Fatty acid-binding protein 9 (FABP9)

Fatty acid-binding protein 9 (FABP9) is a small, cytosolic lipid-binding protein of about 132 amino acids and a member of the fatty acid-binding protein (FABP) superfamily, which features tissue-specific isoforms involved in the intracellular transport and metabolism of long-chain fatty acids[2][3]. FABP9, also known as testis lipid-binding protein, is predominantly expressed in the testis, as well as in tissues like the salivary and mammary glands[2][3]. Its principal function is to bind and facilitate the intracellular movement of long-chain fatty acids, thereby regulating their bioavailability for metabolic and signaling functions[2][3]. FABP9’s typical structure is a flattened beta-barrel, similar to other FABPs, designed for high-affinity interaction with hydrophobic ligands such as fatty acids[2]. Recent research has identified FABP9 upregulation in malignant prostate cell lines and human prostate cancer tissues, suggesting a role as a potential biomarker for prostate cancer progression. FABP9 knockdown appears to decrease cell invasion in highly malignant prostate cancer cell models, connecting its expression to cancer aggressiveness[3]. Like other FABPs, circulating FABP9 may have potential as a tissue-specific biomarker, but its value in other diseases or as a pharmacological target remains largely unexplored[3]. No direct interacting drugs or mechanisms of action have yet been described in the literature.

Other names

TLBPT-FABPPERFPERF15Testis lipid-binding proteinTestis-type fatty acid-binding proteintestis fatty acid binding proteintestis lipid binding protein