• Characterization and localization to human chromosome 1 of human fast-twitch skeletal muscle calsequestrin gene. (uchicago.edu)
  • Recent data support the role of flecainide in preventing ventricular tachyarrhythmias in patients with catecholaminergic polymorphic ventricular tachycardia associated both with ryanodine receptor and calsequestrin mutations. (wjgnet.com)
  • The key proteins in this store are the Ca2+ binding protein calsequestrin (CSQ), the ryanodine receptor (RyR) Ca2+ release channel and triadin and junctin (Beard et al. (edu.au)
  • Chen H, Valle G, Furlan S, Nani A, Gyorke S, Fill M, Volpe P. Mechanism of calsequestrin regulation of single cardiac ryanodine receptor in normal and pathological conditions. (rush.edu)
  • Some of these isoforms are found in complexes with calsequestrin, triadin, and the ryanodine receptor, and have been shown to regulate calcium release from the sarcoplasmic reticulum. (antibodypedia.com)
  • It is usually inherited as an autosomal dominant mutation of the gene encoding the cardiac ryanodine receptor, but it may be inherited as an autosomal recessive mutation of cardiac calsequestrin ( CASQ2 ). (msdmanuals.com)
  • Phosphorylation of cardiac and skeletal muscle calsequestrin isoforms by casein kinase II. (wikipedia.org)
  • Calsequestrin functions as a luminal sarcoplasmic reticulum calcium sensor in both cardiac and skeletal muscle cells. (nih.gov)
  • This antibody recognizes both cardiac and skeletal muscle calsequestrin. (abcam.cn)
  • We have investigated the expression of calsequestrin and Ca 2+ binding in cardiac and skeletal muscle from streptozotocin-induced diabetic rat. (uaeu.ac.ae)
  • 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)
  • Calsequestrin is a calcium-binding protein that acts as a calcium buffer within the sarcoplasmic reticulum. (wikipedia.org)
  • This gene encodes the skeletal muscle specific member of the calsequestrin protein family. (nih.gov)
  • Full length native protein (purified) corresponding to Dog Calsequestrin 2. (abcam.cn)
  • This antibody detects an ~55 kDa protein representing Calsequestrin from canine cardiac extract. (abcam.cn)
  • Calsequestrin, a high-capacity Ca 2+ -binding protein, is involved in the regulation of the excitation-contraction-relaxation cycle of both skeletal and cardiac muscle fibres. (uaeu.ac.ae)
  • In a clinical collaboration with Melvin Scheinman from the UCSF Comprehensive Genetic Arrythmia Program, CVRI investigators Rahul Deo and Natalia Jura, along with MD/PhD trainee Erron Titus, set out to explain how mutations in the calcium-storage protein, calsequestrin, cause lethal arrhthymias. (ucsf.edu)
  • Western blot analysis on total heart homogenate showed no change in β-tubulin when data were normalized to either actin or calsequestrin, although there was a significant increase in failing human hearts when data were normalized only for a constant amount of protein per heart. (houstonmethodist.org)
  • Dr. Allen has been studying the protein-protein interactions in skeletal muscle excitation contraction coupling to discovery the function of RyR1, CaV1.1, Triadin, Calsequestrin, Junctin, CaVbeta1a and CaV alpha2 delta. (cardiac-muscle-society.org)
  • The release of calsequestrin-bound calcium (through a calcium release channel) triggers muscle contraction. (wikipedia.org)
  • Calsequestrin is also secreted in the gut where it deprives bacteria of calcium ions. (wikipedia.org)
  • In this sense, calsequestrin (CSQ) has emerged as a key calcium buffer that modifies the calcium handling. (upc.edu)
  • Mutations in the cardiac calsequestrin gene have been associated with cardiac arrhythmia and sudden death. (wikipedia.org)
  • A Calsequestrin-1 Mutation Associated with a Skeletal Muscle Disease Alters Sarcoplasmic Ca2+ Release. (nih.gov)
  • Calsequestrin 2: Sarcoplasmic reticulum lumen. (abcam.cn)
  • This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells. (abcam.cn)
  • Calsequestrin (CS) is segregated to the junctional sarcoplasmic reticulum (jSR) of skeletal muscle fibers and is responsible for intraluminal Ca(2+) binding. (unipd.it)
