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The interaction between ruthenium red and the isolated sarcoplasmic reticulum
Membrane Biochemistry
|January 1, 1982
Summary
Multivalent anions like ATP and oxalate reduce ruthenium red binding to sarcoplasmic reticulum (SR). This suggests SR calcium transport is less sensitive to ruthenium red inhibition than mitochondrial transport.
Area of Science:
- Biochemistry
- Cell Biology
- Physiology
Background:
- Sarcoplasmic reticulum (SR) plays a crucial role in calcium ion (Ca2+) regulation within muscle cells.
- Ruthenium red (RR) is a known inhibitor of calcium transport, particularly in mitochondria.
- The interaction of RR with SR and its effects on calcium uptake and ATPase activity require further elucidation.
Purpose of the Study:
- To investigate the effect of multivalent anions, specifically ATP and oxalate, on ruthenium red (RR) binding to isolated sarcoplasmic reticulum (SR) preparations.
- To determine the susceptibility of SR calcium transport to RR inhibition compared to mitochondrial calcium transport.
Main Methods:
- Incubation of isolated SR preparations with varying concentrations of ATP and oxalate.
- Measurement of ruthenium red (RR) binding to SR.
- Assessment of RR's inhibitory effects on SR calcium uptake and ATPase activity.
Main Results:
- 5mM concentrations of ATP and oxalate significantly reduced RR binding to SR.
- At lower ATP concentrations and without oxalate, RR exhibited partial inhibition of SR calcium uptake and ATPase activity.
- SR calcium transport demonstrated considerably lower susceptibility to RR inhibition compared to mitochondrial calcium transport.
Conclusions:
- Multivalent anions, such as ATP and oxalate, likely suppress RR's effect on SR by forming soluble complexes with RR.
- SR calcium transport is inherently less sensitive to RR inhibition than mitochondrial calcium transport.