Calsequestrin: 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.Sarcoplasmic Reticulum: 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.Muscle Proteins: The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.Calcium-Binding Proteins: Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.Ryanodine Receptor Calcium Release Channel: 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.Calreticulin: 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.Calcium: 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.Murexide: 5,5'-Nitrilodibarbituric acid ammonium derivative. Used as an indicator for complexometric titrations.Rabbits: 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.Calcium-Transporting ATPases: 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.Myocardium: 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.Muscles: Contractile tissue that produces movement in animals.Mixed Function Oxygenases: 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.Muscle, Skeletal: 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.Calcium Signaling: 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.Sarcoplasmic Reticulum Calcium-Transporting ATPases: 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.Azirines: Unsaturated azacyclopropane compounds that are three-membered heterocycles of a nitrogen and two carbon atoms.Phenolsulfonphthalein: Red dye, pH indicator, and diagnostic aid for determination of renal function. It is used also for studies of the gastrointestinal and other systems.Tachycardia, Ventricular: 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).Dogs: 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)Immunoproliferative Disorders: Disorders characterized by abnormal proliferation of primary cells of the immune system or by excessive production of immunoglobulins.Receptors, Laminin: 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.Laminin: 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.Amino Acid Sequence: 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.Dystroglycans: 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.Molecular Sequence Data: 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.Colorimetry: 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)Hypercalcemia: Abnormally high level of calcium in the blood.Gold: 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.Hyperparathyroidism, Primary: 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.Hyperparathyroidism: 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.Biomimetics: An interdisciplinary field in materials science, ENGINEERING, and BIOLOGY, studying the use of biological principles for synthesis or fabrication of BIOMIMETIC MATERIALS.Meglutol: 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.Competitive Bidding: Pricing statements presented by more than one party for the purpose of securing a contract.Dose-Response Relationship, Drug: The relationship between the dose of an administered drug and the response of the organism to the drug.Ryanodine: 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.Membrane Potentials: 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).Permeability: Property of membranes and other structures to permit passage of light, heat, gases, liquids, metabolites, and mineral ions.Betamethasone: 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)Glucocorticoids: 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.Dexamethasone: An anti-inflammatory 9-fluoro-glucocorticoid.Prenatal Exposure Delayed Effects: 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.Receptors, Glucocorticoid: 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.Calcium Channels: 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.Muscle Fibers, Slow-Twitch: 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.Muscle Fibers, Fast-Twitch: 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.Mice, Knockout: 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.Tetany: 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)Mice, Inbred C57BLPlasmids: Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Genetic Vectors: DNA molecules capable of autonomous replication within a host cell and into which other DNA sequences can be inserted and thus amplified. Many are derived from PLASMIDS; BACTERIOPHAGES; or VIRUSES. They are used for transporting foreign genes into recipient cells. Genetic vectors possess a functional replicator site and contain GENETIC MARKERS to facilitate their selective recognition.

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)

*Calsequestrin

Two forms of calsequestrin have been identified. The cardiac form Calsequestrin-2 (CASQ2) is present in cardiac and slow ... Calsequestrin is also secreted in the gut where it deprives bacteria of calcium ions.[citation needed]. Cardiac calsequestrin ( ... Each molecule of calsequestrin can bind 18 to 50 Ca2+ ions. 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 ...

*Catecholaminergic polymorphic ventricular tachycardia

Mutations in the Calsequestrin isoform 2 (CASQ2) gene has been linked to CPVT. Under normal physiological conditions, CASQ2 is ... Calsequestrin (CASQ2) is a calcium buffering protein of the sarcoplasmic reticulum. Mutation of the Ryanodine receptor isoform ... 2007). "Calsequestrin 2 (CASQ2) mutations increase expression of calreticulin and ryanodine receptors, causing ... 2004). "Abnormal Calcium Signaling and Sudden Cardiac Death Associated With Mutation of Calsequestrin". Circ. Res. 94 (4): 471- ...

*Sarcoplasmic reticulum

... as more is bound to calsequestrin). Therefore, more calcium can be stored (the calsequestrin is said to be a buffer). It is ... However, if calcium within the SR rises too high, more calcium binds to the calsequestrin and therefore it binds to the junctin ... Located within the SR is a protein called calsequestrin. This protein can bind to around 50 Ca2+, which decreases the amount of ... If calcium concentration within the SR falls too low, there will be less calcium bound to the calsequestrin. This means that ...

