Lokuta Andrew J, Komai Hirochika, McDowell Thomas S, Valdivia Héctor H
Department of Physiology, University of Wisconsin Medical School, Madison, WI 53706, USA.
FEBS Lett. 2002 Jan 30;511(1-3):90-6. doi: 10.1016/s0014-5793(01)03312-9.
The properties of ryanodine receptors (RyRs) from rat dorsal root ganglia (DRGs) have been studied. The density of RyRs (Bmax) determined by [3H]ryanodine binding was 63 fmol/mg protein with a dissociation constant (Kd) of 1.5 nM. [3H]Ryanodine binding increased with caffeine, decreased with ruthenium red and tetracaine, and was insensitive to millimolar concentrations of Mg2+ or Ca2+. DRG RyRs reconstituted in planar lipid bilayers were Ca2+-dependent and displayed the classical long-lived subconductance state in response to ryanodine; however, unlike cardiac and skeletal RyRs, they lacked Ca2+-dependent inactivation. Antibodies against RyR3, but not against RyR1 or RyR2, detected DRG RyRs. Thus, DRG RyRs are immunologically related to RyR3, but their lack of divalent cation inhibition is unique among RyR subtypes.
对大鼠背根神经节（DRG）中兰尼碱受体（RyRs）的特性进行了研究。通过[3H]兰尼碱结合测定的RyRs密度（Bmax）为63 fmol/mg蛋白质，解离常数（Kd）为1.5 nM。[3H]兰尼碱结合随咖啡因增加，随钌红和丁卡因降低，并且对毫摩尔浓度的Mg2+或Ca2+不敏感。重构于平面脂质双分子层中的DRG RyRs依赖于Ca2+，并在对兰尼碱的反应中表现出经典的长寿命亚电导状态；然而，与心肌和骨骼肌RyRs不同，它们缺乏Ca2+依赖性失活。抗RyR3抗体而非抗RyR1或RyR2抗体可检测到DRG RyRs。因此，DRG RyRs在免疫上与RyR3相关，但它们缺乏二价阳离子抑制在RyR亚型中是独特的。
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