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Lactoferrin is a natural globular protein with a molecular atomic mass of 80 kD. It is found in milk and many mucosal secretions such as tears and it belongs to the transferring proteins (transferrin, (1) melanotransferrin, ovotransferrin, etc.) showing a high affinity for iron (ferric state).

Talactoferrin, an orally-administered recombinant human lactoferrin, can be produced by the fungus Aspergillus niger var. awamori (2) and has potential antineoplastic, antibacterial and immunomodulating activities. Recombinant human lactoferrin can be produced in various plant systems (e.g., tobacco, potato, rice etc.), animal systems (transgenic mice, cows, rabbits, etc.), viruses, fungi or cell cultures, (2) displaying somewhat different properties according to the expression system used.

When administered topically, talactoferrin alpha binds to keratinocytes and fibroblasts and enhances the production of cytokines and key repair immunomodulatory factors such as interleukins IL-8, IL-6, macrophage inflammatory protein-1 alpha and tumor necrosis factor alpha. (3)

Talactoferrin also appears to have antibacterial properties and it has been recently evaluated as oral therapy in severe sepsis. (3-5) Bovine lactoferrin has been reported to reduce the incidence of early onset sepsis when administered orally, as a supplement, either alone or with the probiotic Lactobacillus rhamnosus GG, in very-low birth weight premature infants (under 1500 g). (2,6)

The effects of orally-administered talactoferrin in cancer or in sepsis (7) are dependent on its transportation into the gut-associated lymphoid tissue (GALT), where it is responsible for recruiting and inducing the maturation of circulating immature dendritic cells bearing tumour antigens. Consequently, lymphoid effector cells induce systemic immune responses through natural killer (NK) cells and cytotoxic T lymphocytes (CTL) thus countering the local tumor-mediated immunosuppression. (8)

In conclusion, talactoferrin is an interesting antineoplastic agent which could also be useful in wound healing and, potentially in severe infections. Phase III studies are needed to clarify its potential role in severe sepsis.


(1.) Solomons H. Carbohydrate deficient transferrin and alcoholism. GERMS 2012;2:75-8.

(2.) Conesa C, Calvo M, Sanchez L. Recombinant human lactoferrin: a valuable protein for pharmaceutical products and functional foods. Biotechnol Adv 2010;28:831-8.

(3.) Engelmayer J, Blezinger P, Varadhachary A. Talactoferrin stimulates wound healing with modulation of inflammation. J Surg Res 2008;149:278-86.

(4.) Fernebro J. Fighting bacterial infections-future treatment options. Drug Resist Updat 2011;14:125-39.

(5.) Huttunen R, Aittoniemi J. New concepts in the pathogenesis, diagnosis and treatment of bacteremia and sepsis. J Infect 2011;63:407-19.

(6.) Manzoni P, Rinaldi M, Cattani S, et al. Bovine lactoferrin supplementation for prevention of late-onset sepsis in very low-birth-weight neonates: a randomized trial. JAMA 2009;302:1421-8.

(7.) Li S, Bao H, Han L, Liu L. Effects of propofol on early and late cytokines in lipopolysaccharide-induced septic shock in rats. J Biomed Res 2010;24:389-94.

(8.) National Cancer Institute at the National Institute of Health. NCI Drug Dictionary. Accessed on: August 11, 012. Available at: dictionary?cdrid=394101

Hilary Denis Solomons' *

Received: August 1, 2012; accepted: August 19, 2012

* Corresponding author: Hilary Denis Solomons, MB BCh, M Med Hematology, Pathology, University of the Witwatersrand, P.O. Box 64203, Highlands North, 2037, South Africa;
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Title Annotation:Correspondence
Author:Solomons, Hilary Denis
Article Type:Report
Geographic Code:6SOUT
Date:Sep 1, 2012
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