Structural Differences between Cardiac and Skeletal Ryanodine Receptors
نویسندگان
چکیده
منابع مشابه
Molecular interaction between nitric oxide and ryanodine receptors of skeletal and cardiac sarcoplasmic reticulum.
In striated muscle, the sarcoplasmic reticulum (SR) is the major storage compartment of intracellular Ca2+ that controls cytosolic free Ca2+ (Cai) and developed force by sequestering and releasing Ca2+ during each contraction. Ca2+ release from the SR occurs through high-conductance Ca2+ release channels or ryanodine receptors (RyR), which are regulated by various signaling processes. Over the ...
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Excitation-contraction coupling in heart muscle requires the activation of Ca(2+)-release channels/type 2 ryanodine receptors (RyR2s) by Ca(2+) influx. RyR2s are arranged on the sarcoplasmic reticular membrane in closely packed arrays such that their large cytoplasmic domains contact one another. We now show that multiple RyR2s can be isolated under conditions such that they remain physically c...
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Ryanodine receptors (RyRs) and inositol triphosphate receptors (InsP3Rs) are structurally related intracellular calcium release channels that participate in multiple primary or secondary amplified Ca(2+) signals, triggering muscle contraction and oscillatory Ca(2+) waves, or activating transcription factors. In the heart, RyRs play an indisputable role in the process of excitation-contraction c...
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Fruen, Bradley R., Jennifer M. Bardy, Todd M. Byrem, Gale M. Strasburg, and Charles F. Louis. Differential Ca sensitivity of skeletal and cardiac muscle ryanodine receptors in the presence of calmodulin. Am J Physiol Cell Physiol 279: C724–C733, 2000.—Calmodulin (CaM) activates the skeletal muscle ryanodine receptor Ca release channel (RyR1) in the presence of nanomolar Ca concentrations. Howev...
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Abnormalities in intracellular calcium release and reuptake are responsible for decreased contractility in heart failure (HF). We have previously shown that cardiac ryanodine receptors (RyRs) are protein kinase A-hyperphosphorylated and depleted of the regulatory subunit calstabin-2 in HF. Moreover, similar alterations in skeletal muscle RyR have been linked to increased fatigability in HF. To ...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2017
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2016.11.549