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Comparison between strontium and calcium uptake by the fragmented sarcoplasmic reticulum
European Journal of Biochemistry
|October 1, 1976
Summary
Strontium uptake by the sarcoplasmic reticulum is rapid and directly proportional to ATP hydrolysis, unlike calcium uptake. This process is not activated by inorganic phosphate (Pi).
Area of Science:
- Biochemistry
- Cell Biology
- Muscle Physiology
Background:
- The sarcoplasmic reticulum (SR) is crucial for regulating intracellular calcium levels in muscle cells.
- Understanding ion transport mechanisms, particularly ATP-dependent ion uptake, is vital for comprehending muscle function and dysfunction.
Purpose of the Study:
- To investigate the characteristics of strontium (Sr2+) uptake by fragmented sarcoplasmic reticulum.
- To compare strontium uptake with calcium (Ca2+) uptake and elucidate the role of the Sr2+-activated ATPase.
Main Methods:
- Utilized fragmented sarcoplasmic reticulum vesicles to study ATP-supported ion transport.
- Measured strontium and calcium uptake rates under varying conditions, including ATP presence, inorganic phosphate (Pi), ADP, and internal/external ion concentrations.
- Determined transport ratios and analyzed the effects of ion exchange and ATP depletion.
Main Results:
- ATP-dependent strontium uptake is monophasic and faster than fast calcium uptake.
- Strontium accumulation is proportional to external concentration and ATP hydrolysis, with a transport ratio of one in the absence of oxalate.
- Strontium uptake is not activated by Pi; however, strontium can activate slow calcium uptake while inhibiting fast calcium uptake, and ion-induced release is partial and transient.
Conclusions:
- The Sr2+-activated ATPase exhibits distinct transport kinetics for strontium compared to calcium.
- Energy conversion during strontium transport is efficient, unlike calcium transport under conditions of inefficient ATP phosphorylation.
- Strontium and calcium can partially and transiently release each other from the sarcoplasmic reticulum, indicating complex regulatory interactions.