Cardiac calsequestrin: quest inside the SR
| Autor: | Sandor Gyorke, Dmitry Terentyev, Sarah C.W. Stevens |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Tachycardia
Gene isoform medicine.medical_specialty Physiology Biology Calsequestrin Catecholaminergic polymorphic ventricular tachycardia Symposium Section Reviews and Perspectives: Calsequestrin Triadin and More Mice Internal medicine medicine Animals Humans Calcium Signaling Calcium signaling Mice Knockout Endoplasmic reticulum Binding protein Models Cardiovascular Cardiac muscle Heart medicine.disease Rats Sarcoplasmic Reticulum Endocrinology medicine.anatomical_structure Mutation Tachycardia Ventricular cardiovascular system medicine.symptom |
| Zdroj: | The Journal of Physiology. 587:3091-3094 |
| ISSN: | 0022-3751 |
| Popis: | Although calsequestrin (CASQ), a major sarcoplasmic reticulum (SR) Ca2+ binding protein, was discovered more than 30 years ago, its precise roles and modes of operation in both skeletal and cardiac muscle remain to be elucidated (Rios, 2009, this issue; Knollmann, 2009, this issue). Recent years witnessed a significant surge of interest in this Ca2+ binding protein after mutations in the gene encoding the cardiac isoform of calsequestrin (CASQ2) were linked to exercise-induced cardiac death due to catecholaminergic polymorphic ventricular tachycardia (CPVT) (Postma et al. 2002; Eldar et al. 2003). Surprisingly, humans and genetically altered mice devoid of CASQ2 preserve nearly normal cardiac structure and function but develop lethal arrhythmias under conditions of adrenergic stimulation (Postma et al. 2002; Knollmann et al. 2006; Song et al. 2007). Here we provide a brief overview of our current understanding of the functional role and mode of operation of CASQ2 in the heart, of how hearts missing CASQ2 cope in the absence of this protein and of the mechanisms of CPVT. |
| Databáze: | OpenAIRE |
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