analysis has suggested that calcium is not bound in distinct pockets via EF-hand motifs, but rather via presentation of a charged protein surface. Two forms of calsequestrin have been identified. The cardiac form is present in cardiac and slow skeletal muscle and the fast skeletal form is found in fast skeletal muscle. The release of calsequestrin-bound calcium (through a a calcium release channel) triggers muscle contraction. The active protein is not highly structured, more than 50% of it adopting a random coil conformation [(PUBMED:3427023)]. When calcium binds there is a structural change whereby the alpha-helical content of the protein increases from 3 to 11% [(PUBMED:3427023)]. Both forms of calsequestrin are ...
TY - JOUR. T1 - Casq2 deletion causes sarcoplasmic reticulum volume increase, premature Ca2+ release, and catecholaminergic polymorphic ventricular tachycardia. AU - Knollmann, Björn C.. AU - Chopra, Nagesh. AU - Hlaing, Thinn. AU - Akin, Brandy. AU - Yang, Tao. AU - Ettensohn, Kristen. AU - Knollmann, Barbara E.C.. AU - Horton, Kenneth D.. AU - Weissman, Neil J.. AU - Holinstat, Izabela. AU - Zhang, Wei. AU - Roden, Dan M.. AU - Jones, Larry R.. AU - Franzini-Armstrong, Clara. AU - Pfeifer, Karl. PY - 2006/9/1. Y1 - 2006/9/1. N2 - Cardiac calsequestrin (Casq2) is thought to be the key sarcoplasmic reticulum (SR) Ca2+ storage protein essential for SR Ca2+ release in mammalian heart. Human CASQ2 mutations are associated with catecholaminergic ventricular tachycardia. However, homozygous mutation carriers presumably lacking functional Casq2 display surprisingly normal cardiac contractility. Here we show that Casq2-null mice are viable and display normal SR Ca2+ release and contractile function ...
1SJI: Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerization.
rat calsequestrin protein: amino acid sequence given in first source; MW 56-66 kDa; a major skeletal muscle laminin binding protein
We showed that CSQ2-associated RyR2 channels, activated by 1 μM cytosolic Ca2+, were sensitive to luminal Ca2+. They were not sensitive to changes in luminal Mg2+. Thus, the CSQ2-dependent luminal RyR2 Ca2+ regulation mechanism distinguishes between these ions. It does not require the presence of another cytosolic activator (ATP or sulmazole). It does not require the presence of additional free CSQ2 in the luminal bath as illustrated by Fig. 1 B (filled circles) where regulation occurs with no unbound CSQ2 in the lumenal bath. This means CSQ2-dependent regulation does not involve CSQ2 association/dissociation and that made it impractical to define the CSQ2 dose dependency. We considered examining the dose dependency of CSQ2 reassociation over a set interval but the physiological importance of this parameter is not entirely clear. Instead, we simply elected to define function at a set bath CSQ2 concentration, a concentration like that used successfully by other groups (Gyorke et al., 2004; Beard ...
Triadin, also known as TRDN, is a human gene associated with the release of Calcium ions from the sarcoplasmic reticulum triggering muscular contraction through calcium-induced calcium release. Triadin is a multiprotein family, arising from different processing of the TRDN gene on chromosome 6. It is a transmembrane protein on the sarcoplasmic reticulum due to a well defined hydrophobic section and it forms a quaternary complex with the cardiac Ryanodine receptor (RYR2), calsequestrin (CASQ2) and junctin proteins. The luminal (inner compartment of the sarcoplasmic reticulum) section of Triadin has areas of highly charged amino acid residues that act as luminal Ca2+ receptors. Triadin is also able to sense luminal Ca2+ concentrations by mediating interactions between RYR2 and CASQ2. Triadin has several different forms; Trisk 95 and Trisk 51, which are expressed in skeletal muscle, and Trisk 32 (CT1), which is mainly expressed in cardiac muscle. TRDN has been shown to interact with RYR1. Triadin ...
The mechanisms that terminate \(Ca^{2+}\) release from the sarcoplasmic reticulum are not fully understood. D4cpv-Casq1 (Sztretye et al. 2011. J. Gen. Physiol. doi:10.1085/jgp.201010591) was used in mouse skeletal muscle cells under voltage clamp to measure free \(Ca^{2+}\) concentration inside the sarcoplasmic reticulum (SR), \([Ca^{2+}]_{SR}\), simultaneously with that in the cytosol, \([Ca^{2+}]_c\), during the response to long-lasting depolarization of the plasma membrane. The ratio of \(Ca^{2+}\) release flux (derived from \([Ca^{2+}]_c(t)\)) over the gradient that drives it (essentially equal to \([Ca^{2+}]_{SR}\)) provided directly, for the first time, a dynamic measure of the permeability to \(Ca^{2+}\) of the releasing SR membrane. During maximal depolarization, flux rapidly rises to a peak and then decays. Before 0.5 s, \([Ca^{2+}]_{SR}\) stabilized at ~35% of its resting level; depletion was therefore incomplete. By 0.4 s of depolarization, the measured permeability decayed to ~10% of ...
Luminal Ca2+ regulation of RyR2 channels by the CSQ2-R33Q and CSQ2-L167H mutants. Mutant CSQ2 (0.5 μg/ml) was added to the luminal side of previously CSQ2-stri
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Catecholaminergic polymorphic ventricular tachycardia is characterized by polymorphic ventricular tachycardia in the structurally normal heart. It is typically triggered by physical activity, emotional stress or catecholamine infusion. Ventricular tachycardia can lead to dizziness, syncope, seizures, ventricular fibrillation and sudden death.. The Catecholaminergic polymorphic ventricular tachycardia NGS panel consists of nine genes: ANK2, CALM1, CALM2, CALM3, CASQ2, KCNJ2, RYR2, TECRL and TRDN.. Copy number variation (CNV) analysis of the catecholaminergic polymorphic ventricular tachycardia genes is also offered as a panel. Additionally, CTGT offers a comprehensive test (both NGS and CNV panels) for these genes. Panel genes are also offered as individual sequencing and deletion/duplication tests unless otherwise indicated.. ...
The following pages link to Catecholaminergic Polymorphic Ventricular Tachycardia: View (previous 50 , next 50) (20 , 50 , 100 , 250 , 500) ...
