Proteins and Disease | Structural Insight and Functional Diversity of Mammalian Fatty Acid Binding Proteins in Health and Disease

McDermott, Lindsay C.; Storch, Judith

doi:10.1016/b978-0-12-819460-7.00173-0

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“…( a ) Superimposition of crystal structures of unliganded FABP1–9 generated in PyMOL (FABP1, 2F73; FABP2, 1IFC; FABP3, 6AQ1; FABP4, 3RZY; FABP5, 4LKP; FABP6, 5L8I; FABP7, 1FDQ; FABP8, 3NR3; and FABP9, 4A60). Panel adapted from Reference 119 with permission from Elsevier. ( b ) Table listing the mammalian FABPs, whose numbers reflect the order of their initial discovery.…”

Section: Figurementioning

confidence: 99%

The Multifunctional Family of Mammalian Fatty Acid–Binding Proteins

Storch

Córsico

2023

Annu. Rev. Nutr.

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Fatty acid–binding proteins (FABPs) are small lipid-binding proteins abundantly expressed in tissues that are highly active in fatty acid (FA) metabolism. Ten mammalian FABPs have been identified, with tissue-specific expression patterns and highly conserved tertiary structures. FABPs were initially studied as intracellular FA transport proteins. Further investigation has demonstrated their participation in lipid metabolism, both directly and via regulation of gene expression, and in signaling within their cells of expression. There is also evidence that they may be secreted and have functional impact via the circulation. It has also been shown that the FABP ligand binding repertoire extends beyond long-chain FAs and that their functional properties also involve participation in systemic metabolism. This article reviews the present understanding of FABP functions and their apparent roles in disease, particularly metabolic and inflammation-related disorders and cancers. Expected final online publication date for the Annual Review of Nutrition, Volume 43 is August 2023. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

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Section: Figurementioning

confidence: 99%