FABP12 exhibits restricted tissue expression:
Tissue/Cell Type | Expression Level | Source |
---|---|---|
Retinoblastoma cells | High | |
Testis (rodent) | Moderate | |
Prostate cancer cells | Elevated in metastatic cases | |
Male germline stem cells | Detected |
The Human Protein Atlas notes limited expression in standard human tissues, suggesting context-specific roles .
Facilitates fatty acid trafficking to organelles (e.g., nucleus, mitochondria) .
Activates peroxisome proliferator-activated receptor gamma (PPARγ), a nuclear receptor linked to lipid metabolism and cancer progression .
Prostate Cancer: Elevated FABP12 levels correlate with aggressive metastasis by inducing epithelial-to-mesenchymal transition (EMT) and enhancing fatty acid-dependent energy production .
Neurological Disorders: Predicted involvement in brain lipid metabolism, though direct evidence is limited .
Prostate Cancer: Serum FABP12 levels may serve as a prognostic marker for metastasis .
Metabolic Disorders: Linked to lipid dysregulation, though further validation is needed .
Inhibiting FABP12-PPARγ signaling could suppress metastasis in prostate cancer .
Small-molecule modulators of FABP12 are under exploration for metabolic and inflammatory diseases .
Fatty Acid Binding Protein-12 (FABP12) is a member of the fatty acid-binding protein (FABP) family, which plays a crucial role in the intracellular transport of fatty acids and other lipophilic substances such as eicosanoids and retinoids . These proteins are essential for the transfer of fatty acids between extra- and intracellular membranes, facilitating various metabolic processes.
FABP12 is one of the more recently identified members of the FABP family. The gene encoding FABP12 has been identified, but detailed studies on the protein itself are still limited . The FABP12 gene is a protein-coding gene associated with lipid binding and transporter activity . It is predicted to be located in the cytosol and is involved in pathways related to triglyceride metabolism and general metabolism .
FABPs are small, structurally conserved cytosolic proteins characterized by a water-filled interior-binding pocket surrounded by ten anti-parallel beta sheets, forming a beta barrel. Two alpha-helices cap the pocket at the superior surface, which is thought to regulate binding . FABP12, like other FABPs, is believed to play a role in lipid transport within cells .
FABP12 is expressed in several retinoblastoma cell lines, indicating its potential role in lipid transport within these cells . The protein’s exact functions and mechanisms are still under investigation, but it is believed to be involved in the intracellular transport of fatty acids and other lipophilic molecules, contributing to various metabolic processes .
The FABP family demonstrates strong evolutionary conservation and is present in a wide range of species, including Drosophila melanogaster, Caenorhabditis elegans, mice, and humans . This conservation suggests that FABPs, including FABP12, play fundamental roles in cellular metabolism and lipid transport.