*Triadin

Shin, D. W.; Ma, J.; Kim, D. H. (2000). "The asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca2+ and ... Shin DW, Ma J, Kim DH (2001). "The asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca2+ and interacts with ... Guo, W; Campbell K P (Apr 1995). "Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the ... Gyorke, I.; Hester, N.; Jones, L. R.; Gyorke, S. (2004). "The Role of Calsequestrin, Triadin, and Junctin in Conferring Cardiac ...

*ASPH

1997). "Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac ...

*Istaroxime

Ca(2+)-transporting ATPase, phospholamban, and calsequestrin levels in nonfailing and failing human myocardium. Circulation, 90 ...

*RYR1

Guo W, Campbell KP (April 1995). "Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the ...

*P2RX4

... rescue of the calsequestrin overexpression model of cardiomyopathy". American Journal of Physiology. Heart and Circulatory ...

*Ryanodine receptor

Calsequestrin has multiple Ca2+ binding sites and binds Ca2+ ions with very low affinity so they can be easily released. ... The cardiac-specific isoform of the receptor (RyR2) is known to form a quaternary complex with luminal calsequestrin, junctin, ...

*Muscle contraction

... sarcoplasmic reticulum has a large calcium buffering capacity partially due to a calcium-binding protein called calsequestrin. ...

*Calcium-binding protein

... low-affinity calcium-binding protein calsequestrin. Calretinin is another type of Calcium binding protein weighing 29kD. It is ... Antagonists Calcium Binding Protein Modulator Inhibitors Additional Calcium Binding Protein Modulators calmodulin calsequestrin ...

*Larynx

Laitman & Reidenberg 1997 Lipan, Reidenberg & Laitman 2006 "Sarcoplasmic-endoplasmic-reticulum Ca2+-ATPase and calsequestrin ...

*Calcium sparks

This is thought to be due to the calsequestrin binding more strongly to the RyR, preventing it from opening and decreasing the ... As well as this, a protein called calsequestrin (found within the SR) detaches from the RyR, when calcium concentration is too ...

*Calreticulin

... also known as calregulin, CRP55, CaBP3, calsequestrin-like protein, and endoplasmic reticulum resident protein 60 ...

*SERCA

Another protein, calsequestrin, binds calcium within the SR and helps to reduce the concentration of free calcium within the SR ...

