INIBIOLP   05426
INSTITUTO DE INVESTIGACIONES BIOQUIMICAS DE LA PLATA "PROF. DR. RODOLFO R. BRENNER"
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Unraveling intestinal fatty acid binding proteins functions: analysis of FABP-membrane and FABP-protein interactions.
Autor/es:
FALOMIR LOCKHART LJ; FRANCHINI GR; GUERBI MX; STORCH J; CÓRSICO B
Lugar:
Brasil
Reunión:
Congreso; VII Iberoamerican Congress of Biophysics; 2009
Institución organizadora:
SAB
Resumen:
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Unraveling intestinal fatty acid binding proteins functions: analysis of FABP-membrane and FABP-protein interactions.
Lisandro
J. Falomir Lockhart#+, María Ximena Guerbi#, Gisela R.
Franchinni#, Judith Storch¶ and Betina Córsico#+.
# INIBIOLP, University of La Plata,
Calle 60 y120, 1900, La Plata, Argentina.
+ Consejo Nacional de Investigaciones Científicas y Técnicas, Avda. Rivadavia 1917, C1033AAJ, Cdad. de Buenos Aires, Argentina.
¶ Department of Nutritional Sciences, Rutgers the State University of New
Jersey, 96 Lipman Dr, New Brunswick, NJ, 08901-8525, U.S.A.
e-mail: lysfalomir@yahoo.com.ar,
bcorsico@atlas.med.unlp.edu.ar
Introduction: Intestinal enterocytes
express large concentrations of two homologous fatty acid binding proteins
(FABPs): intestinal FABP (IFABP) (15.1 kDa) and liver FABP (LFABP) (14.2 kDa).
It has long been hypothesized that FABPs participate in the intracellular
transport and processing of the large quantities of fatty acids (FA) absorbed
by the intestine, but their specific function are still poorly understood. In
particular, it is currently not known why a single cell type contains two
distinct types of FABP.
Objective: We expect to identify the interaction
partners of intestinal FABPs in order to describe the molecular crosstalk
relevant for its biological functions.
Methods: In this work, we took advantage of different
structural variants of intestinal FABPs and a battery of biochemical and
biophysical methodologies to analyze its interaction with membranes and other
proteins. Tb/DPA complex leakage, binding
to sucrose loaded vesicles, Cyt c competition assay and radiolabeled
photoactivable phospholipid crosslinking were employed to study different
factors (vesicle curvature, ligand nature, lipid composition, etc) that
modulate the interaction of FABPs with artificial model membranes. On the other
hand, a fluorescence based assay was employed to analyze colisional transfer of
fatty acid analogs between IFABP and LFABP in a stopped-flow module.
Results: Lipid composition and ligand binding
show strong changes in membrane interaction properties of IFABP and LFABP, as
evidenced by different techniques. Collisional transfer of fluorescent fatty
acids suggests functional interaction between these intestinal FABPs.
Conclusions: Intestinal FABPs could interact
differentially with each other and with subcellular membranous fractions
accordingly with ligand binding. The results in vitro presented here may reflect in vivo functions of intestinal FABPs. Increasing evidence supports
the idea that FABPs participate and modulate several cell functions and further
studies will be needed to unravel its physiological role.
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