Abstract

Lactoferrin is an iron-binding cationic glycoprotein that is constitutively synthesized by exocrine glands and by neutrophils. Its biosynthesis can be markedly A picture taken of a statue in Rome showing how Romulus and Remus are being nursed back to health by la Lupa Capitolina. Milk is an excellent source of lactoferrin, a protein with many health benefits increased during infection and inflammation. This multifunctional protein also acts as a major player in host defense in bodily fluids while it simultaneously protects the human mucosa. Several functions of lactoferrin are dependent on its ability to avidly bind two ferric ions in two characteristic binding sites while other biological activities do not require this property and they are mediated by other parts of the protein. In particular, the highly basic N-terminal regions of human and bovine lactoferrin seem to play an important role in the antimicrobial and immuno-regulatory properties of the protein, which can be emulated to some extent by using synthetic peptide derivatives that resemble this region. From the 1960s onward, when the protein was first purified from milk, the number of scientific publications concerning its biochemical properties, the various biological functions and the potential therapeutic applications of lactoferrin and its bioactive peptides has significantly increased. This research area is regularly being reviewed and the reader may wish to consult some of these contributions to gain an entry into the field (Valenti et al. 2004; Lonnerdal 2009; Baker and Baker 2012; Vogel 2012). Currently a Pubmed search in the NCBI Medline database identifies almost 7,000 publications for this topic and this number increases by about 300 publications each year. In particular the potential for therapeutic or health-promoting applications of lactoferrin has led to a sustained research effort in this area. P. Valenti (&) Department of Public Health and Infectious Diseases, Sapienza University of Rome, Rome, Italy e-mail: piera.valenti@uniroma1.it

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.