Genomes and Genes
Gene Symbol: Casq1
Description: calsequestrin 1
Alias: calsequestrin-1, Aspartactin, Laminin-binding protein, calsequestrin 1 (fast-twitch, skeletal muscle), calsequestrin, skeletal muscle isoform
- Nissinen M, Kaisto T, Salmela P, Peltonen J, Metsikkö K. Restricted distribution of mRNAs encoding a sarcoplasmic reticulum or transverse tubule protein in skeletal myofibers. J Histochem Cytochem. 2005;53:217-27 pubmed..In summary, the mRNAs encoding either a resident SR protein or a transverse tubule protein were located beneath the sarcolemma, implying that translocation of the respective proteins to the lumen of ER takes place at this location. ..
- Tomasi M, Canato M, Paolini C, Dainese M, Reggiani C, Volpe P, et al. Calsequestrin (CASQ1) rescues function and structure of calcium release units in skeletal muscles of CASQ1-null mice. Am J Physiol Cell Physiol. 2012;302:C575-86 pubmed publisher..composition of sarcoplasmic reticulum (SR) are altered in fast-twitch skeletal muscles of calsequestrin-1 (CASQ1)-null mice...
- Dainese M, Quarta M, Lyfenko A, Paolini C, Canato M, Reggiani C, et al. Anesthetic- and heat-induced sudden death in calsequestrin-1-knockout mice. FASEB J. 2009;23:1710-20 pubmed publisherCalsequestrin-1 (CASQ1) is a moderate-affinity, high-capacity Ca(2+)-binding protein in the sarcoplasmic reticulum (SR) terminal cisternae of skeletal muscle...
- Hasstedt S, Chu W, Das S, Wang H, Elbein S. Type 2 diabetes susceptibility genes on chromosome 1q21-24. Ann Hum Genet. 2008;72:163-9 pubmed publisher..The significant variant pairs were apolipoprotein A-II (APOA2) rs6413453 interacting with calsequestrin 1 (CASQ1) rs617698, dual specificity phosphatase 12 (DUSP12) rs1503814, and retinoid X receptor gamma (RXRG) ..
- Zhang L, Wang L, Li S, Xue J, Luo D. Calsequestrin-1 Regulates Store-Operated Ca2+ Entry by Inhibiting STIM1 Aggregation. Cell Physiol Biochem. 2016;38:2183-93 pubmed publisher..Our results demonstrate that CSQ1 monomers suppress SOCE by interacting with STIM1 and attenuating STIM1 aggregation via its C-terminal amino acid 362-396. ..
- Hunter R, Mitchell Felton H, Essig D, Kandarian S. Expression of endoplasmic reticulum stress proteins during skeletal muscle disuse atrophy. Am J Physiol Cell Physiol. 2001;281:C1285-90 pubmed..However, the upregulation of HO-1 may indicate ER adaptation to oxidative stress during muscle unloading...
- Donoghue P, Ribaric S, Moran B, Cebasek V, Erzen I, Ohlendieck K. Early effects of denervation on Ca(2+)-handling proteins in skeletal muscle. Int J Mol Med. 2004;13:767-72 pubmed..Hence, changes in muscle activity appear to have a profound effect on the abundance and isoform expression pattern of Ca(2+)-handling elements...
- Bataille N, Schmitt N, Aumercier Maes P, Ollivier B, Lucas Heron B, Lestienne P. Molecular cloning of human calmitine, a mitochondrial calcium binding protein, reveals identity with calsequestrine. Biochem Biophys Res Commun. 1994;203:1477-82 pubmed..Calmitine represents the Ca2+ reservoir of mitochondria, the function of which could be similar to what has been reported for calsequestrine in the sarcoplasmic reticulum. ..
- Jorgensen A, Shen A, Campbell K, MacLennan D. Ultrastructural localization of calsequestrin in rat skeletal muscle by immunoferritin labeling of ultrathin frozen sections. J Cell Biol. 1983;97:1573-81 pubmed
- Ohlendieck K, Harmon S, Koll M, Paice A, Preedy V. Ca2+-regulatory muscle proteins in the alcohol-fed rat. Metabolism. 2003;52:1102-12 pubmed..0950). We conclude that upregulation of SERCA1 protein and Ca(2+)-ATPase activity may be an adaptive mechanism and/or a contributory process in the pathology of alcohol-induced muscle disease. ..
