Liver fatty acid-binding protein binds monoacylglycerol in vitro and in mouse liver cytosol

Liver fatty acid-binding protein (LFABP; FABP1) is expressed both in liver and intestinal mucosa. Mice null for LFABP were recently shown to have altered metabolism of not only fatty acids but also monoacylglycerol, the two major products of dietary triacylglycerol hydrolysis (Lagakos, W. S., Gajda,...

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Autores principales: Lagakos, W. S., Guan, X., Ho, S.-Y., Rodriguez Sawicki, Luciana, Córsico, Betina, Kodukula, S., Murota, K., Stark, R. E., Storch, J.
Formato: Articulo
Lenguaje:Inglés
Publicado: 2013
Materias:
Ciencias Médicas
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/85699
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-85699
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Médicas
spellingShingle Ciencias Médicas
Lagakos, W. S.
Guan, X.
Ho, S.-Y.
Rodriguez Sawicki, Luciana
Córsico, Betina
Kodukula, S.
Murota, K.
Stark, R. E.
Storch, J.
Liver fatty acid-binding protein binds monoacylglycerol in vitro and in mouse liver cytosol
topic_facet Ciencias Médicas
description Liver fatty acid-binding protein (LFABP; FABP1) is expressed both in liver and intestinal mucosa. Mice null for LFABP were recently shown to have altered metabolism of not only fatty acids but also monoacylglycerol, the two major products of dietary triacylglycerol hydrolysis (Lagakos, W. S., Gajda, A. M., Agellon, L., Binas, B., Choi, V., Mandap, B., Russnak, T., Zhou, Y. X., and Storch, J. (2011) Am. J. Physiol. Gastrointest. Liver Physiol. 300, G803-G814). Nevertheless, the binding and transport of monoacylglycerol (MG) by LFABP are uncertain, with conflicting reports in the literature as to whether this single chain amphiphile is in fact bound by LFABP. In the present studies, gel filtration chromatography of liver cytosol from LFABP-/- mice shows the absence of the low molecular weight peak of radiolabeled monoolein present in the fractions that contain LFABP in cytosol from wild type mice, indicating that LFABP binds sn-2 MG in vivo. Furthermore, solution-state NMRspectroscopy demonstrates two molecules of sn-2 monoolein bound in the LFABP binding pocket in positions similar to those found for oleate binding. Equilibrium binding affinities are ~2-fold lower for MG compared with fatty acid. Finally, kinetic studies examining the transfer of a fluorescent MG analog show that the rate of transfer of MG is 7-fold faster from LFABP to phospholipid membranes than from membranes to membranes and occurs by an aqueous diffusion mechanism. These results provide strong support for monoacylglycerol as a physiological ligand for LFABP and further suggest that LFABP functions in the efficient intracellular transport of MG.
format Articulo
Articulo
author Lagakos, W. S.
Guan, X.
Ho, S.-Y.
Rodriguez Sawicki, Luciana
Córsico, Betina
Kodukula, S.
Murota, K.
Stark, R. E.
Storch, J.
author_facet Lagakos, W. S.
Guan, X.
Ho, S.-Y.
Rodriguez Sawicki, Luciana
Córsico, Betina
Kodukula, S.
Murota, K.
Stark, R. E.
Storch, J.
author_sort Lagakos, W. S.
title Liver fatty acid-binding protein binds monoacylglycerol in vitro and in mouse liver cytosol
title_short Liver fatty acid-binding protein binds monoacylglycerol in vitro and in mouse liver cytosol
title_full Liver fatty acid-binding protein binds monoacylglycerol in vitro and in mouse liver cytosol
title_fullStr Liver fatty acid-binding protein binds monoacylglycerol in vitro and in mouse liver cytosol
title_full_unstemmed Liver fatty acid-binding protein binds monoacylglycerol in vitro and in mouse liver cytosol
title_sort liver fatty acid-binding protein binds monoacylglycerol in vitro and in mouse liver cytosol
publishDate 2013
url http://sedici.unlp.edu.ar/handle/10915/85699
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