High affinity ryanodine binding sites in rat liver endoplasmic reticulum

Varda Shoshan-Barmatz

doi:10.1016/0014-5793(90)81403-B

High affinity ryanodine binding sites in rat liver endoplasmic reticulum

Varda Shoshan-Barmatz

Department of Life Sciences

Research output: Contribution to journal › Article › peer-review

35 Scopus citations

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 (< 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⁺.

Original language	English
Pages (from-to)	317-320
Number of pages	4
Journal	FEBS Letters
Volume	263
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(90)81403-B
State	Published - 24 Apr 1990

Keywords

Ca release
Caffeine
Endoplasmic reticulum
Ryanodine

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(90)81403-B

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title = "High affinity ryanodine binding sites in rat liver endoplasmic reticulum",

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 (< 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+.",

keywords = "Ca release, Caffeine, Endoplasmic reticulum, Ryanodine",

author = "Varda Shoshan-Barmatz",

note = "Funding Information: Acknowledgements: This research was supported by PHS Grant NDDK-DK-36916. We thank S. Higham for technical assistance and Drs T. Nelson and A. Chu for helpful suggestions.",

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T1 - High affinity ryanodine binding sites in rat liver endoplasmic reticulum

AU - Shoshan-Barmatz, Varda

N1 - Funding Information: Acknowledgements: This research was supported by PHS Grant NDDK-DK-36916. We thank S. Higham for technical assistance and Drs T. Nelson and A. Chu for helpful suggestions.

PY - 1990/4/24

Y1 - 1990/4/24

N2 - 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+.

AB - 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+.

KW - Ca release

KW - Caffeine

KW - Endoplasmic reticulum

KW - Ryanodine

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DO - 10.1016/0014-5793(90)81403-B

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EP - 320

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

High affinity ryanodine binding sites in rat liver endoplasmic reticulum

Abstract

Keywords

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