FRAP experiments revealed that the dynamics of GFP-SERCA2a, either when diffused throughout the SR or when localized near the Z disk, did not show any difference in the mobile fraction and the diffusion constant (Mf of 88.8% ± 9.1%, n = 16, and 93.2% ± 4.0%, n = 23; D of 0.22 ± 0.1 μm2/s and 0.20 ± 0.1 μm2/s, respectively), as shown in Fig. 2C. The diffusion constant of GFP-InsP3R1 was similar in undifferentiated and differentiated myotubes (D of 0.13 ± 0.07 μm2/s and 0.07 ± 0.05 μm2/s, respectively). However, the Mf of GFP-InsP3R1 was reduced from 79.1% ± 11.2% (n = 20) to 62.8% ± 11.3% (P ≤ 0.01, n = 14) when the protein was organized at the Z disk level (Fig. 2F). InsP3R1 has been described to associate with the actin cytoskeleton through its interaction with protein 4.1N (26, 27). Accordingly, a GFP-InsP3R1 construct missing the C-terminal 14 aa that are responsible for binding to protein 4.1N (28) was prepared (GFP-InsP3R1Δ14). In differentiated myotubes, the GFP-InsP3R1Δ14 ...
AAV serotype 9-based delivery of the SaCas9 system can efficiently disrupt a disease-causing allele in cardiomyocytes in vivo. This work highlights the potential of somatic genome editing approaches for the treatment of lethal autosomal-dominant inherited cardiac disorders, such as catecholaminergic …
On 24.05.2017 05:11, Assia Alexandrova wrote: [...] , Ok, so if I understand correctly from this and from some cursory , reading of the source code around JSR 223, the def keyword operates , within a lexical scope and that lexical scope must be completely known , in advance before the statement can be evaluated. There is no global , lexical scope (just like there isnt in Java) that one can operate , within in a REPL. However, there is a global dynamic scope that is , accessible by being careful to omit the def keyword (and I suppose , type names as well?). sounds about right... no type name either, yes. , I must admit I dont understand what the , semantics are, but as long as it makes some sense to Groovy users, , thats fine. I hope it does ;) [...] ,,, ,,, groovy:000, def x = 10; ,,, ,,, ===, 10 ,,, ,,, groovy:000, x ,,, ,,, Unknown property: x ,, ,, hmmm... strange... I have the vague memory that somebody already fixed ,, that... ah... right... this is JSR-223 not groovysh. For ...
Monoklonale und polyklonale CASQ2 Antikörper für viele Methoden. Ausgesuchte Qualitäts-Hersteller für CASQ2 Antikörper. Hier bestellen.
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Valle, G.; Vergani, B.; Sacchetto, R.; Reggiani, C.; De Rosa, E.; Maccatrozzo, L.; Nori, A.; Villa, A.; Volpe, P., 2017: Characterization of fast-twitch and slow-twitch skeletal muscles of calsequestrin 2 (CASQ2)-knock out mice: unexpected adaptive changes of fast-twitch muscles only
TY - JOUR. T1 - Calmodulin mutations causing catecholaminergic polymorphic ventricular tachycardia confer opposing functional and biophysical molecular changes. AU - Søndergaard, Mads T. AU - Sorensen, Anders B. AU - Skov, Louise L. AU - Kjaer-Sorensen, Kasper. AU - Bauer, Mikael C. AU - Nyegaard, Mette. AU - Linse, Sara. AU - Oxvig, Claus. AU - Overgaard, Michael Toft. N1 - This article is protected by copyright. All rights reserved.. PY - 2015/1/14. Y1 - 2015/1/14. U2 - 10.1111/febs.13184. DO - 10.1111/febs.13184. M3 - Journal article. C2 - 25557436. VL - 282. SP - 803. EP - 816. JO - F E B S Journal. JF - F E B S Journal. SN - 1742-464X. IS - 4. ER - ...
Cardiomyocytes (CMs) are nonregenerative. Self-renewable pluripotent human embryonic stem cells (hESCs) can differentiate into CMs for cell-based therapies. We recently reported that Ca2+ handling, crucial to excitation-contraction coupling of hESC-derived CMs (hESC-CMs), is functional but immature. Such immature properties as smaller cytosolic Ca2+ transient amplitudes, slower kinetics, and reduced Ca2+ content of sarcoplasmic reticulum (SR) can be attributed to the differential developmental expression profiles of specific Ca2+ handling and regulatory proteins in hESC-CMs and their adult counterparts. In particular, calsequestrin (CSQ), the most abundant, high-capacity but low-affinity, Ca2+-binding protein in the SR that is anchored to the ryanodine receptor, is robustly expressed in adult CMs but completely absent in hESC-CMs. Here we hypothesized that gene transfer of CSQ in hESC-CMs suffices to induce functional improvement of SR. Transduction of hESC-CMs by the recombinant adenovirus ...
Physical inactivity is associated with increased cardiovascular disease, obesity, type II diabetes and some types of cancers. Studies have shown that genetics play a significant role in the regulation of voluntary physical activity. However, these studies involve ad libitum access to wheel running, which may cause confounded results due to a training effect, especially in inherently high active animals. This study investigated the levels of gene expression of four potential candidate genes that have been noted to be expressed differentially between high and low active animals: Myostatin (Mstn), Calsequestrin 1 (Casq1), Glucose Transporter member 4 (Slc2a4), and Leptin Receptor (Lepr). These genes where evaluated in previously used high active (C57L/J, n=6) and low active (C3H/HeJ, n=6) inbred mice that were housed with a locked running wheel. The locked wheel eliminated potential training effects on gene expression. Total RNA was isolated from soleus and nucleus accumbens tissue and quantitative real
The ERRα transcriptional pathway has been shown in recent years to play a central role in the regulation of mitochondrial energy metabolism in many cell and tissue types, including striated muscle (20, 63). In the present study, we explored the hypothesis that ERRα may function more broadly as an essential regulatory component of myogenesis. Myocyte differentiation requires precise regulation of multiple gene programs, consisting of genes encoding contractile and sarcoplasmic reticulum proteins, along with ubiquitously expressed proteins involved in energy metabolism. Such coordination may be mediated by transcriptional regulators of energy metabolism genes, including the ERR isoforms and their PGC-1 coactivators, that are temporally induced as part of the myogenic program (Refs. 28, 66; present study). Our findings suggest that ERRα does promote differentiation when overexpressed and is required for normal myogenesis. A surprising finding was that the broader regulatory function for ERRα in ...
human Calsequestrin-1 / CASQ1 gene cDNA, cloning vector & expression plasmid, mutiple tags. Optimized for high expression in mammalian cells. Save up to 60%.
