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Lactoferrin: a Glycoprotein Involved in Immunomodulation, Anticancer, and Antimicrobial Processes

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Lactoferrin: a Glycoprotein Involved in Immunomodulation, Anticancer, and Antimicrobial Processes molecules Review Lactoferrin: A Glycoprotein Involved in Immunomodulation, Anticancer, and Antimicrobial Processes Quintín Rascón-Cruz, Edward A. Espinoza-Sánchez, Tania S. Siqueiros-Cendón , Sayuri I. Nakamura-Bencomo , Sigifredo Arévalo-Gallegos and Blanca F. Iglesias-Figueroa * Laboratorio de Biotecnología I, Facultad de Ciencias Químicas, Universidad Autónoma de Chihuahua, Circuito Universitario s/n Campus Universitario 2, Chihuahua C.P. 31125, Mexico; [email protected] (Q.R.-C.); [email protected] (E.A.E.-S.); [email protected] (T.S.S.-C.); [email protected] (S.I.N.-B.); [email protected] (S.A.-G.) * Correspondence: bfi[email protected]; Tel.: +52-614-2366-000 Abstract: Lactoferrin is an iron binding glycoprotein with multiple roles in the body. Its participation in apoptotic processes in cancer cells, its ability to modulate various reactions of the immune system, and its activity against a broad spectrum of pathogenic microorganisms, including respiratory viruses, have made it a protein of broad interest in pharmaceutical and food research and industry. In this review, we have focused on describing the most important functions of lactoferrin and the possible mechanisms of action that lead to its function. Keywords: lactoferrin; immune system; anti-cancer activity; antibacterial activity 1. Introduction Citation: Rascón-Cruz, Q.; Espinoza- Current lifestyles and emerging diseases that threaten everyday life have led to the Sánchez, E.A.; Siqueiros-Cendón, T.S.; search for new, more natural, pharmacological alternatives to face new challenges in Nakamura-Bencomo, S.I.; Arévalo- medicine. Various human-origin proteins have been studied for a long time because of Gallegos, S.; Iglesias-Figueroa, B.F. their multifunctional characteristics in the body and their practical use as therapeutic Lactoferrin: A Glycoprotein Involved agents. In this context, lactoferrin (Lf), described in the first reports as the “red fraction of in Immunomodulation, Anticancer, and the milk”, is a non-hematic iron-binding glycoprotein, secreted mainly by epithelial cells of Antimicrobial Processes. Molecules 2021, the mammary gland [1,2]. According to its conserved three-dimensional structure and its 26, 205. https://dx.doi.org/10.3390/ ability to chelate iron ions, Lf belongs to the transferrin family [3] and has been reported as molecules26010205 a nutraceutical and multifunctional glycoprotein for its antimicrobial, antiviral, and antifun- gal effects, and recently, it has been shown to be effective in the treatment of neuropathies Academic Editor: Derek J. McPhee and cancer cells [4]. In the present review, we focus on detailing the most important Received: 9 October 2020 Accepted: 12 November 2020 functions of lactoferrin, which make it highly attractive to the pharmaceutical industry. Published: 3 January 2021 2. Lactoferrin Structure and Production Publisher’s Note: MDPI stays neu- Lactoferrin is a non-hematic iron-binding glycoprotein with a molecular weight of tral with regard to jurisdictional claims 78–80 kDa depending on the species. Lf is composed of a simple polypeptide chain in published maps and institutional with approximately 700 amino acids folded into two globular carboxyl (C) and amino affiliations. (N) terminal lobes, which are regions connected through an α-helix and made up of two domains known as C1, C2, N1 and N2, which create a β-sheet [5–7]. The N-terminal lobe includes 1–332, amino acids, whereas the C-terminal lobe includes the amino acids 344–703 [8]. Three potential glycosylation sites have been found in human lactoferrin (hLf) Copyright: © 2021 by the authors. Li- (Asn138, Asn479 and Asn624) and five potential sites in bovine lactoferrin (bLf) (Asn233, censee MDPI, Basel, Switzerland. This Asn281, Asn368, Asn476 and Asn545) (Figure1); these sites are mostly exposed on the outer article is an open access article distributed surface of the molecule and may participate in recognition of specific receptors [9]. Lf has a under the terms and conditions of the high affinity for iron; each lobe can bind to a ferric ion; furthermore, it can bind Cu+2, Zn+2 Creative Commons Attribution (CC BY) +2 license (https://creativecommons.org/ and Mn ions [10]. Mammals produce Lf, and its production is attributed to the cells of licenses/by/4.0/). the epithelial mucosa within the majority of exocrine fluids, including tears, saliva, vaginal Molecules 2021, 26, 205. https://dx.doi.org/10.3390/molecules26010205 https://www.mdpi.com/journal/molecules Molecules 2021, 26, 205 Molecules 2020, 25, x 2 of 152 of 17 affinity for iron; each lobe can bind to a ferric ion; furthermore, it can bind Cu+2, Zn+2 and