Lipocalin-2 protein (LCN2)

Lipocalin-2 protein (LCN2) is a small, secreted glycoprotein of the lipocalin family characterized by an eight-stranded β-barrel structure forming a hydrophobic pocket. It is primarily known for its role in the innate immune response, where it limits bacterial growth by sequestering iron through binding bacterial and mammalian siderophores. LCN2 is widely expressed—including in neutrophils, liver, kidney, adipose tissue, and various epithelia—and acts as a transporter for small hydrophobic molecules, such as lipids and steroid hormones. The protein exists in monomeric, homodimeric, and heterodimeric forms (the latter most notably in complex with matrix metalloproteinase-9). It can function both as a growth and differentiation factor, modulate apoptosis, facilitate synaptic plasticity, and regulate the acute-phase response. LCN2 is a validated biomarker for acute kidney injury and is significantly upregulated during diverse cellular injuries, infections, inflammation, and cancer. It is under continuing clinical investigation for roles as both a biomarker and a therapeutic target. (If more drug-specific information is needed beyond the iron chelator deferiprone, none are currently established as directly targeting LCN2 in drug databases as of the latest literature.)

Other names

neutrophil gelatinase-associated lipocalinNGALoncogene 24p3siderocalin25 kDa α2-microglobulin-related proteinmigration-stimulating factor inhibitor (MSFI)p25SIP24uterocalin

iron chelation or modulation of iron homeostasis (by binding siderophores); modulation of downstream inflammation and oxidative stress