calsequestrin 2
Última atualização 20 May 2021
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A CASQ2 gene provides instructions for making a protein called calsequestrin 2. This protein is found in heart (cardiac) muscle cells called myocytes, where it is involved in the storage and transport of positively charged calcium atoms (calcium ions).
Normal function
A CASQ2 gene provides instructions for making a protein called calsequestrin 2. This protein is found in heart (cardiac) muscle cells called myocytes, where it is involved in the storage and transport of positively charged calcium atoms (calcium ions).
Within myocytes, calsequestrin 2 is located in a cell structure called the sarcoplasmic reticulum, which acts as a storage center for calcium ions. Most of these ions are stored by attaching (binding) to calsequestrin 2. This protein also helps regulate a protein called the RYR2 channel, which controls the flow of calcium ions out of the sarcoplasmic reticulum.
For the heart to beat normally, the cardiac muscle must tense (contract) and relax in a coordinated way. This cycle of muscle contraction and relaxation results from the precise control of calcium ions within myocytes. In response to certain signals, calcium ions stored by calsequestrin 2 in the sarcoplasmic reticulum are released into the surrounding cell fluid (the cytoplasm). The resulting increase in calcium ion concentration triggers the cardiac muscle to contract, which pumps blood out of the heart. Calcium ions are then transported back into the sarcoplasmic reticulum, and the cardiac muscle relaxes. In this way, the release and reuptake of calcium ions in myocytes produces a regular heart rhythm.
Conditions referring to this gene or chromosome
Other names
calsequestrin 2 (cardiac muscle)
calsequestrin 2, fast-twitch, cardiac muscle
cardiac calsequestrin 2
CASQ2_HUMAN
PDIB2
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Leitura adicional e referências
- calsequestrin 2; MedlinePlus, National Library of Medicine.
- Cerrone M, Napolitano C, Priori SG. Catecholaminergic polymorphic ventricular tachycardia: A paradigm to understand mechanisms of arrhythmias associated to impaired Ca(2+) regulation. Heart Rhythm. 2009 Nov;6(11):1652-9. doi: 10.1016/j.hrthm.2009.06.033. Epub 2009 Jun 30.
- di Barletta MR, Viatchenko-Karpinski S, Nori A, Memmi M, Terentyev D, Turcato F, Valle G, Rizzi N, Napolitano C, Gyorke S, Volpe P, Priori SG. Clinical phenotype and functional characterization of CASQ2 mutations associated with catecholaminergic polymorphic ventricular tachycardia. Circulation. 2006 Sep 5;114(10):1012-9. doi: 10.1161/CIRCULATIONAHA.106.623793. Epub 2006 Aug 14.
- Gyorke S. Molecular basis of catecholaminergic polymorphic ventricular tachycardia. Heart Rhythm. 2009 Jan;6(1):123-9. doi: 10.1016/j.hrthm.2008.09.013. Epub 2008 Sep 16.
- Katz G, Arad M, Eldar M. Catecholaminergic polymorphic ventricular tachycardia from bedside to bench and beyond. Curr Probl Cardiol. 2009 Jan;34(1):9-43. doi: 10.1016/j.cpcardiol.2008.09.002.
- Liu N, Priori SG. Disruption of calcium homeostasis and arrhythmogenesis induced by mutations in the cardiac ryanodine receptor and calsequestrin. Cardiovasc Res. 2008 Jan 15;77(2):293-301. doi: 10.1093/cvr/cvm004. Epub 2007 Aug 14.
- Mohamed U, Napolitano C, Priori SG. Molecular and electrophysiological bases of catecholaminergic polymorphic ventricular tachycardia. J Cardiovasc Electrophysiol. 2007 Jul;18(7):791-7. doi: 10.1111/j.1540-8167.2007.00766.x.
- Postma AV, Denjoy I, Hoorntje TM, Lupoglazoff JM, Da Costa A, Sebillon P, Mannens MM, Wilde AA, Guicheney P. Absence of calsequestrin 2 causes severe forms of catecholaminergic polymorphic ventricular tachycardia. Circ Res. 2002 Oct 18;91(8):e21-6. doi: 10.1161/01.res.0000038886.18992.6b.
- Terentyev D, Nori A, Santoro M, Viatchenko-Karpinski S, Kubalova Z, Gyorke I, Terentyeva R, Vedamoorthyrao S, Blom NA, Valle G, Napolitano C, Williams SC, Volpe P, Priori SG, Gyorke S. Abnormal interactions of calsequestrin with the ryanodine receptor calcium release channel complex linked to exercise-induced sudden cardiac death. Circ Res. 2006 May 12;98(9):1151-8. doi: 10.1161/01.RES.0000220647.93982.08. Epub 2006 Apr 6.
- Valle G, Galla D, Nori A, Priori SG, Gyorke S, de Filippis V, Volpe P. Catecholaminergic polymorphic ventricular tachycardia-related mutations R33Q and L167H alter calcium sensitivity of human cardiac calsequestrin. Biochem J. 2008 Jul 15;413(2):291-303. doi: 10.1042/BJ20080163.
- Viatchenko-Karpinski S, Terentyev D, Gyorke I, Terentyeva R, Volpe P, Priori SG, Napolitano C, Nori A, Williams SC, Gyorke S. Abnormal calcium signaling and sudden cardiac death associated with mutation of calsequestrin. Circ Res. 2004 Mar 5;94(4):471-7. doi: 10.1161/01.RES.0000115944.10681.EB. Epub 2004 Jan 8.
- Wang Q, Michalak M. Calsequestrin. Structure, function, and evolution. Cell Calcium. 2020 Sep;90:102242. doi: 10.1016/j.ceca.2020.102242. Epub 2020 Jun 20.
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