NDLI: Membrane Binding Proteins are the Major Determinants for the Hepatocellular Transmembrane Flux of Long-Chain Fatty Acids Bound to Albumin

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Membrane Binding Proteins are the Major Determinants for the Hepatocellular Transmembrane Flux of Long-Chain Fatty Acids Bound to Albumin

Content Provider	Springer Nature Link
Author	Rajaraman, G. Roberts, M. S. Hung, D. Wang, G. Q. Burczynski, F. J.
Copyright Year	2005
Abstract	The hepatic transmembrane flux of long-chain fatty acids (LCFA) occurs through passive and fatty acid transport protein facilitated processes from blood. The extent that these transport processes can be related to the unbound and protein-bound fractions of LCFA in blood is not clear.We used hepatocyte suspensions, hepatoma monolayers, and perfused rat livers to quantitate the transport of purified [$^{3}$H]palmitate ([$^{3}$H]PA) and 12-(N-methyl)-N-[(7-nitrobenz-2oxa-1,3-diazol-4yl-)amino]octadecanoicacid (12-NBDS) from solutions with a constant unbound LCFA concentration with varying bovine serum albumin (BSA) concentrations and in the presence and absence of antisera raised against cytosolic liver fatty acid binding protein (L-FABP).In the absence of L-FABP antisera, using an unbound ligand concentration that was adjusted to remain constant at each BSA concentration, hepatocyte [$^{3}$H]PA and 12-NBDS uptake rates increased linearly with an increase in BSA concentration (p < 0.0001). In the presence of L-FABP antisera, [$^{3}$H]PA uptake showed a greater reduction in the presence of 100 μM BSA than 5 μM BSA. The calculated permeability surface area product (PS) confirmed that both unbound and bound fractions of LCFA contributed to the overall flux, but only the PS for the protein-bound fraction was reduced in the presence of L-FABP antisera. In situ rat liver perfusion studies showed that the only rate process for the disposition of [$^{3}$H]PA in the liver inhibited by L-FABP antisera was that for influx, as defined by PS, and that it reduced PS in the perfused liver by 42%.These results suggest that, at physiological albumin concentrations, most of the LCFA uptake is mediated from that bound to albumin by a hepatocyte basolateral membrane transport protein, and uptake of unbound LCFA occurring by passive diffusion contributes a minor component.
Starting Page	1793
Ending Page	1804
Page Count	12
File Format	PDF
ISSN	07248741
Journal	Pharmaceutical Research
Volume Number	22
Issue Number	11
e-ISSN	1573904X
Language	English
Publisher	Springer-Verlag
Publisher Date	2005-08-16
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	albumin FABP hepatocyte liver long-chain fatty acid palmitate stearate uptake Pharmacology/Toxicology Pharmacy Biochemistry Medical Law Biomedical Engineering
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Pharmacology Molecular Medicine Pharmacology (medical) Biotechnology Pharmaceutical Science

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