Lactotransferrin (Lactoferrin) (LTF)

Lactotransferrin (LTF), commonly known as lactoferrin, is a multifunctional 80 kDa iron-binding glycoprotein and a prominent member of the transferrin family [1, 4]. It is synthesized by mucosal epithelial cells and stored in the secondary granules of neutrophils, from which it is released into the extracellular environment during infection or inflammation [2, 5]. Lactoferrin serves as a key component of the innate immune system, providing broad-spectrum antimicrobial activity by sequestering iron required for microbial growth and directly disrupting the cell membranes of bacteria, viruses, and fungi [4, 5]. Additionally, it functions as a potent immunomodulator by interacting with specific receptors on immune cells, such as LRP1 and Intelectin-1, to regulate cytokine production and promote the maturation of T and B cells [1, 5]. In therapeutic development, recombinant human lactoferrin (e.g., talactoferrin alfa) has been explored for its potential in treating sepsis, cancer, and chronic wounds, while its presence in stool is used as a diagnostic biomarker for intestinal inflammation [3, 4].

Other names

LactoferrinLFGIG12TalactoferrinNeutrophil lactoferrinLactoferrin receptor ligand

Sequestration of ferric iron (Fe3+) to inhibit microbial growth; direct binding to lipopolysaccharides (LPS) and microbial membranes to cause lysis; modulation of the NF-kappaB pathway to reduce pro-inflammatory cytokine expression; and binding to cell surface receptors (e.g., LRP1, Intelectin-1) to stimulate immune cell differentiation and activity [1, 4, 5].