Functional properties of ryanodine receptors from rat dorsal root ganglia

FEBS Letters

Lokuta, Andrew J.²  Komai, Hirochika¹  McDowell, Thomas S.¹  Valdivia, Héctor H.² 

[1] Department of Anesthesiology, University of Wisconsin Medical School, 1300 University Avenue, Madison, WI 53706, USA;Department of Physiology, University of Wisconsin Medical School, 1300 University Avenue, Madison, WI 53706, USA

关键词: Calcium release channel;    Ryanodine receptor;    Dorsal root ganglion;    Calcium-induced calcium release;    [3H]Ryanodine binding;    Planar lipid bilayer;    CICR;    Ca2+-induced Ca2+ release;    DRG;    dorsal root ganglion;    P o;    open probability;    RyR;    ryanodine receptor;   

DOI  :  10.1016/S0014-5793(01)03312-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The properties of ryanodine receptors (RyRs) from rat dorsal root ganglia (DRGs) have been studied. The density of RyRs (B _max) determined by [³H]ryanodine binding was 63 fmol/mg protein with a dissociation constant (K _d) 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.

【 授权许可】

Unknown