Lactotransferrin (LTF) (LTF)

Human lactoferrin (LTF), also known as lactotransferrin, is a multifunctional 80 kDa glycoprotein belonging to the transferrin family, primarily found in mucosal secretions and neutrophil granules (UniProt P02788). It plays a pivotal role in the innate immune system by sequestering free iron, thereby inhibiting the growth of iron-dependent pathogens, and by exerting direct bactericidal effects through its N-terminal peptide derivative, lactoferricin (PubMed: 21847071). Lactoferricin is released via proteolytic cleavage by pepsin and acts as a potent antimicrobial peptide that disrupts microbial membranes (PubMed: 16218809). Beyond its antimicrobial properties, lactoferrin modulates the inflammatory response by binding to bacterial lipopolysaccharides and interacting with various cell surface receptors, including LRP1 and TLR4, to regulate cytokine production (PubMed: 28933413). In clinical development, recombinant human lactoferrin (e.g., talactoferrin alfa) has been investigated as a therapeutic agent for sepsis and non-small cell lung cancer, while fecal lactoferrin is widely utilized as a diagnostic biomarker for inflammatory bowel disease (PubMed: 19126301).

Other names

LactoferrinLFGIG12LactoferricinLfcinHTalactoferrin

Lactoferrin acts primarily through iron sequestration (bacteriostatic effect) and direct interaction with microbial membranes via its lactoferricin domain (bactericidal effect). It also modulates the immune system by binding to bacterial lipopolysaccharides (LPS) and competing with receptors like TLR4, thereby reducing pro-inflammatory cytokine production (PubMed: 21847071, PubMed: 28933413).