High affinity ryanodine binding sites in rat liver endoplasmic reticulum

FEBS Letters

Shoshan-Barmatz, Varda¹ 

[1] Deparment of Biology, Ben-Gurion University of the Negev, Beer-Sheva, Israel

关键词: Endoplasmic reticulum;    Ryanodine;    Caffeine;    Ca2+ release;    EGTA;    [ethylenebis(oxyethylenenitrilo)]tetraacetic acid;    MOPS;    3-(N-morpholino)propanesulfonic acid;    SDS;    sodium dodecyl sulfate;    ER;    endoplasmic reticulum;    SR;    sareoplasmic reticulum;   

DOI  :  10.1016/0014-5793(90)81403-B

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The binding of [³H]ryanodine to liver microsomal subfractions was investigated. The smooth microsomal membranes were enriched with ryanodine binding sites and also with a polypeptide of 360 kDa. Caffeine completely inhibited [³H]ryanodine binding. Ryanodine also affected the membrane Ca²⁺ permeability. At low concentrations (< 10 μM) ryanodine stimulated Ca²⁺ efflux and at higher concentrations (> 50 μM) it blocked Ca²⁺ efflux. These results suggest that hepatic microsomes contain ryanodine binding sites which can modify the membrane permeability for Ca²⁺.

【 授权许可】

Unknown