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Fatty acid binding protein inhibits glycolithocholate sulfation.
S S Singer1, D Dravis, K Henkels
1Chemistry Department, University of Dayton, OH 45469.
Biochemistry International
|July 1, 1992
Summary
Fatty acid binding protein (FABP) interferes with the sulfation of toxic monohydroxy bile salts, potentially increasing their liver toxicity. This effect was specific to lithocholate, not other bile salts tested.
Area of Science:
- Biochemistry
- Hepatology
- Toxicology
Background:
- Sulfation is a key detoxification pathway for harmful monohydroxy bile salts in the liver.
- Fatty acid binding protein (FABP) binds bile salts, with binding affinity decreasing as hydroxylation increases.
- FABP binding may impede bile salt sulfation and exacerbate toxicity.
Purpose of the Study:
- To investigate the role of FABP in the sulfation of hepatotoxic monohydroxy bile salts.
- To determine if FABP binding affects the activity of bile salt sulfotransferases (BSTs).
Main Methods:
- Enzyme kinetics assays were performed using bile salt sulfotransferases (BST 1 and BST 2).
- The effect of FABP on the sulfation of specific monohydroxy bile salts (glycolithocholate, glycodeoxycholate, glycochenodeoxycholate) was measured.
- Sulfation reduction was quantified using glycolithocholate as a substrate for BST 1.
Main Results:
- FABP significantly inhibited the sulfation of glycolithocholate by BST 1 by up to 42.8%.
- FABP did not affect the sulfation of glycodeoxycholate or glycochenodeoxycholate by BST 1.
- FABP's inhibitory effect was observed on BST 1, a primary bile salt sulfotransferase.
Conclusions:
- FABP specifically interferes with the sulfation of lithocholate and its metabolites.
- This interaction suggests FABP may play a crucial role in modulating the hepatotoxicity of lithocholate.