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Gentamicin binding to brush border and basolateral membranes isolated from rat kidney cortex
Journal of Pharmacobio-Dynamics
|November 1, 1985
Summary
Gentamicin specifically binds to rat kidney membranes, interacting with anionic sites. This binding is influenced by polycations and phospholipids, suggesting charge-based interactions regulate its renal accumulation.
Area of Science:
- Nephrology
- Pharmacology
- Biochemistry
Background:
- Gentamicin is an aminoglycoside antibiotic.
- Renal cortex is the primary site for gentamicin accumulation.
- Understanding gentamicin-kidney interaction is crucial for managing nephrotoxicity.
Purpose of the Study:
- To investigate the in vitro interaction of gentamicin with rat renal cortex membranes.
- To identify the specific membrane components and interactions involved in gentamicin binding.
Main Methods:
- In vitro binding assay using brush border and basolateral membranes from rat renal cortex.
- Investigated effects of polycations, phospholipase A2, proteolytic enzymes, sulfhydryl reagents, acidic phospholipids, and calcium on gentamicin binding.
- Determined membrane surface charge using metachromasy.
Main Results:
- Gentamicin specifically bound to plasma membrane fractions.
- Binding was inhibited by polycations and influenced by phospholipids and calcium.
- Membrane surface charge alterations correlated with gentamicin binding, indicating charge interactions.
- Other aminoglycosides competed for binding based on their positive charge.
Conclusions:
- Gentamicin exhibits charge-based interactions with anionic sites on renal brush border and basolateral membranes.
- The binding characteristics are similar for both membrane types.
- Renal accumulation of gentamicin may be regulated by transport across these plasma membranes.