Abstract
[3H]Ryanodine binds with high affinity to saturable and Ca2+-dependent sites in heavy sarcoplasmic reticulum (SR) preparations from rabbit skeletal and cardiac muscle. Ruthenium red, known to interfere with Ca2+-induced Ca2+ release from SR vesicles, inhibits [3H]ryanodine specific binding in both skeletal and cardiac preparations whereas Mg2+, Ba2+, Cd2+ and La3+ selectively inhibit the skeletal preparation. The toxicological relevance of the [3H]ryanodine binding site is established by the correlation of binding inhibition with toxicity for seven ryanoids including two botanical insecticides. These findings provide direct evidence for Ca2+-ryanodine receptor complexes that may play a role in excitation-contraction coupling.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 449-456 |
| Number of pages | 8 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 128 |
| Issue number | 1 |
| DOIs | |
| State | Published - Apr 16 1985 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
The calcium-Ryanodine receptor complex of skeletal and cardiac muscle. / Pessah, Isaac N; Waterhouse, Andrew L.; Casida, John E.
In: Biochemical and Biophysical Research Communications, Vol. 128, No. 1, 16.04.1985, p. 449-456.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The calcium-Ryanodine receptor complex of skeletal and cardiac muscle
AU - Pessah, Isaac N
AU - Waterhouse, Andrew L.
AU - Casida, John E.
PY - 1985/4/16
Y1 - 1985/4/16
N2 - [3H]Ryanodine binds with high affinity to saturable and Ca2+-dependent sites in heavy sarcoplasmic reticulum (SR) preparations from rabbit skeletal and cardiac muscle. Ruthenium red, known to interfere with Ca2+-induced Ca2+ release from SR vesicles, inhibits [3H]ryanodine specific binding in both skeletal and cardiac preparations whereas Mg2+, Ba2+, Cd2+ and La3+ selectively inhibit the skeletal preparation. The toxicological relevance of the [3H]ryanodine binding site is established by the correlation of binding inhibition with toxicity for seven ryanoids including two botanical insecticides. These findings provide direct evidence for Ca2+-ryanodine receptor complexes that may play a role in excitation-contraction coupling.
AB - [3H]Ryanodine binds with high affinity to saturable and Ca2+-dependent sites in heavy sarcoplasmic reticulum (SR) preparations from rabbit skeletal and cardiac muscle. Ruthenium red, known to interfere with Ca2+-induced Ca2+ release from SR vesicles, inhibits [3H]ryanodine specific binding in both skeletal and cardiac preparations whereas Mg2+, Ba2+, Cd2+ and La3+ selectively inhibit the skeletal preparation. The toxicological relevance of the [3H]ryanodine binding site is established by the correlation of binding inhibition with toxicity for seven ryanoids including two botanical insecticides. These findings provide direct evidence for Ca2+-ryanodine receptor complexes that may play a role in excitation-contraction coupling.
UR - http://www.scopus.com/inward/record.url?scp=0022395442&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0022395442&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(85)91699-7
DO - 10.1016/0006-291X(85)91699-7
M3 - Article
C2 - 3985981
AN - SCOPUS:0022395442
VL - 128
SP - 449
EP - 456
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -