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Biochim Biophys Acta. 2012 Mar;1820(3):226-36. doi: 10.1016/j.bbagen.2011.06.018. Epub 2011 Jun 25.

Lactoferrin a multiple bioactive protein: an overview.

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  • 1Laboratorio de Biotecnología, Facultad de Ciencias Químicas, Universidad Autónoma de Chihuahua, Circuito 1, Nuevo Campus Universitario, CP 31125, Chihuahua, Mexico.

Abstract

BACKGROUND:

Lactoferrin (Lf) is an 80kDa iron-binding glycoprotein of the transferrin family. It is abundant in milk and in most biological fluids and is a cell-secreted molecule that bridges innate and adaptive immune function in mammals. Its protective effects range from anticancer, anti-inflammatory and immune modulator activities to antimicrobial activities against a large number of microorganisms. This wide range of activities is made possible by mechanisms of action involving not only the capacity of Lf to bind iron but also interactions of Lf with molecular and cellular components of both hosts and pathogens.

SCOPE OF REVIEW:

This review summarizes the activities of Lf, its regulation and potential applications.

MAJOR CONCLUSIONS:

The extensive uses of Lf in the treatment of various infectious diseases in animals and humans has been the driving force in Lf research however, a lot of work is required to obtain a better understanding of its activity.

GENERAL SIGNIFICANCE:

The large potential applications of Lf have led scientists to develop this nutraceutical protein for use in feed, food and pharmaceutical applications. This article is part of a Special Issue entitled Molecular Mechanisms of Iron Transport and Disorders.

Copyright © 2011 Elsevier B.V. All rights reserved.

PMID:
21726601
[PubMed - indexed for MEDLINE]
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