Abstract Title:

Lactoferrin functions: current status and perspectives.

Abstract Source:

J Clin Gastroenterol. 2004 Jul ;38(6 Suppl):S127-9. PMID: 15220678

Abstract Author(s):

Piera Valenti, Francesca Berlutti, Maria Pia Conte, Catia Longhi, Lucilla Seganti

Article Affiliation:

Piera Valenti


Lactoferrin, an iron-binding glycoprotein synthesized by neutrophils and exocrine glands, plays an important role in human innate defense mechanisms against bacteria, fungi, and viruses. First, a bacteriostatic activity of lactoferrin, depending on iron withholding to bacteria, and successively a bactericidal iron-independent effect, related to its binding on bacterial surfaces, was recognized. Many other functions have been ascribed to this cationic protein, including the inhibiting action toward bacterial adhesion and invasion of target host cells. Recent research also reported the lactoferrin influence on bacterial aggregation and biofilm development of Pseudomonas aeruginosa and Streptococcus mutans. The different lactoferrin functions can be justified by different physicochemical properties of the molecule, which include the iron-binding capability, the binding to anionic cell surfaces and molecules, and serine protease activity.

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