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The potentiatory effects of CASQ2 on the Ca2+-release channels were evidenced by the following findings. Expression of CASQ2R33Q resulted in a shortening of the activation kinetics of Ca2+ transients, and increased CICR gain compared with control myocytes or myocytes overexpressing CASQ2WT. Additionally, the frequency of spontaneous Ca2+ sparks and waves were increased in myocytes expressing CASQ2R33Q. These changes in focal and global cytosolic Ca2+ transients were accompanied by a dramatic decrease in intra-SR [Ca2+], consistent with an increase in the leak of Ca2+ through RyR2s in CASQ2R33Q-expressing cells. The consequences of expressing CASQ2R33Q on Ca2+ handling were clearly different from the effects of expressing the CASQ2D307H mutant protein, the only other CPVT-linked CASQ2 mutation that has been characterized at the cellular and molecular level thus far.16,17 In those earlier studies, ectopic expression of CASQ2D307H in myocytes led to decreases in both active SR Ca2+ release and SR ...
en] Catecholaminergic polymorphic ventricular tachycardia is important to be diagnosed as an underlying disease in children with syncope and normal heart, because of its poor prognosis. CASE REPORT: A 3-year-old boy was referred for stress and emotion induced syncope. Primary ventricular arrhythmia, consisting of salvos of bidirectional ventricular tachycardia, was reproducibly induced by physical exertion. The syncopal events and severe arrhythmia disappeared with beta-blocking therapy. CONCLUSION: Despite its rare occurrence, catecholaminergic polymorphic ventricular tachycardia is an important cause of stress and emotion induced syncope and sudden death in children ...
Authors: Thomas M Roston, Zhiguang Yuchi, Prince J Kannankeril, Julie Hathaway, Jeffrey M Vinocur, Susan P Etheridge, James E Potts, Kathleen R Maginot, Jack C Salerno, Mitchell I Cohen, Robert M Hamilton, Andreas Pflaumer, Saira Mohammed, Lynn Kimlicka, Ronald J Kanter, Martin J LaPage, Kathryn K Collins, Roman A Gebauer, Joel D Temple, Anjan S Batra, Christopher Erickson, Maria Miszczak-Knecht, Peter Kubus, Yaniv Bar-Cohen, Michal Kantoch, Vincent C Thomas, Gabriele Hessling, Chris Anderson, Ming-Lon Young, Sally HJ Choi, Michel Cabrera Ortega, Yung R Lau, Christopher L Johnsrude, Anne Fournier, Filip Van Petegem, Shubhayan Sanatani
A major focus of the working group of Translational Cardiology are molecular mechanisms, which control muscle function and pathophysiological changes due to disease. We use a variety of techniques including biophysics, cell biology, molecular biology, high-resolution imaging (confocal and super resolution microscopy; voltage mapping), transgenic models and comprehensive phenotyping methods. In particular, calcium binding proteins and intracellular calcium signaling are a major interest. For example cardiac ryanodine receptor (RyR2) calcium release channels, which control cardiac contraction and relaxation and modulate physiological stress adaptation during the fight-or-flight response. On the other hand, RyR2 channel dysfunction contributes to heart failure, arrhythmias, and sudden cardiac death. We develop therapeutic options for RyR2 mutation carriers with the syndrome Catecholaminergic Polymorphic Ventricular Tachycardia (CPVT), characterized by stress-induced syncope and sudden death. ...
CPVT (catecholaminergic polymorphic ventricular tachycardia) is an inherited heart condition found in young people and children and it is believed that conditions such as this, can go without detection or diagnosis, and can be a cause of sudden cardiac death in young people.. Brendas son Kristian was 19 when he suffered a sudden cardiac arrest whilst on holiday on the Isle of Skye. Ongoing tests and the record of his medical family tree now suggest a diagnosis of CPVT. Brenda said: We were having breakfast, Kristian got up and just fell to the ground. His eyes glazed over, he turned grey and went clammy. I knew this was serious, we started to do CPR, amazingly the paramedics arrived within 4/5 minutes. They administered defibrillation 4 times and restarted his heart - he was then flown by air-ambulance to hospital in Glasgow.. My own interest in our family history has uncovered a number of fatalities and family members having experienced sudden cardiac arrest. My research has uncovered ...
mouse Asph protein: 26-kDa protein isolated from cardiac junctional sarcoplasmic reticulum; hydroxylates ASP or ASN residues in EGF domains of some proteins; RefSeq NM_023066
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The precise control of Ca2+ levels during the contraction-relaxation cycle in cardiac myocytes is extremely important for normal beat-to-beat contractile activity. The sarcoplasmic reticulum (SR) plays a key role controlling calcium concentration in the cytosol. The SR Ca2+-ATPase (SERCA2) transports Ca2+ inside the SR lumen during relaxation of the cardiac myocyte. Calsequestrin (Casq2) is the main protein in the SR lumen, functioning as a Ca2+ buffer and participating in Ca2+ release by interacting with the ryanodine receptor 2 (RyR2) Ca2+-release channel. Alterations in normal Ca2+ handling significantly contribute to the contractile dysfunction observed in cardiac hypertrophy and in heart failure. Transcriptional regulation of the SERCA2 gene has been extensively studied and some of the mechanisms regulating its expression have been elucidated. Overexpression of Sp1 factor in cardiac hypertrophy downregulates SERCA2 gene expression and increased levels of thyroid hormone up-regulates its ...
Recent studies have been directed towards the potential therapeutic value of improving the sarcoplasmic reticulum (SR) Ca2+ ATPase (SERCA) function in the failing myocardium. Overexpression of SERCA pump or inhibiting the function of phospholamban (PLB) has been shown to improve the cardiac function in failing myocardium. Towards this goal, we enhanced the SERCA pump activity in both atria and ventricle by ablating its key regulators, PLB and sarcolipin (SLN). The homozygous double knockout (dKO) pups were delivered in Mendelian ratio and reached adulthood without any visible abnormalities. However, these mice develop cardiac hypertrophy. The heart weight to body weight ratio significantly increased in 3- 4 months old dKO mice (WT-3.08±0.11 vs. dKO-4.14±0.14) and is associated with enlargement of myocytes (WT-117±8 μm2 vs. dKO-166±10 μm2). Ablation of PLB and SLN did not affect the expression of major Ca2+ handling proteins including SERCA2a, calsequestrin, L-type Ca2+ channel and ...
According to our results in chickens, the possible channel units of DHPRs and RyRs in a sebokeratinocyte are peripherally located. This spatial relationship seems to resemble the arrangement of the smooth muscle cell in which the sarcoplasmic proteins, calsequestrin and RyRs colocalize with DHPRs in numerous, peripherally located sites within the caveolar domains (Moore et al., 2004; Pucovsky and Bolton, 2006). Due to the native arrangement of the stratified epidermis in our study, the exact array of DHPRs on the plasma membrane could not be revealed. However, RyRs were located in the proximity of the plasma membrane in horizontally aligned clusters, indicating the possible sites where the two channels might interact via spatial proximity. In a single smooth muscle cell of the urinary bladder, DHPRs have been shown to occupy the plasmalemma in longitudinal stripes that overlap almost entirely with the corresponding stripes formed by labelled RyR proteins (Moore et al., 2004). The authors ...
