Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2021 Jul 17;10(7):1810.
doi: 10.3390/cells10071810.

A Review on Lactoferrin and Central Nervous System Diseases

Affiliations
Review

A Review on Lactoferrin and Central Nervous System Diseases

Yu-Qi Li et al. Cells. .

Abstract

Central nervous system (CNS) diseases are currently one of the major health issues around the world. Most CNS disorders are characterized by high oxidative stress levels and intense inflammatory responses in affected tissues. Lactoferrin (Lf), a multifunctional iron-binding glycoprotein, plays a significant role in anti-inflammatory, antibacterial, antiviral, reactive oxygen species (ROS) modulator, antitumor immunity, and anti-apoptotic processes. Previous studies have shown that Lf is abnormally expressed in a variety of neurological diseases, especially neurodegenerative diseases. Recently, the promotion of neurodevelopment and neuroprotection by Lf has attracted widespread attention, and Lf could be exploited both as an active therapeutic agent and drug nanocarrier. However, our understanding of the roles of Lf proteins in the initiation or progression of CNS diseases is limited, especially the roles of Lf in regulating neurogenesis. This review highlights recent advances in the understanding of the major pharmacological effects of Lf in CNS diseases, including neurodegenerative diseases, cerebrovascular disease, developmental delays in children, and brain tumors.

Keywords: central nervous system diseases; iron homeostasis; lactoferrin; neurodevelopment; neuroprotection.

PubMed Disclaimer

Conflict of interest statement

The authors declare that no competing interests exist.

References

    1. Elzoghby A.O., Abdelmoneem M.A., Hassanin I.A., Abd Elwakil M.M., Elnaggar M.A., Mokhtar S., Fang J.Y., Elkhodairy K.A. Lactoferrin, a multi-functional glycoprotein: Active therapeutic, drug nanocarrier & targeting ligand. Biomaterials. 2020;263:120355. doi: 10.1016/j.biomaterials.2020.120355. - DOI - PMC - PubMed
    1. Wang B., Timilsena Y.P., Blanch E., Adhikari B. Lactoferrin: Structure, function, denaturation and digestion. Crit. Rev. Food Sci. Nutr. 2019;59:580–596. doi: 10.1080/10408398.2017.1381583. - DOI - PubMed
    1. Metz-Boutigue M.H., Jolles J., Mazurier J., Schoentgen F., Legrand D., Spik G., Montreuil J., Jolles P. Human lactotransferrin: Amino acid sequence and structural comparisons with other transferrins. Eur. J. Biochem. 1984;145:659–676. doi: 10.1111/j.1432-1033.1984.tb08607.x. - DOI - PubMed
    1. Gonzalez-Chavez S.A., Arevalo-Gallegos S., Rascon-Cruz Q. Lactoferrin: Structure, function and applications. Int. J. Antimicrob. Agents. 2009;33:e301–e308. doi: 10.1016/j.ijantimicag.2008.07.020. - DOI - PubMed
    1. Cutone A., Rosa L., Ianiro G., Lepanto M.S., Bonaccorsi di Patti M.C., Valenti P., Musci G. Lactoferrin’s Anti-Cancer Properties: Safety, Selectivity, and Wide Range of Action. Biomolecules. 2020;10:456. doi: 10.3390/biom10030456. - DOI - PMC - PubMed

Publication types

LinkOut - more resources