Plasma membrane fatty acid-binding protein (FABPpm) (FABPpm)

Plasma membrane fatty acid-binding protein (FABPpm) is a 43-kDa peripheral membrane protein that facilitates the transport of long-chain fatty acids (LCFAs) across the plasma membrane of metabolically active cells, including myocytes and adipocytes (Glatz et al., 2010, PubMed). It is biochemically identical to the mitochondrial isoform of aspartate aminotransferase (mAST or GOT2), yet a significant fraction is localized to the cell surface to mediate lipid uptake (Stremmel et al., 1985, PubMed; Berk et al., 1990, PubMed). In the context of metabolic disease, FABPpm expression and its translocation to the plasma membrane are significantly increased in individuals with obesity and type 2 diabetes, contributing to intramuscular lipid accumulation and insulin resistance (Bonen et al., 2004, PubMed). While it is not currently the primary target of any FDA-approved drugs, it is a major focus of research into metabolic regulation, with experimental inhibitors like phloretin and sulfo-N-succinimidyl oleate (SSO) demonstrating the ability to reduce fatty acid uptake (Clarke et al., 2004, PubMed). Targeting FABPpm offers a potential therapeutic strategy for managing lipid oversupply in metabolic syndrome, although the protein's dual role in mitochondrial amino acid metabolism presents a significant challenge for systemic drug design (Glatz et al., 2010, PubMed).

Other names

Mitochondrial aspartate aminotransferasemASTGlutamic-oxaloacetic transaminase 2GOT2mAspATFatty acid-binding protein, plasma membraneFABP-pm

Inhibition of long-chain fatty acid uptake and translocation across the plasma membrane.