ZUHAIR N. AL-HASSNAN, SAHAR TULBAH, WALEED AL-MANEA and MAJID AL-FAYYADH The Phenotype of a CASQ2 Mutation in a Saudi Family with Catecholaminergic Polymorphic Ventricular Tachycardia Pacing and Clinical Electrophysiology 36. Version of Record online: 31 MAY 2012 , DOI: 10.1111/j.1540-8159.2012.03434.x. Complete the form below and we will send an e-mail message containing a link to the selected article on your behalf. Required = Required Field. ...
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Journal of Sedimentary Research, v. 83, i. 6, p. 427-442, Published on June 2013, First Published on June 04, 2013, doi:10.2110/jsr.2013.36 ...
DUGi: Viewing Item from repository Recercat: Catecholaminergic polymorphic ventricular tachycardia (CPVT) is a difficult-to-diagnose cause of sudden cardiac death (SCD). We identified a family of 1400 individuals with multiple cases of CPVT, including 36 SCDs during youth. Objectives: We sought to identify the genetic cause of CPVT in this family, to preventively treat and clinically characterize the mutation-positive individuals, and to functionally characterize the pathogenic mechanisms of the mutation. Methods: Genetic testing was performed for 1404 relatives. Mutation-positive subjects were preventively treated with β-blockers and clinically characterized with a serial exercise treadmill test (ETT) and Holter monitoring. In vitro functional studies included caffeine sensitivity and store overload-induced calcium release activity of the mutant channel in HEK293 cells. Results: We identified the p.G357S_RyR2 mutation, in the cardiac ryanodine receptor, in 179 family members and in 6 SCD victims. No
Patients affected by catecholaminergic polymorphic ventricular tachycardia (CPVT) present bidirectional (BVT), polymorphic ventricular tachycardia (PVT) and ventricular fibrillation (VF), resulting in sudden death. Since RyR2 gene mutations leading to CPVT result in abnormal Ca2+ release it has been inferred that VT/VF is due to delayed after-depolarization (DAD)-induced triggered activity. However, the origin and mechanisms of VT/VF in CPVT are unknown. Recently, a knock-in mouse carrying the RyR2-R4496C mutation (MUT) was shown to reproduce the human BVT, PVT and VF phenotype during adrenergic stimulation. We used volume-conducted ECGs and epicardial optical mapping in 12 MUT and 4 wildtype (WT) hearts to determine whether the arrhythmias originate at the Purkinje fiber (PF) network. Hearts were Langendorff-perfused with Tyrodes solution containing 2.7-3.6 mM/L Ca2+ and 100-200 nM/L isoproterenol. Spontaneous VT occurred in 66% of MUT hearts (41 episodes). No VT was shown in WT hearts ...
This study describes the biochemical composition of junctional feet in skeletal muscle utilizing a fraction of isolated triad junctions. [3H]Ouabain entrapment was employed as a specific marker for T-tubules. The integrity of the triad junction was assayed by the isopycnic density of [3H]ouabain activity (24-30% sucrose for free T-tubules, 38-42% sucrose for intact triads). Trypsin, chymotrypsin, and pronase all caused separation of T-tubules from terminal cisternae, indicating that the junction is composed as least in part of protein. Trypsin and chymotrypsin hydrolyzed four proteins: the Ca2+ pump, a doublet 325,000, 300,000, and an 80,000 Mr protein. T-tubules which had been labeled covalently with 125I were joined to unlabeled terminal cisternae by treatment with K cacodylate. The reformed triads were separated from free T-tubules and then severed by passage through a French press. When terminal cisternae were separated from T-tubules, some 125I label was transferred from the labeled ...
The second messenger cyclic adenosine monophosphate (cAMP) is the most important modulator of sympathetic control over cardiac contractility. In cardiac myocytes and many other cell types, however, cAMP transduces the signal generated upon stimulation of various receptors and activates different cellular functions, raising the issue of how specificity can be achieved. In the general field of signal transduction, the view is emerging that specificity is guaranteed by tight localization of signaling events. Here, we show that in neonatal rat cardiac myocytes, beta-adrenergic stimulation generates multiple microdomains with increased concentration of cAMP in correspondence with the region of the transverse tubule/junctional sarcoplasmic reticulum membrane. The restricted pools of cAMP show a range of action as small as approximately 1 micrometer, and free diffusion of the second messenger is limited by the activity of phosphodiesterases. Furthermore, we demonstrate that such gradients of cAMP specifically
We have used tryptic digestion to determine whether Ca(2+) can regulate cardiac ryanodine receptor (RyR) channel gating from within the lumen of the sarcoplasmic reticulum (SR) or whether Ca(2+) must first flow through the channel and act via cytosolically located binding sites. Cardiac RyRs were incorporated into bilayers, and trypsin was applied to the luminal side of the bilayer. We found that before exposure to luminal trypsin, the open probability of RyR was increased by raising the luminal [Ca(2+)] from 10 micromol/L to 1 mmol/L, whereas after luminal trypsin exposure, increasing the luminal [Ca(2+)] reduced the open probability. The modification in the response of RyRs to luminal Ca(2+) was not observed with heat-inactivated trypsin, indicating that digestion of luminal sites on the RyR channel complex was responsible. Our results provide strong evidence for the presence of luminally located Ca(2+) activation and inhibition sites and indicate that trypsin digestion leads to selective damage to
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Radcliffe Cardiology article authored by Sunil JSR Logantha covering topics - Ventricular arrhythmias, ultrastructure, Purkinje fibre-ventricular junction & on other cardiology field
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This gene encodes calsequestrin, the major calcium-binding protein and calcium buffer within the sarcoplasmic reticulum. ... The calcium is then held within the sarcoplasmic reticulum by a protein called calsequestrin. Fine-tuning of this process can ... Mutations associated with CPVT have also been identified in the CASQ2 gene which encodes calsequestrin, a protein that binds ... In addition to its role as a calcium buffer, calsequestrin also regulates the release of calcium from the sarcoplasmic ...
Genetic mutations affecting calsequestrin are responsible for an autosomal recessive form of catecholaminergic polymorphic ... while the most important within calcium buffer within the sarcoplasmic reticulum is calsequestrin. Alterations in calcium ...
... as more is bound to calsequestrin).[8] Therefore, more calcium can be stored (the calsequestrin is said to be a buffer). It is ... there will be less calcium bound to the calsequestrin. This means that there is more room on the calsequestrin, to bind to the ... Located within the SR is a protein called calsequestrin. This protein can bind to around 50 Ca2+, which decreases the amount of ... However, if calcium within the SR rises too high, more calcium binds to the calsequestrin and therefore it binds to the junctin ...
