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Review
. 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

Isui Abril García-Montoya  1 , Tania Siqueiros Cendón, Sigifredo Arévalo-Gallegos, Quintín Rascón-Cruz
Affiliations
Review

Lactoferrin a multiple bioactive protein: an overview

Isui Abril García-Montoya et al. Biochim Biophys Acta. 2012 Mar.

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.

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Figures

Fig. 1
Fig. 1
Predicted structure of lactoferrin. a) From EU812318 (bLF) sequence using PDB ID: 1BIY (buffalo) as a template, showing two-lobe, four-domain polypeptide. b) Canonical iron-binding pocket site of lactoferrin. Fe + 3 (cream) CO3 (gray and red). Modeled using Protein Model Portal , and viewed using Chimera software (http://www.cgl.ucsf.edu/chimera/).
Fig. 2
Fig. 2
Predicted structure of antiviral-active peptides using PDB ID: 1FCK as template. a) From N-lobe 1–280 aa. b) From C-lobe 345–689 aa. Modeled using DeepView software , and viewed using Chimera software (http://www.cgl.ucsf.edu/chimera/).
Fig. 3
Fig. 3
Location of field and aqueous solvated structure comparison of the human and bovine lactoferricin. a) Domain of in situ hLfcin (residues 17–41; PDB ID: 1BLF) and, aqueous solvated b) hLfcin and c) bLfcin. Viewed using Chimera software (http://www.cgl.ucsf.edu/chimera/).
See this image and copyright information in PMC

References

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