  • This correlated with an increased Ca(2+) content of the sarcoplasmic reticulum (SR). In MTSMC from T-bet KO mice, the expression of the SR Ca(2+) buffers calreticulin and calsequestrin was higher compared to wild- type mice. (uni-muenchen.de)
  • Calsequestrin is one of the most abundant proteins in muscle sarcoplasmic reticulum and featuring high capacity but low affinity for Ca2 + binding. (tetra-bio.com)
  • The calsequestrin gene is 8.6 kb in length and consists of 11 exons. (ualberta.ca)
  • Additional bands at 97 kDa may be observed and have been reported to be Calsequestrin-like proteins. (abcam.cn)
  • Immunoblotting of microsomal membranes from normal and streptozotocin-induced diabetic muscle revealed no significant changes in heart, but an increase in the relative abundance of calsequestrin and calsequestrin-like proteins in skeletal muscle. (uaeu.ac.ae)
  • Characterization of Two Human Skeletal Calsequestrin Mutants Implicated in Malignant Hyperthermia and Vacuolar Aggregate Myopathy. (nih.gov)
  • The team solved a new X-ray crystal structure of human cardiac calsequestrin, revealing the biochemical basis of calsequestrin's assembly into filaments. (ucsf.edu)
  • The up-regulation of the high-capacity Ca 2+ -binding element calsequestrin might represent a compensatory mechanism of diabetic skeletal muscle. (uaeu.ac.ae)
  • This abnormal Ca(2+) handling within the cell may be attributed to a reduction (2.4-fold) in calsequestrin expression in conjunction with an up-regulation (1.5-fold) of Na(+)-Ca(2+) exchanger. (fsu.edu)
  • We have isolated two overlapping 17-kilobase (kb) genomic clones which, together, encode the rabbit fasttwitch skeletal muscle calsequestrin. (ualberta.ca)
  • Each molecule of calsequestrin can bind 18 to 50 Ca2+ ions. (wikipedia.org)
  • Both forms of calsequestrin are phosphorylated by casein kinase 2, but the cardiac form is phosphorylated more rapidly and to a higher degree. (wikipedia.org)
  • Multimotored killed, https://www.testinformatica.it/ti-revia-antaxone-nalorex-narcoral-generici-del-naltrexone.html readdresses, even if pectinea ventolin broncovaleas italia - inguina inside subcelestial postorbital timed she calsequestrin ahead article of mine toploftier adequateness. (testinformatica.it)
  • Alpha blockade potentiates CPVT therapy in calsequestrin-mutant mice. (bvsalud.org)
  • Infante C, Ponce M, Manchado M. Duplication of calsequestrin genes in teleosts: molecular characterization in the Senegalese sole (Solea senegalensis). (ucdenver.edu)
  • Phosphorylation of cardiac and skeletal muscle calsequestrin isoforms by casein kinase II. (wikipedia.org)
  • 16. Egr-1 negatively regulates calsequestrin expression and calcium dynamics in ventricular cells. (nih.gov)
  • Each molecule of calsequestrin can bind 18 to 50 Ca2+ ions. (wikipedia.org)
  • Calsequestrin is also secreted in the gut where it deprives bacteria of calcium ions. (wikipedia.org)
  • Most of these ions are stored by attaching (binding) to calsequestrin 2. (medlineplus.gov)
  • Calsequestrin provides high local Ca 2+ at the junctional SR and communicates changes in luminal Ca 2+ concentration to Ca 2+ release channels, thus it is an essential component of excitation-contraction coupling. (nih.gov)
  • Here we provide a comprehensive overview of calsequestrin, with recent advances in structure, diverse functions, phylogenetic analysis, and its role in muscle physiology, stress responses and human pathology. (nih.gov)
  • Understand the role of cardiac calsequestrin in normal heart development and function. (nih.gov)
  • Nitric oxide may regulate cytoplasmic Ca(2+) level through conformational alterations of SERCA, and decreasing levels of calsequestrin in SR may also play regulatory role in SERCA activity and expression. (aston.ac.uk)
  • Two forms of calsequestrin have been identified. (wikipedia.org)
  • Both forms of calsequestrin are phosphorylated by casein kinase 2, but the cardiac form is phosphorylated more rapidly and to a higher degree. (wikipedia.org)