Cardiac calsequestrin[edit]. Cardiac calsequestrin (CASQ2) plays an integral role in cardiac regulation. Mutations in the ... Two forms of calsequestrin have been identified. The cardiac form Calsequestrin-2 (CASQ2) is present in cardiac and slow ... Each molecule of calsequestrin can bind 18 to 50 Ca2+ ions.[1] Sequence analysis has suggested that calcium is not bound in ... Calsequestrin is a calcium-binding protein of the sarcoplasmic reticulum. The protein helps hold calcium in the cisterna of the ...
Calsequestrin. *Calsyntenin. *Cannabinoid receptor. *Carbamoyl phosphate synthase II. *Carbamoyl phosphate synthetase I ...
rat calsequestrin protein: amino acid sequence given in first source; MW 56-66 kDa; a major skeletal muscle laminin binding ... rat calsequestrin protein. Subscribe to New Research on rat calsequestrin protein amino acid sequence given in first source; MW ...
Calsequestrin. PFAM accession number:. PF01216. Interpro abstract (IPR001393):. Calsequestrin is the principal calcium-binding ... Two forms of calsequestrin have been identified. The cardiac form is present in cardiac and slow skeletal muscle and the fast ... The domain within your query sequence starts at position 11 and ends at position 402; the E-value for the Calsequestrin domain ... The release of calsequestrin-bound calcium (through a a calcium release channel) triggers muscle contraction. The active ...
Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium ... Calsequestrin, cardiac muscle isoform protein, length: 350 (BLAST) Sequence Similarity Cutoff. Rank. Chains in Cluster. Cluster ... Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium ...
Measurement of RyR Permeability Reveals a Role of Calsequestrin in Termination of SR \(Ca^{2+}\) Release in Skeletal Muscle. ... In cells of mice null for Casq1, permeability did not decrease in the same way, indicating that calsequestrin (Casq) is ... Measurement of RyR Permeability Reveals a Role of Calsequestrin in Termination of SR \(Ca^{2+}\) Release in Skeletal Muscle. ... Measurement of RyR Permeability Reveals a Role of Calsequestrin in Termination of SR \(Ca^{2+}\) Release in Skeletal Muscle. ...
Calsequestrin is an inhibitor of skeletal muscle ryanodine receptor calcium release channels. Biophys. J. 82:310-320. ... Ca2+ binding effects on protein conformation and protein interactions of canine cardiac calsequestrin. J. Biol. Chem. 263:1376- ... Luminal Ca2+ Regulation of Single Cardiac Ryanodine Receptors: Insights Provided by Calsequestrin and its Mutants. Jia Qin, ... Regulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation. Biophys. J. 88:3444-3454. ...
Cardiac calsequestrin protein expression increased 2-fold between fetal day 21 and postnatal day 1 and continued to increase ... Calreticulin was detected as a 55kDa band and calsequestrin as 55 and 63kDa bands in 21 day fetal hearts. Only the 55kDa ... Overexpression of the conserved Ca2+-binding proteins calreticulin and calsequestrin impairs cardiac function, leading to ... Effects of prenatal glucocorticoid exposure on cardiac calreticulin and calsequestrin protein expression during early ...
Luminal Ca2+ regulation of single cardiac ryanodine receptors: insights provided by calsequestrin and its mutants. ... Luminal Ca2+ regulation of single cardiac ryanodine receptors: insights provided by calsequestrin and its mutants. ...
Cardiac calsequestrin[edit]. Cardiac calsequestrin (CASQ2) plays an integral role in cardiac regulation. Mutations in the ... Two forms of calsequestrin have been identified. The cardiac form Calsequestrin-2 (CASQ2) is present in cardiac and slow ... Each molecule of calsequestrin can bind 18 to 50 Ca2+ ions.[1] Sequence analysis has suggested that calcium is not bound in ... Calsequestrin is a calcium-binding protein of the sarcoplasmic reticulum. The protein helps hold calcium in the cisterna of the ...
There are no specific protocols for Recombinant Human Calsequestrin 2 protein (ab93736). Please download our general protocols ...
... Heart Rhythm. 2010 Nov;7( ... Objective: To optimize antiarrhythmic therapy in recessively inherited CPVT caused by calsequestrin (CASQ2) mutations. ...
The lollipop plot above illustrates recurrent (observed in 3 or more out of 4440 TCGA tumor samples from 15 cancer types) and therefore potentially oncogenic missense mutations (click on Show Cancer Mutations). The bar plot below shows the proportion of tumor samples that have any kind of altering mutation(s) in the given protein. ...
Calsequestrins (CSQ) are high capacity, medium affinity, calcium-binding proteins present in the sarcoplasmic reticulum (SR) of cardiac and skeletal muscles. CSQ sequesters Ca2+ during muscle relaxation and increases the Ca2+-storage capacity of the SR. Mammalian CSQ has been well studied as a model of human disease, but little is known about the environmental adaptation of CSQ isoforms from poikilothermic organisms. The mummichog, Fundulus heteroclitus, is an intertidal fish that experiences significant daily and seasonal environmental fluctuations and is an interesting study system for investigations of adaptation at the protein level. We determined the full-length coding sequence of a CSQ isoform from skeletal muscle of F. heteroclitus (FCSQ) and characterized the function and structure of this CSQ. The dissociation constant (Kd) of FCSQ is relatively insensitive to changes in temperature ...
Shop a large selection of products and learn more about Calsequestrin 1 Rabbit anti-Human, HRP, Polyclonal, Novus Biologicals ... calmitin, calmitine, calsequestrin 1 (fast-twitch, skeletal muscle), Calsequestrin, skeletal muscle isoform, calsequestrin-1, ... Calsequestrin 1 Polyclonal antibody specifically detects Calsequestrin 1 in Human samples. It is validated for ELISA, ... Produced in rabbits immunized with purified, recombinant Calsequestrin 1 (P31415; Gln35-Asp396).. ...
... Int J Biochem Cell Biol. 2013 Aug;45(8 ... myomesin-2 and calsequestrin-1, but not with caveolin-3 or dystrophin. In conclusion, although IP and BN are useful tools to ... calsequestrin-1; caveolin-3; cytoplasmic dynein 1 light intermediate chain 2; dihydropyridine receptor; fascio-scapulo-humeral ...
offers a broad range of Calsequestrin CRISPR/Cas9 Knockout plasmids and Calsequestrin Double Nickase Plasmids. ... Calsequestrin gene silencers are available as Calsequestrin CRISPR/Cas9 Knockout plasmids and Calsequestrin Double Nickase ... Calsequestrin Antibodies for analysis of cellular responses to Calsequestrin CRISPR Products * For further details describing ... calsequestrin 1 CRISPR/Cas9 KO Plasmid (h2) sc-403375-KO-2. h. Gene Knockout. GFP. ...
