High affinity ryanodine binding sites in rat liver endoplasmic reticulum - PubMed (original) (raw)

High affinity ryanodine binding sites in rat liver endoplasmic reticulum

V Shoshan-Barmatz. FEBS Lett. 1990.

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Abstract

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 (less than 10 microM) ryanodine stimulated Ca2+ efflux and at higher concentrations (greater than 50 microM) it blocked Ca2+ efflux. These results suggest that hepatic microsomes contain ryanodine binding sites which can modify the membrane permeability for Ca2+.

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