Ann V. Hertzel

TL;DR: Intracellular fatty acid-binding proteins associate with fatty acids and other hydrophobic biomolecules in an internal cavity, providing for solubilization and metabolic trafficking, and their in vivo function is analyzed by molecular and genetic techniques.

TL;DR: Intracellular lipid-binding proteins are a family of low-molecular-weight single-chain polypeptides that form 1:1 complexes with fatty acids, retinoids, or other hydrophobic ligands that are products of a large multigene family of unlinked loci distributed throughout the genome.

TL;DR: It is demonstrated that mal1 modulates adipose tissue function and contributes to systemic glucose metabolism and constitutes a potential therapeutic target in insulin resistance.

TL;DR: The identification of the epithelial fatty acid-binding protein (E-FABP) as a molecular target for 4-HNE modification both in vitro and in vivo and the hypothesis that E-fABP functions as an antioxidant protein by scavenging reactive lipids through covalent modification of Cys-120 are indicated.

TL;DR: Evidence is presented that endogenous ACBP, ALBP, and KLBP not only localize to the cytoplasm but also exhibit a prominent nuclear localization in 3T3-L1 adipocytes, suggesting that lipid-binding proteins, when expressed at high levels, may function as negative regulators of PPAR activation by certain ligands.