Cardiac calsequestrin-null mice (Casq2-/-) display catecholaminergic ventricular tachycardia akin to humans with CASQ2 ... Calsequestrin / deficiency, genetics, metabolism*. Cardiac Pacing, Artificial. Diastole. Disease Models, Animal. Heart Rate. ... Cardiac calsequestrin-null mice (Casq2-/-) display catecholaminergic ventricular tachycardia akin to humans with CASQ2 ... Modest reductions of cardiac calsequestrin increase sarcoplasmic reticulum Ca2+ leak independent of luminal Ca2+ and trigger ...
CASQ2 (cardiac calsequestrin) is commonly believed to serve as the SR (sarcoplasmic reticulum) luminal Ca2+ sensor. Ablation of ... The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium ... Mechanism of calsequestrin regulation of single cardiac ryanodine receptor in normal and pathological conditions ... Vesicle budding from endoplasmic reticulum is involved in calsequestrin routing to sarcoplasmic reticulum of skeletal muscles ...
Calsequestrin 1 antibody LS-C155368 is an unconjugated rabbit polyclonal antibody to Calsequestrin 1 (CASQ1) from human, mouse ... About CASQ1 / Calsequestrin 1. Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an ... Calsequestrin 1 antibody LS-C155368 is an unconjugated rabbit polyclonal antibody to Calsequestrin 1 (CASQ1) from human, mouse ... Calsequestrin 1 antibody LS-C155368 is an unconjugated rabbit polyclonal antibody to Calsequestrin 1 (CASQ1) from human, mouse ...
The key element of the sensor system is calsequestrin (CSQ) functionalized GNPs, which have an approximate size of 13 nm, and ... Bioinspired Colorimetric Detection of Calcium(II) Ions in Serum Using Calsequestrin-Functionalized Gold Nanoparticles.. код для ... 4202 Figure 1. a) Schematic representation of the calcium ion sensor: the aggregation of calsequestrin (CSQ) functionalized ... calsequestrin · nanostructures · sensors [1] A. H. Gowenlock, J. R. McMurray, D. M. McLanchlan, Varleys Practical Clinical ...
Calsequestrin and the calcium release channel of skeletal and cardiac muscle. Prog Biophys Mol Biol. 2004; 85: 33-69. ... Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum. Nat Struct Biol. 1998; 5: 476-483. ... Park H, Wu S, Dunker AK, Kang C. Polymerization of calsequestrin: implications for Ca2+ regulation. J Biol Chem. 2003; 278: ... Figure 1. Immunoblot analysis of calsequestrin levels in myocytes infected with Ad-Control, Ad-CASQ2WT, and Ad-CASQ2R33Q ...
Characterization of fast-twitch and slow-twitch skeletal muscles of calsequestrin 2 (CASQ2)-knock out mice: unexpected adaptive ... This study investigates the functional role of calsequestrin 2 (CASQ2) in both fast-twitch and slow-twitch skeletal muscles by ... Characterization of fast-twitch and slow-twitch skeletal muscles of calsequestrin 2 (CASQ2)-knock out mice: unexpected adaptive ... Characterization of fast-twitch and slow-twitch skeletal muscles of calsequestrin 2 (CASQ2)-knock out mice: unexpected adaptive ...
Mcfarland, Timothy, "Cardiac Calsequestrin Phosphorylation And Trafficking In The Mammalian Cardiomyocyte" (2011). Wayne State ...
... hidden medical causes of Myopathy due to calsequestrin and SERCA1 protein overload, risk factors, and what causes Myopathy due ... Causes of Myopathy due to calsequestrin and SERCA1 protein overload including triggers, ... Myopathy due to calsequestrin and SERCA1 protein overload: Introduction. *Summary Overview: Myopathy due to calsequestrin and ... Next: Treatment for Myopathy due to calsequestrin and SERCA1 protein overload Diseases » Myopathy due to calsequestrin and ...
This gene encodes calsequestrin, the major calcium-binding protein and calcium buffer within the sarcoplasmic reticulum. ... The calcium is then held within the sarcoplasmic reticulum by a protein called calsequestrin. Fine-tuning of this process can ... Mutations associated with CPVT have also been identified in the CASQ2 gene which encodes calsequestrin, a protein that binds ... In addition to its role as a calcium buffer, calsequestrin also regulates the release of calcium from the sarcoplasmic ...
Native Canine Calsequestrin \ 228-10167-2 for more molecular products just contact us ... Calsequestrin is the major calcium storage protein of the sarcoplasmic reticulum. Intraluminar Ca2+ binds to calsequestrin ... Index / Ray Biotech / Native Canine Calsequestrin / Product Detail : 228-10167-2 Native Canine Calsequestrin. Related keywords ... We have also other products like : Native Canine Calsequestrin. Related products : Native Canine Calsequestrin ...
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Cardiac calsequestrin (CASQ2), and its binding partners junction and triadin-1 (TRDN), are key regulators of sarcoplasmic ... Calsequestrin in Ventricular Arrhythmia and Sudden Death Knollmann, Bjorn C. Vanderbilt University Medical Center, Nashville, ... Calsequestrin in Ventricular Arrhythmia and Sudden Death. Knollmann, Bjorn C. / Vanderbilt University Medical Center. $18,055. ... Calsequestrin in Ventricular Arrhythmia and Sudden Death. Knollmann, Bjorn C. / Vanderbilt University Medical Center. $351,000 ...
Differential distribution of calcium stores in Paramecium cells : occurrence of a subplasmalemmal store with a calsequestrin- ... Differential distribution of calcium stores in Paramecium cells : occurrence of a subplasmalemmal store with a calsequestrin- ... Differential distribution of calcium stores in Paramecium cells : occurrence of a subplasmalemmal store with a calsequestrin- ... calsequestrin (CS) and calreticulin (CR) using antibodies against CS from rat skeletal muscle and against CR from rat liver, ...
This gene encodes the skeletal muscle specific member of the calsequestrin protein family. Calsequestrin functions as a luminal ... Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in ... calsequestrin 1. Enable Javascript to view the expand/collapse boxes.. Open All Close All ...
Calsequestrin 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene ... orf clones - Search results for 108 available Calsequestrin gene related products * Overview of 108 available Calsequestrin ... orf clones - Search results for 108 available Calsequestrin gene related products * Overview of 108 available Calsequestrin ... This gene encodes the skeletal muscle specific member of the calsequestrin protein family. Calsequestrin functions as a luminal ...
Calsequestrin 1 Overexpression Lysate (Adult Normal), Novus Biologicals (NBL1-08719). Supplier: Novus Biologicals. ...
