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Interaction of lanthanides with muscle microsomes
Recent Advances in Studies on Cardiac Structure and Metabolism
|May 26, 1976
Summary
Gadolinium binding to muscle microsomes reveals two distinct sites, influenced by divalent cations and ionophores. ATP enhances binding, suggesting a separation of binding and hydrolysis in the transport site.
Area of Science:
- Biochemistry
- Pharmacology
- Cell Biology
Background:
- Gadolinium (Gd), a lanthanide, exhibits calcium-blocking properties.
- Muscle microsomes are crucial for cellular calcium regulation.
Purpose of the Study:
- To investigate the interaction of gadolinium with isolated muscle microsomes.
- To characterize gadolinium binding sites and their modulation.
Main Methods:
- Studied gadolinium binding to isolated muscle microsomes.
- Investigated the effects of divalent cations and antibiotic ionophores.
- Examined the influence of Adenosine Triphosphate (ATP) on binding.
Main Results:
- Identified two classes of gadolinium binding sites.
- Divalent cations (Ca, Zn, Cd) inhibited higher affinity binding.
- Ionophores (X537A, A23187) and ATP enhanced binding, with positive cooperativity observed.
- ATP-enhanced binding occurred without ATP hydrolysis at low concentrations.
Conclusions:
- Gadolinium binding to muscle microsomes is complex, involving multiple sites.
- The data suggest a functional dissociation between the binding and ATP-hydrolytic components of the transport site within the intact membrane.