*Congenital myopathy

... calsequestrin, and RYR1 have been shown to bind to cylindrical spirals. Cylindrical spirals have also been shown to react with ...
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 ...
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) ...
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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UriBuilder builds URI, asking URIBuilder are you matching it is confusing, because it is a builder, not a matcher. UriTemplate may have a number of useful methods letting users to get the properties of a given template - and having most of those methods would not make sense to have at UriBuilder level; ...
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 ...
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 ...
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 ...
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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BVT is an infrequent arrhythmia that has nevertheless mesmerized electrophysiologists for many years. It is most commonly observed under conditions of digitalis intoxication and in advanced heart disease.22 On ECG, BVT is manifested as an alternation in the polarity of the QRS axis in some of the leads; the remaining leads may demonstrate changes in morphology.22 The tachycardia is often regular, occurs in brief salvoes, and often resolves spontaneously or may degenerate into PVT or VF. The alternating pattern is usually associated with bundle branch block morphology in the precordial leads, with the alternating QRS complexes differing from each other in amplitude and duration. Since its first description in 1922,23 several hypotheses have been postulated for the mechanism of BVT, including enhanced automaticity with the existence of 2 separate ventricular foci22,24 or even reentry.22 More recently, the demonstration of RyR2 gain-of-function mutations in patients with familial CPVT has led to ...
Gene therapy has progressed from a dream to a bedside reality in quite a few human diseases. From its first application in adenosine deaminase deficiency, through the years, its application has evolved to vascular angiogenesis and cardiac arrhythmias. Gene based biological pacemakers using viral vectors or mesenchymal cells tested in animal models hold much promise. Induction of pacemaker activity within the left bundle branch can provide stable heart rates. Genetic modification of the AV node mimicking beta blockade can be therapeutic in the management of atrial fibrillation. G protein overexpression to modify the AV node also is experimental. Modification and expression of potassium channel genes altering the delayed rectifier potassium currents may permit better management of congenital long QT syndromes. Arrhythmias in a failing heart are due to abnormal calcium cycling. Potential targets for genetic modulation include the sarcoplasmic reticulum calcium pump, calsequestrin and sodium calcium ...
Gene therapy has progressed from a dream to a bedside reality in quite a few human diseases. From its first application in adenosine deaminase deficiency, through the years, its application has evolved to vascular angiogenesis and cardiac arrhythmias. Gene based biological pacemakers using viral vectors or mesenchymal cells tested in animal models hold much promise. Induction of pacemaker activity within the left bundle branch can provide stable heart rates. Genetic modification of the AV node mimicking beta blockade can be therapeutic in the management of atrial fibrillation. G protein overexpression to modify the AV node also is experimental. Modification and expression of potassium channel genes altering the delayed rectifier potassium currents may permit better management of congenital long QT syndromes. Arrhythmias in a failing heart are due to abnormal calcium cycling. Potential targets for genetic modulation include the sarcoplasmic reticulum calcium pump, calsequestrin and sodium calcium ...
There are few areas in cardiology in which the impact of genetics and genetic testing on clinical management has been as great as in cardiac channelopathies,arrhythmic disorders of genetic origin related to the ionic control of the cardiac action potential. Among the growing number of diseases identified as channelopathies,3 are sufficiently prevalent to represent significant clinical and societal problems and to warrant adequate understanding by practicing cardiologists: long QT syndrome,catecholaminergic polymorphic ventricular tachycardia,and Brugada syndrome. This review will focus selectively on the impact of genetic discoveries on clinical management of these 3 diseases. For each disorder,we will discuss to what extent genetic knowledge and clinical genetic test results modify the way cardiologists should approach and manage affected patients. We will also address the optimal use of genetic testing,including its potential limitations and the potential medico-legal implications when such ...