  • In cells of mice null for Casq1, permeability did not decrease in the same way, indicating that calsequestrin (Casq) is essential in the mechanism of channel closure and termination of \(Ca^{2+}\) release. (harvard.edu)
  • The cardiac form Calsequestrin-2 (CASQ2) is present in cardiac and slow skeletal muscle and the fast skeletal form Calsequestrin-1(CASQ1) is found in fast skeletal muscle. (wikipedia.org)
  • Cardiac calsequestrin (CASQ2) plays an integral role in cardiac regulation. (wikipedia.org)
  • To optimize antiarrhythmic therapy in recessively inherited CPVT caused by calsequestrin (CASQ2) mutations. (nih.gov)
  • Cardiac calsequestrin-null mice (Casq2-/-) display catecholaminergic ventricular tachycardia akin to humans with CASQ2 mutations. (biomedsearch.com)
  • Catecholaminergic polymorphic ventricular tachycardia (CPVT) is a familial arrhythmogenic disorder associated with mutations in the cardiac ryanodine receptor ( RyR2 ) and cardiac calsequestrin ( CASQ2 ) genes. (ahajournals.org)
  • Two genetic variants of the disease have been described: a recessive form associated with homozygous mutations in the gene encoding the cardiac isoform of calsequestrin ( CASQ2 ) 2,3 and a second form transmitted as an autosomal dominant trait associated with mutations in the gene encoding the cardiac ryanodine receptor ( RyR2 ). (ahajournals.org)
  • CASQ2-/- causes increase in calsequestrin 1 (CASQ1) expression, but without functional changes in both muscle types. (eurekamag.com)
  • Cardiac calsequestrin (CASQ2), and its binding partners junction and triadin-1 (TRDN), are key regulators of sarcoplasmic reticulum (SR) Ca storage and release. (grantome.com)
  • All modifications are more pronounced (or only found) in fast-twitch extensor digitorum longus muscle compared to slow-twitch soleus muscle, likely because the latter expresses higher amounts of calsequestrin type-2 (CASQ2). (unich.it)
  • The CASQ2 gene provides instructions for making a protein called calsequestrin 2. (medlineplus.gov)
  • Calsequestrin (Casq2) is the main protein in the SR lumen, functioning as a Ca 2+ buffer and participating in Ca 2+ release by interacting with the ryanodine receptor 2 (RyR2) Ca 2+ -release channel. (ingentaconnect.com)
  • Auf www.antikoerper-online.de finden Sie aktuell 76 Calsequestrin 2 (Cardiac Muscle) (CASQ2) Antikörper von 14 unterschiedlichen Herstellern. (antikoerper-online.de)
  • CASQ2 -/- causes increase in calsequestrin 1 (CASQ1 (zeige CASQ1 Antikörper )) expression. (antikoerper-online.de)
  • Calsequestrin 2 (CASQ2) mutations increase expression of calreticulin and ryanodine receptors, causing catecholaminergic polymorphic ventricular tachycardia. (semanticscholar.org)
  • Antigen standard for calsequestrin 2 (cardiac muscle) (CASQ2) is a lysate prepared from HEK293T cells transiently transfected with a TrueORF gene-carrying pCMV plasmid and then lysed in RIPA Buffer. (creativebiomart.net)
  • Calsequestrin 1 antibody LS-C155368 is an unconjugated rabbit polyclonal antibody to Calsequestrin 1 (CASQ1) from human, mouse and rat. (lsbio.com)
  • In cells of mice null for Casq1, permeability did not decrease in the same way, indicating that calsequestrin (Casq) is essential in the mechanism of channel closure and termination of \(Ca^{2+}\) release. (harvard.edu)
  • CASQ1 (Calsequestrin 1) is a Protein Coding gene. (genecards.org)
  • BACKGROUND: Mice lacking calsequestrin-1 (CASQ1-null), a Ca-binding protein that modulates the activity of Ca release in the skeletal muscle, exhibit lethal hypermetabolic episodes that resemble malignant hyperthermia in humans when exposed to halothane or heat stress. (unich.it)
  • CASQ1 mutations impair calsequestrin polymerization and cause tubular aggregate myopathy. (nih.gov)
  • Mutations in the cardiac calsequestrin gene have been associated with cardiac arrhythmia and sudden death. (wikipedia.org)
  • Calsequestrin gene silencers are available as Calsequestrin CRISPR/Cas9 Knockout plasmids and Calsequestrin Double Nickase Plasmids. (scbt.com)
  • Calsequestrin CRISPR/dCas9 Activation Plasmids and CRISPR Lenti Activation Systems for gene activation are also available. (scbt.com)
  • This gene encodes the skeletal muscle specific member of the calsequestrin protein family. (nih.gov)
  • The recently cloned rabbit cardiac calsequestrin gene is over 30 kb and contains 11 exons. (davidson.edu)
  • All isoforms of the calsequestrin gene have similar splicing patterns, so no alternative splicing pattern is apparent (Yano and Zarain Hertzberg, 1994). (davidson.edu)
  • The protein encoded by this gene specifies the cardiac muscle family member of the calsequestrin family. (avivasysbio.com)
  • Enhancing atrial-specific gene expression using a calsequestrin cis-regulatory module 4 with a sarcolipin promoter. (semanticscholar.org)
  • Calsequestrin-1 is an isoform of calsequestrin. (sinobiological.com)
  • Note: This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells. (avivasysbio.com)
  • To determine whether intra-uterine growth retardation or programmed hypertension was associated with altered calreticulin or calsequestrin expression, effects of prenatal glucocorticoid overexposure (maternal dexamethasone treatment on days 15-21 of pregnancy) were examined during fetal life and postnatal development until adulthood (24 weeks). (biochemj.org)
  • Calreticulin was detected as a 55kDa band and calsequestrin as 55 and 63kDa bands in 21 day fetal hearts. (biochemj.org)
  • Modest reductions of cardiac calsequestrin increase sarcoplasmic reticulum Ca2+ leak independent of luminal Ca2+ and trigger ventricular arrhythmias in mice. (biomedsearch.com)
  • Calsequestrin functions as a luminal sarcoplasmic reticulum calcium sensor in both cardiac and skeletal muscle cells. (nih.gov)
  • We investigated the hypothesis that prolonged exposure to low luminal Ca2+ causes conformational changes in calsequestrin and deregulation of ryanodine receptors, allowing channel activity to increase. (edu.au)
  • Lowering of luminal Ca2+ from 1 mM to 100 microM for several minutes resulted in conformational changes with dissociation of 65-75% of calsequestrin from the junctional face membrane. (edu.au)
  • In contrast, when ryanodine receptors were calsequestrin regulated, lowering luminal Ca2+ either did not alter or decreased activity. (edu.au)
  • We have investigated the possibility that calsequestrin is a luminal calcium concentration sensor for the ryanodine receptor. (edu.au)
  • We measured the luminal calcium concentration at which calsequestrin dissociates from the ryanodine receptor and the effect of calsequestrin on the response of the ryanodine receptor to changes in luminal calcium. (edu.au)