Mn+2 ions [10]. Mammals produce Lf, and its production is attributed to the cells of the epithelial mucosa within the majorityand seminal of exocrine fluids, fluids, nasal including and bronchial tears,secretions, saliva, vaginal and and bile seminal and gastric fluids, juices. nasal However, and bronchial its highest concentration is found in milk and colostrum; humans produce approximately secretions, and bile and gastric juices. However, its highest concentration is found in milk and 2 g/L and 7 g/L in milk and colostrum, respectively, while in cows its concentration in milk colostrum; humans produce approximately 2 g/L and 7 g/L in milk and colostrum, respectively, while and colostrum is 0.2 g/L and 1.5 g/L, respectively [11,12]. A considerable amount of Lf is in cows its concentration in milk and colostrum is 0.2 g/L and 1.5 g/L, respectively [11,12]. A found in the secondary granules of neutrophils (15 µg/106 neutrophils, and Lf is released considerableinto plasma amount during of Lf an is found inflammatory in the second or infectiousary granules process. of neutrophils Under normal (15 µg/106 conditions, neutrophils, and Lfthe is concentration released into of plasma Lf in plasma during is 0.4–2.0an inflammatoryµg/mL and or it increasesinfectious upprocess. to 200 µUnderg/mL innormal conditions,infections the andconcentration immunological of Lf in disorders plasma [is13 0.4–2.0–15]. The µg/mL concentration and it increases of Lf in up plasma to 200 is µg/mL not in infectionsrelated and to immunological the number of neutrophils, disorders [13–15]. but depends The concentration on the degree of of Lf degranulation in plasma is not of these. related to the numberLikewise, of neutrophils, plasma Lf levels but depends can be alteredon the degre duringe of pregnancy degranulation [16]. Lfof these. has a highLikewise, similarity plasma Lf levelsbetween can be altered species; during human pregnancy Lf (hLf) and [16]. bovine Lf has Lf a high (bLf) similarity show the between highest degree species; of human similarity Lf (hLf) and bovinein terms Lf of(bLf) structure show the and highest function; degree 78% of of simi thelarity human in Lfterms sequence of structure is identical and function; to bovine 78% of the humanLf [17 ].Lf sequence is identical to bovine Lf [17]. Figure 1. Predicted structure of Lactoferrin and its potential glycosylation sites (Asnn). (a) Human lactoferrin. (b) Bovine lactoferrin. Potential asparagine-linked glycosylation sites are shown in red. Figure 1. Predicted structure of Lactoferrin and its potential glycosylation sites (Asnn). (a) Human The glycosylation of the molecule may be strongly involved in the mechanism of action of its various lactoferrin. (b) Bovine lactoferrin. Potential asparagine-linked glycosylation sites are shown in red. physiological processes. The protein sequence was extracted from GenBank: M83202_1 (hLf) and The glycosylation of the molecule may be strongly involved in the mechanism of action of its various M63502_1 (bLf) and modeled using Phyre2 (http://www.sbg.bio.ic.ac.uk/phyre2/[18]). physiological processes. The protein sequence was extracted from GenBank: M83202_1 (hLf) and M63502_13. Immunomodulatory (bLf) and modeled and using Anti-Inflammatory Phyre2 (http://www.sbg.bio.ic.ac.uk/phyre2/ Activity [18]). The immunomodulatory and anti-inflammatory activity of lactoferrin is related to 3. Immunomodulatoryits ability to interact and with Anti-Inflammatory specific cell surface Activity receptors on epithelial cells and cells of the Theimmune immunomodulatory system, as well and as its anti-inf abilitylammatory to bind to pathogen-associatedactivity of lactoferrin molecularis related to patterns its ability to interact(PAMPs), with specific mainly cell recognized surface receptors by Toll-like on epithelial receptors cells (TLRs) and cells [19]. of Such the immune binding system, has been as well reported for Gram-negative bacterial lipopolysaccharide (LPS) [20]. The mechanisms of as its ability to bind to pathogen-associated molecular patterns (PAMPs), mainly recognized by Toll- the interaction of lactoferrin with various receptors are strongly linked to its glycan con- like receptors (TLRs) [19]. Such binding has been reported for Gram-negative bacterial formation; it has been observed that there is an interaction between some TLRs and Lf, lipopolysaccharide (LPS) [20]. The mechanisms of the interaction of lactoferrin with various receptors mediated by glycans of the molecule, allowing an immunomodulatory effect [21,22]. Lf are stronglyalso plays linked a role to inits the glycan differentiation, conformation; maturation, it has been activation, observed migration, that there proliferation, is an interaction betweenand some function TLRs of and cells Lf, belonging mediated to by antigen-presenting glycans of the molecule, cells (APCs), allowing such an immunomodulatory as B cells,
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