F49 Molecular Cloning and Sequencing of the HRC Gene from Mouse Heart Reveals a Highly Unstable GAG Repeat. Shundi Shi, Steven R. Brunnert. Columbia University, Institute of Comparative Medicine 630 W. 168th Street, Mail Box 17, New York, NY 10032. Histidine-rich calcium binding protein (HRC) is a luminal sarcoplasmic reticulum protein that has been mapped to human Chromosome 19 and mouse Chromosome 7 and considered a candidate gene of several genetic diseases in humans and mice. We derived a 2407-bp clone encoding for a 738 AA protein by PCR from C57BL/6J mouse heart and found a highly unstable GAG repeat in the middle of the coding region. The instability of the GAG repeat could be detected within individual C57BL/6J and DBA/2J mice in both genomic DNA and cDNA, and no polymorphism was found between two mouse HRC cDNAs except the unstable GAG repeats. At normal physiologic conditions, no GAG expansion was found in the unstable GAG repeat region in the dystrophic cardiac calcinosis (DCC) ...
Cardiac differentiation of iPSC-derived from CPVT1 RyR2R420Q and CPVT2 CASQ2D307H patients and healthy control. (A) Immunofluorescence expression of typical myo
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Catecholaminergic polymorphic ventricular tachycardia (CPVT) is a potentially fatal cardiac arrhythmia in individuals with a structurally normal heart. The disorder is characterized by syncope, typically beginning in the first decade of life, which may be triggered by physical activity or intense emotion. In patients with CPVT, stress- induced release of catecholamines causes a dysfunction of calcium-ion channel in myocytes. The ion channel dysfunction induces ventricular arrhythmias, which can lead to syncope or sudden cardiac death. Spontaneous recovery from the arrhythmia is possible, but the ventricular tachycardia can progress to ventricular fibrillation and sudden death. The incidence of CPVT within the population is not precisely known, but is estimated to be 1:10,000. Symptoms include syncope, dizziness, arrhythmia, and sudden cardiac death. Diagnosis may prove difficult, due to normal echocardiogram and electrocardiogram at a resting state. Testing must be performed under ...
Jung, C. B., Moretti, A., Mederos y Schnitzler, M., Iop, L., Storch, U., Bellin, M., Dorn, T., Ruppenthal, S., Pfeiffer, S., Goedel, A., Dirschinger, R. J., Seyfarth, M., Lam, J. T., Sinnecker, D., Gudermann, T., Lipp, P. and Laugwitz, K.-L. (2012), Dantrolene rescues arrhythmogenic RYR2 defect in a patient-specific stem cell model of catecholaminergic polymorphic ventricular tachycardia. EMBO Mol Med, 4: 180-191. doi: 10.1002/emmm.201100194 ...
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One measure would ban the sale of semiautomatic handguns and rifles. People who currently own such weapons could keep them, but would have to register them.. The second proposal would limit ammunition magazines to 10 or fewer rounds. Sen. Dan Kotowski, the bills sponsor, says he wants to concentrate on the high-capacity magazines because they make assault weapons more lethal.. Democrats are pushing the gun restrictions in the wake of the school massacre in Connecticut last month. ...
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It includes sequencing of all coding regions of the following 27 genes ABCC9, AKAP9, ANK2, CACNA1C, CACNA2D1, CACNB2, CALM1, CASQ2, CAV3, DPP6, GPD1L, HCN4, KCNE1, KCNE2, KCNE3, KCNH2, KCNJ2, KCNJ8, KCNQ1, LMNA, RYR2, SCN1B, SCN3B, SCN5A, SNTA1, TNNT2, TRDN ...
Phospholamban兔多克隆抗体(ab85146)可与小鼠, 大鼠, 人样本反应并经WB, IHC实验严格验证。所有产品均提供质保服务,中国75%以上现货。
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It has often been assumed that the amount of pain a person experiences is directly proportional to the amount of tissue damage. How people cope or deal with their pain experience has been shown to be an important factor in determining the level of pain and disability. The most widely used instrument is the Coping Strategies Questionnaire (CSQ). The CSQ is designed to assess a participants normal means of coping with painful situations. Despite the popularity of the CSQ as a research and clinical instrument, a shorter version would be beneficial for a number of reasons. The current study assessed the properties of a shorter version of the CSQ that was developed in the lab. The study included 22 chronic pain patients who were asked to complete a number of measures that assessed pain, activity interference, coping, functional status, and mood. The results of the study suggest that the internal reliability of the short-form of the CSQ is not comparable to the original version. However, correlation ...
The endoplasmic reticulum (ER) is a critical organelle for protein synthesis, folding and modification, and lipid synthesis and calcium storage. Dysregulation of ER functions leads to the accumulation of misfolded- or unfolded-protein in the ER lumen, and this triggers the unfolded protein response …
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As many of you know, JCache (JSR 107) narrowly missed Java EE 7. JCache is clearly a very important and long-anticipated API as indicated in the well-participated Java EE 7 survey. I am happy to report that JCache keeps making steady progress and recently posted a public review. The review is open until August 5th and you are encouraged to get your comments in. You can send your comments directly to [email protected] or enter issues on GitHub. At the current pace, JCache should be ready well.... ...
Phospholamban兔多克隆抗体(ab15000)可与小鼠, 大鼠, 兔, 仓鼠, 牛, 人, 猪, 中国仓鼠样本反应并经WB, IHC, ICC/IF实验严格验证,被7篇文献引用并得到11个独立的用户反馈。
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Abnormal Interactions of Calsequestrin With the Ryanodine Receptor Calcium Release Channel Complex Linked to Exercise-Induced...Abnormal Interactions of Calsequestrin With the Ryanodine Receptor Calcium Release Channel Complex Linked to Exercise-Induced...