  • These data suggest that the quaternary complex is intact in vivo, and provides further evidence that calsequestrin is involved in the sarcoplasmic reticulum calcium signaling pathway and has a role as a luminal calcium sensor for the ryanodine receptor. (edu.au)
  • Dulhunty, Angela F. / Regulation of Ryanodine receptors by Calsequestrin: Effect of high luminal Ca2+ and phosphorylation . (edu.au)
  • Although a reduced Ca(2+) buffering capacity has been shown to exist in the dystrophic sarcoplasmic reticulum, surprisingly no changes in the abundance of the main luminal Ca(2+) reservoir protein calsequestrin have been observed in microsomal preparations. (maynoothuniversity.ie)
  • Calsequestrin 1 Polyclonal antibody specifically detects Calsequestrin 1 in Human samples. (fishersci.com)
  • Recombinant fragment corresponding to a region within amino acids 136 and 381 of Calsequestrin 1 (SwissProt P31415). (lsbio.com)
  • This protein can bind to around 50 Ca 2+ , which decreases the amount of free Ca 2+ within the SR (as more is bound to calsequestrin). (wikipedia.org)
  • The release of calcium bound to calsequestrin through a calcium release channel triggers muscle contraction. (avivasysbio.com)
  • Ryanodine receptors are regulated by calsequestrin under physiological conditions where calsequestrin is polymerized. (edu.au)
  • The calcium ions are actively pumped into the SR by SERCA2a, bound in the lumen by calsequestrin, and released into the cytosol by IP 3 - or ryanodine receptors. (davidson.edu)
  • Transgenic mouse hearts overexpressing the Ca 2+ -binding protein calsequestrin (CSQ) have an accompanying 10-fold increase in the sarcoplasmic reticulum (SR) Ca 2+ load, however, exhibits slow and small Ca 2+ -induced Ca 2+ release. (elsevier.com)
  • Furthermore, we found that the calcium storage protein calsequestrin 1 of the little brown bat and the bottlenose dolphin functionally converged in its ability to form calcium-sequestering polymers at lower calcium concentrations, which may contribute to rapid calcium transients required for superfast muscle physiology. (sciencemag.org)
  • Phosphorylation of cardiac and skeletal muscle calsequestrin isoforms by casein kinase II. (wikipedia.org)
  • Third, contrary to the restricted expresion of the fast skeletal isoform, cardiac calsequestrin mRNA is present in both cardiac and slow skeletal muscle, but not in fast skeletal muscle. (elsevier.com)
  • Calsequestrin is localized to the sarcoplasmic reticulum in cardiac and slow skeletal muscle cells. (avivasysbio.com)
  • Genetic mutations affecting calsequestrin are responsible for an autosomal recessive form of catecholaminergic polymorphic ventricular tachycardia, an inherited cardiac condition that can lead to sudden death. (wikipedia.org)
  • In cardiac muscle cells, the most important buffers within the cytoplasm include troponin C, SERCA, calmodulin, and myosin, while the most important within calcium buffer within the sarcoplasmic reticulum is calsequestrin. (wikipedia.org)
  • Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. (lsbio.com)
  • Calsequestrin is the major calcium buffering protein localized in the lumen of adult cardiac SR. It binds calcium with high capacity and low affinity during muscle relaxation. (davidson.edu)
  • [3] Calsequestrin is also secreted in the gut where it deprives bacteria of calcium ions. (wikipedia.org)
  • The key element of the sensor system is calsequestrin (CSQ) functionalized GNPs, which have an approximate size of 13 nm, and can form aggregates in the presence of appropriate amounts of calcium ions. (docme.ru)
  • Within myocytes, calsequestrin 2 is located in a cell structure called the sarcoplasmic reticulum, which acts as a storage center for calcium ions. (medlineplus.gov)
  • In response to certain signals, calcium ions stored by calsequestrin 2 in the sarcoplasmic reticulum are released into the surrounding cell fluid (the cytoplasm). (medlineplus.gov)
  • A lack of properly functioning calsequestrin 2 may also affect regulation of the RYR2 channel, allowing calcium ions to "leak" out of the sarcoplasmic reticulum. (medlineplus.gov)
  • Each molecule of calsequestrin can bind 18 to 50 Ca 2+ ions. (wikipedia.org)
  • Bioinspired Colorimetric Detection of Calcium(II) Ions in Serum Using Calsequestrin-Functionalized Gold Nanoparticles. (docme.ru)
  • During systole, Calsequestrin coordinately releases ~40--50 Ca2+ ions per molecule for each contraction-relaxation cycle by an uncertain mechanism. (antibody-antibodies.com)
  • Most of these ions are stored by attaching (binding) to calsequestrin 2. (medlineplus.gov)
  • Since there is no apparent mechanism to keep the calsequestrin inside the SR, it must either use an unknown mechanism or bind to another SR protein. (davidson.edu)
  • A calcium buffer is contained within the lumen of the SR to reduce the concentration gradient which the calcium pumps must work against, and to prevent the precipitation of calcium salts inside the SR. The major calcium buffer in muscle cells is calsequestrin and it is the key to successful storage and release of calcium (Tharin et. (davidson.edu)
  • Calsequestrin is an anchored protein network within the lumen of the SR (Yano and Zarain-Hertzberg, 1994) that is retained within the lumen of the SR after transcription. (davidson.edu)
  • Cardiac calsequestrin contains 391 amino acid residues plus a 19-residue amino-terminal signal sequence. (elsevier.com)
  • We conclude that the deduced amino acid sequence of cardiac calsequestrin is consistent with its ability to bind large amounts of Ca 2+ (40 mol of Ca 2+ /mol of calsequestrin). (elsevier.com)
  • Some of these mutations change single protein building blocks (amino acids) in the calsequestrin 2 protein, while other mutations prevent the cell from producing any functional calsequestrin 2. (medlineplus.gov)
  • Calsequestrin 1 Overexpression Lysate (Adult Normal). (vwr.com)
  • Intraluminar Ca2+ binds to calsequestrin during diastole to prevent Ca2+ precipitation and to lower its free ionic concentration to facilitate efficient storage. (antibody-antibodies.com)
  • Among the latter is calsequestrin (CSQ), the major Ca 2+ -binding protein condensed within both the terminal cisternae of striated muscle SR and the ER vacuolar domains of some neurons and smooth muscles. (elsevier.com)
  • This included the main terminal cisternae constituent, calsequestrin, and the previously implicated Ca(2+)-shuttle element, sarcalumenin. (maynoothuniversity.ie)