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Review
. 2006 Mar-Apr;142(3-4):262-274.
doi: 10.1016/j.cbpc.2005.11.006. Epub 2006 Jan 19.

Invertebrate intracellular fatty acid binding proteins

Affiliations
Review

Invertebrate intracellular fatty acid binding proteins

Adriana Esteves et al. Comp Biochem Physiol C Toxicol Pharmacol. 2006 Mar-Apr.

Abstract

Fatty acid binding proteins are multigenic cytosolic proteins largely distributed along the zoological scale. Their overall identity at primary and tertiary structure is conserved. They are involved in the uptake and transport of hydrophobic ligands to different cellular fates. The precise functions of each FABP type remain imperfectly understood, since sub-specialization of functions is suggested. Evolutionary studies have distinguished major subfamilies that could have been derived from a common ancestor close to vertebrate/invertebrate split. Since the isolation of the first invertebrate FABP from Schistocerca gregaria in 1990, the number of FABPs isolated from invertebrates has been increasing. Differences at the sequence level are appreciable and relationships with vertebrate FABPs are not clear, and lesser among invertebrate proteins, introducing some uncertainty to infer functional relatedness and phylogenetic relationships. The objective of this review is to summarize the information available on invertebrate FABPs to elucidate their mutual relationships, the relationship with their vertebrate counterparts and putative functions. Structure, gene structure, putative functions, expression studies and phylogenetic relationships with vertebrate counterparts are analyzed. Previous suggestions of the ancestral position concerning the heart-type of FABPs are reinforced by evidence from invertebrate models.

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