- Nori A, Furlan S, Patiri F, Cantini M, Volpe P. Site-directed mutagenesis and deletion of three phosphorylation sites of calsequestrin of skeletal muscle sarcoplasmic reticulum. Effects on intracellular targeting. Exp Cell Res. 2000;260:40-9 pubmed..Thus, the targeting mechanism of CS in vivo is not affected by phosphorylation(s); i.e., sorting and segregation of CS appear to be independent of posttranslational phosphorylation(s). ..
- Nori A, Bortoloso E, Frasson F, Valle G, Volpe P. Vesicle budding from endoplasmic reticulum is involved in calsequestrin routing to sarcoplasmic reticulum of skeletal muscles. Biochem J. 2004;379:505-12 pubmed..It also appears that CS routing from ER to SR does not involve classical secretory pathways through ER-Golgi intermediate compartments, cis -medial Golgi and trans -Golgi network. ..
- Tharin S, Hamel P, Conway E, Michalak M, Opas M. Regulation of calcium binding proteins calreticulin and calsequestrin during differentiation in the myogenic cell line L6. J Cell Physiol. 1996;166:547-60 pubmed..Calreticulun, but not calsequestrin, staining was also observed in the perinuclear region. These data suggest that expression of calreticulin and calsequestrin may be under different control during myogenesis in rat L6 cells in culture. ..
- Lee D, Michalak M. Membrane associated Ca2+ buffers in the heart. BMB Rep. 2010;43:151-7 pubmed..The Ca2+ homeostasis regulated by the endoplasmic and sarcoplasmic reticulum is critical for the development and proper function of the heart. ..
- Howarth F, Glover L, Culligan K, Qureshi M, Ohlendieck K. Calsequestrin expression and calcium binding is increased in streptozotocin-induced diabetic rat skeletal muscle though not in cardiac muscle. Pflugers Arch. 2002;444:52-8 pubmed..An increased Ca2+-buffering capacity of the sarcoplasmic reticulum lumen might counteract elevated cytosolic Ca2+ levels in diabetes thereby preventing Ca2+-dependent myo-necrosis. ..
- Goodman C, Horvath D, Stathis C, Mori T, Croft K, Murphy R, et al. Taurine supplementation increases skeletal muscle force production and protects muscle function during and after high-frequency in vitro stimulation. J Appl Physiol (1985). 2009;107:144-54 pubmed publisher..Also, we demonstrate that raising Tau protects muscle function during high-frequency in vitro stimulation and the ensuing recovery period and helps reduce oxidative stress during prolonged stimulation. ..
- Sanchez E, Lewis K, Danna B, Kang C. High-capacity Ca2+ binding of human skeletal calsequestrin. J Biol Chem. 2012;287:11592-601 pubmed publisher..On the basis of these findings, we propose a mechanism for the observed in vitro and in vivo dynamic high-capacity and low-affinity Ca(2+)-binding activity of calsequestrin...
- Zheng Y, Wang L, Zhu Z, Yan X, Zhang L, Xu P, et al. Altered platelet calsequestrin abundance, Na?/Ca²? exchange and Ca²? signaling responses with the progression of diabetes mellitus. Thromb Res. 2014;134:674-81 pubmed publisher..Besides the downregulation of CSQ-1 that mainly disrupts basal Ca(2+) homeostasis, insufficient Na(+)/Ca(2+) exchange also contributes, at least in part, to the hyperactive Ca(2+) response to stimulation in diabetic platelets. ..
- Das S, Chu W, Zhang Z, Hasstedt S, Elbein S. Calsquestrin 1 (CASQ1) gene polymorphisms under chromosome 1q21 linkage peak are associated with type 2 diabetes in Northern European Caucasians. Diabetes. 2004;53:3300-6 pubmed..We identified two SNPs that showed strong associations, and both mapped to within intron 2 of the calsequestrin 1 (CASQ1) gene...
- Greenway D, MacLennan D. Assembly of the sarcoplasmic reticulum. Synthesis of calsequestrin and the Ca2+ + Mg2+ -adenosine triphosphatase on membrane-bound polyribosomes. Can J Biochem. 1978;56:452-6 pubmed..The disposition of the ATPase during synthesis is, as yet, unknown. ..