Cellular fatty acid-binding proteins: Their function and physiological significance

https://www.sfu.ca/biology/faculty/haunerland/Haunerland+Spener2004a.pdf

Fatty acid-binding proteins--insights from genetic manipulations.

Structural and functional features of different types of cytoplasmic fatty acid-binding proteins

Publisher Summary This chapter provides a comprehensive overview of the current state of knowledge of the research with particular emphasis on evolving concepts of fatty acid binding proteins (FABP) structure, regulation, and function. Long-chain fatty acids provide the main energy source of most mammalian tissues and also comprise essential components of the structural lipids of cell membranes. The purification of the specific proteins responsible for the low-molecular-weight fatty-acid binding protein activity in different tissues leads to the characterization of three structurally distinct FABP of similar size, each the product of a separate gene. The three cytosolic FABP are generally named according to their tissues of greatest abundance, and comprise liver FABP, intestinal FABP, and heart muscle FABP. A role for the 40-kDa LPM-FABP as a specific cell membrane carrier in the transport of long chain fatty acids into the cells of the liver and possibly other tissues as well is available. The 14- to 15-kDa cytosolic FABPs may function as intracellular acceptors and carriers of long-chain fatty acids and their coenzyme A (CoA) esters, maintaining the ability of the tissues, particularly liver, intestine, heart, and skeletal muscle to utilize fatty acids over wide and acutely varying ranges of flux.

The cellular fatty acid binding proteins: aspects of structure, regulation, and function.

Expression of rat intestinal fatty acid-binding protein in Escherichia coli. Purification and comparison of ligand binding characteristics with that of Escherichia coli-derived rat liver fatty acid-binding protein.

H J Kempen

Papers

Diurnal variation of cytosolic fatty acid-binding protein content and of palmitate oxidation in rat liver and heart