CONICET | Buscador de Institutos y Recursos Humanos

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.