Lactoferrin is an iron-binding glycoprotein of the transferrin family, first isolated from milk but also found in most exocrine secretions as well as in the secondary granules of neutrophils. The many reports on its antimicrobial and antiinflammatory activity in vitro identify lactoferrin as important in host defense against infection and excessive inflammation. Most if not all lactoferrin actions are mediated through iron sequestration and/or interaction with a large variety of ligands including microbial cell wall components and cellular receptors, through its highly positively charged N-terminus. Lactoferrin exerts its effects on glandular epithelia, secretions, mucosal surfaces as well as in the interstitium and vascular compartments where it has been postulated to participate in iron metabolism, disease defense, and modulation of inflammatory and immune responses. A need to understand the diverse biological actions of lactoferrin and the prospect of a wide variety of potential applications in human health care have stimulated studies of the relation between lactoferrin structure and function, the regulation of lactoferrin secretion and development of large scale production of recombinant human lactoferrin (hLf). This review provides a synthesis of our current understanding of lactoferrin. Space limitations have led us to refer to review articles whenever possible; the reader is advised to use these articles for access to the primary experimental literature.

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