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 ...
more infohttp://circres.ahajournals.org/content/98/9/1151

Calsequestrin - WikipediaCalsequestrin - Wikipedia

Two forms of calsequestrin have been identified. The cardiac form Calsequestrin-2 (CASQ2) is present in cardiac and slow ... Calsequestrin is also secreted in the gut where it deprives bacteria of calcium ions.[citation needed]. Cardiac calsequestrin ( ... Each molecule of calsequestrin can bind 18 to 50 Ca2+ ions. 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 ...
more infohttps://en.wikipedia.org/wiki/Calsequestrin

calsequestrin 2 (dog)calsequestrin 2 (dog)

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. ...
more infohttps://www.phosphosite.org/proteinAction.action?id=5126&showAllSites=true

Recombinant Human Calsequestrin 2 protein (ab93736) ProtocolsRecombinant Human Calsequestrin 2 protein (ab93736) Protocols

There are no specific protocols for Recombinant Human Calsequestrin 2 protein (ab93736). Please download our general protocols ...
more infohttps://www.abcam.com/recombinant-human-calsequestrin-2-protein-ab93736-protocols.html

rat calsequestrin protein
     Summary Report | CureHunterrat calsequestrin protein Summary Report | CureHunter

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 ...
more infohttp://www.curehunter.com/public/keywordSummaryC057137-rat-calsequestrin-protein.do

Calsequestrin CRISPR Plasmids | SCBT - Santa Cruz BiotechnologyCalsequestrin CRISPR Plasmids | SCBT - Santa Cruz Biotechnology

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. ...
more infohttps://www.scbt.com/scbt/browse/Calsequestrin-CRISPR-Plasmids/_/N-wrpn5z

Functional and Structural Characterization of a Eurytolerant Calsequestrin from the Intertidal Teleost Fundulus heteroclitusFunctional and Structural Characterization of a Eurytolerant Calsequestrin from the Intertidal Teleost Fundulus heteroclitus

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 and pH, thus indicating that FCSQ is a eurytolerant protein. We identified and characterized a highly conserved
more infohttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0050801

CASQ1 / Calsequestrin 1 Antibody for WB/Western LS-C155368CASQ1 / Calsequestrin 1 Antibody for WB/Western LS-C155368

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 ...
more infohttps://www.lsbio.com/antibodies/casq1-antibody-calsequestrin-1-antibody-wb-western-ls-c155368/162211

Sequence Similarity 









- 1SJI: Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a...Sequence Similarity - 1SJI: Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a...

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 ...
more infohttp://www.rcsb.org/pdb/explore/sequenceCluster.do?structureId=1SJI

Bioinspired Colorimetric Detection of Calcium(II) Ions in Serum Using Calsequestrin-Functionalized
      Gold Nanoparticles.Bioinspired Colorimetric Detection of Calcium(II) Ions in Serum Using Calsequestrin-Functionalized Gold Nanoparticles.

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 ...
more infohttps://www.docme.ru/doc/1908056/bioinspired-colorimetric-detection-of-calcium-ii--ions-in..

Modest reductions of cardiac calsequestrin increase sarcoplasmic reticulum Ca2+ leak independent of luminal Ca2+ and trigger...Modest reductions of cardiac calsequestrin increase sarcoplasmic reticulum Ca2+ leak independent of luminal Ca2+ and trigger...

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 ...
more infohttp://www.biomedsearch.com/nih/Modest-reductions-cardiac-calsequestrin-increase/17656677.html

cardiac ryanodine receptor luminal Ca2+ sensor governs Ca2+ waves, ventricular tachyarrhythmias and cardiac hypertrophy in...cardiac ryanodine receptor luminal Ca2+ sensor governs Ca2+ waves, ventricular tachyarrhythmias and cardiac hypertrophy in...

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 ...
more infohttps://portlandpress.com/biochemj/article/461/1/99/46780/The-cardiac-ryanodine-receptor-luminal-Ca2-sensor

Luminal Ca2+ Regulation of Single Cardiac Ryanodine Receptors: Insights Provided by Calsequestrin and its Mutants | JGPLuminal Ca2+ Regulation of Single Cardiac Ryanodine Receptors: Insights Provided by Calsequestrin and its Mutants | JGP

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. ...
more infohttp://jgp.rupress.org/content/131/4/325

Cardiac Calsequestrin Phosphorylation And Trafficking In The Mammalian Cardiomyocyte  by Timothy Mcfarland"Cardiac Calsequestrin Phosphorylation And Trafficking In The Mammalian Cardiomyocyte " by Timothy Mcfarland

Mcfarland, Timothy, "Cardiac Calsequestrin Phosphorylation And Trafficking In The Mammalian Cardiomyocyte" (2011). Wayne State ...
more infohttps://digitalcommons.wayne.edu/oa_dissertations/176/

Measurement of RyR Permeability Reveals a Role of Calsequestrin in Termination of SR \(Ca^{2+}\) Release in Skeletal MuscleMeasurement 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. ...
more infohttps://dash.harvard.edu/handle/1/8480658

Causes of Myopathy due to calsequestrin and SERCA1 protein overload - RightDiagnosis.comCauses of Myopathy due to calsequestrin and SERCA1 protein overload - RightDiagnosis.com

... 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 ...
more infohttps://www.rightdiagnosis.com/m/myopathy_due_to_calsequestrin_and_serca1_protein_overload/causes.htm

Effects of prenatal glucocorticoid exposure on cardiac calreticulin and calsequestrin protein expression during early...Effects of prenatal glucocorticoid exposure on cardiac calreticulin and calsequestrin protein expression during early...

