INIBIOLP   05426
INSTITUTO DE INVESTIGACIONES BIOQUIMICAS DE LA PLATA "PROF. DR. RODOLFO R. BRENNER"
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Functional analysis of soluble lipid binding proteins.
Autor/es:
CÓRSICO B
Lugar:
Tucumán
Reunión:
Congreso; XLV Congreso de SAIB; 2009
Institución organizadora:
SAIB
Resumen:
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Functional analysis of soluble lipid binding proteins.
Betina Córsico
INIBIOLP (CONICET-UNLP), Calle 60
y120, 1900, La Plata. Argentina.
The evolution of different families of intracellular soluble lipid
binding proteins (SLBPs) may be connected to the wide range of functions of
lipids and their very low solubility in the cellular media. Among these SLBPs,
the mammalian fatty acid binding proteins (FABPs) are ubiquitously expressed,
with distinct expression patterns for the individual FABPs. The large number of
FABP types is suggestive of distinct functions in specific tissues. Individual
FABPs possess both unique and overlapping functions, some of which are based on
specific elements in the protein structure. Structure-function studies indicate
that subtle three-dimensional changes that occur upon ligand binding may
promote specific protein-protein or protein-membrane interactions that
ultimately determine the function of each FABP. The conformational changes are
focused in the FABP helical/portal domain, a region that was identified by in
vitro studies to be vital for the fatty acid transport properties of the FABPs.
Thus, the FABPs modulate intracellular lipid homeostasis by regulating FA
transport in the cell. Modification of their expression in cultivo shows their
participation in lipid uptake and intracellular distribution, in so doing, they
also impact systemic energy homeostasis.