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 ...
more infohttp://www.biochemj.org/content/371/1/61

Get PDF - Characterization of fast-twitch and slow-twitch skeletal muscles of calsequestrin 2 (CASQ2)-knock out mice:...Get PDF - Characterization of fast-twitch and slow-twitch skeletal muscles of calsequestrin 2 (CASQ2)-knock out mice:...

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 ...
more infohttps://eurekamag.com/research/059/490/059490025.php

Gentaur Molecular :Ray Biotech \ Native Canine Calsequestrin \ 228-10167-2Gentaur Molecular :Ray Biotech \ Native Canine Calsequestrin \ 228-10167-2

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 ...
more infohttp://www.antibody-antibodies.com/product_det.php?id=1783180&supplier=search&name=Native%20Canine%20Calsequestrin

Buy Recombinant Human Calsequestrin Protein (pro-799)Buy Recombinant Human Calsequestrin Protein (pro-799)

Buy online Recombinant Human Calsequestrin Protein from Prospec cat# pro-799. ProteoGenix provides you the best Recombinant ...
more infohttps://www.proteogenix-products.com/2776-casq2.html

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- ... 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, ...
more infohttps://kops.uni-konstanz.de/handle/123456789/6592

Human Calsequestrin-1 / CASQ1 Gene ORF cDNA clone expression plasmid, N-HA tag | SinoBiologicalHuman Calsequestrin-1 / CASQ1 Gene ORF cDNA clone expression plasmid, N-HA tag | SinoBiological

human Calsequestrin-1 / CASQ1 gene cDNA, cloning vector & expression plasmid, mutiple tags. Optimized for high expression in ... Two forms of calsequestrin have been identified: Calsequestrin-2 and Calsequestrin-1. Calsequestrin-1 is found in fast skeletal ... Calsequestrin-1 is an isoform of calsequestrin. Calsequestrin is a calcium-binding protein of the sarcoplasmic reticulum. It ... Calsequestrin-1 / CASQ1. Gene Clone CRO Service. *. Calsequestrin-1 / CASQ1. Gene Expression-Ready Vector Construction CRO ...
more infohttps://www.sinobiological.com/commodity_101128_casq1_cdna-clone.html

Regulation of Ryanodine receptors by Calsequestrin: Effect of high luminal Ca2+ and phosphorylation<...Regulation of Ryanodine receptors by Calsequestrin: Effect of high luminal Ca2+ and phosphorylation<...

4 mM dissociates calsequestrin from junctional face membrane, whereas in the range of 1-3 mM calsequestrin remains attached; 2 ... 4 mM dissociates calsequestrin from junctional face membrane, whereas in the range of 1-3 mM calsequestrin remains attached; 2 ... 4 mM dissociates calsequestrin from junctional face membrane, whereas in the range of 1-3 mM calsequestrin remains attached; 2 ... 4 mM dissociates calsequestrin from junctional face membrane, whereas in the range of 1-3 mM calsequestrin remains attached; 2 ...
more infohttps://researchprofiles.canberra.edu.au/en/publications/regulation-of-ryanodine-receptors-by-calsequestrin-effect-of-high

Head-to-tail oligomerization of calsequestrin: A novel mechanism for heterogeneous distribution of endoplasmic reticulum...Head-to-tail oligomerization of calsequestrin: A novel mechanism for heterogeneous distribution of endoplasmic reticulum...

keywords = "Calsequestrin, Calsequestrin mutants, Condensation, Endo/sarcoplasmic reticulum, L6 and HeLa cells", ... Gatti G, Trifari S, Mesaeli N, Parker JMR, Michalak M, Meldolesi J. Head-to-tail oligomerization of calsequestrin: A novel ... Gatti, G, Trifari, S, Mesaeli, N, Parker, JMR, Michalak, M & Meldolesi, J 2001, Head-to-tail oligomerization of calsequestrin ... Among the latter is calsequestrin (CSQ), the major Ca2+-binding protein condensed within both the terminal cisternae of ...
more infohttps://qfrd.pure.elsevier.com/en/publications/head-to-tail-oligomerization-of-calsequestrin-a-novel-mechanism-f
  • Recombinant fragment corresponding to a region within amino acids 136 and 381 of Calsequestrin 1 (SwissProt P31415). (lsbio.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)