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Published: 10 March 2023

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1

Oria, Rosa, Maznah Ismail, Lourdes Sánchez, Miguel Calvo, and Jeremy H. Brock. "Effect of heat treatment and other milk proteins on the interaction of lactoferrin with monocytes." Journal of Dairy Research 60, no. 3 (August 1993): 363–69. http://dx.doi.org/10.1017/s0022029900027709.

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SummaryThe interaction of lactoferrin from human and bovine milk with the human promonocytic cell line U937 has been studied. Both human and bovine Fe-lactoferrins bound to the cells. Binding of bovine lactoferrin was inhibited by excess bovine lactoferrin but not by human lactoferrin, suggesting that the binding mechanisms for the two proteins are different. Binding of human but not bovine lactoferrin was inhibited by bovine lactoperoxidase, while a 20-fold excess of human IgA inhibited binding of human but not bovine lactoferrin. Human and bovine α-lactalbumins, bovine β-lactoglobulin, and human lysozyme had no effect on binding of lactoferrin from either species. Samples of bovine Fe- and apolactoferrin in capillary tubes were exposed to temperatures of 72 °C for 20 s, 85 °C for 20 min or 137 °C for 8 s. All the heated samples inhibited binding of native Fe- and apolactoferrin, though to a lesser extent than the native proteins. Both heated and native lactoferrins enhanced [3H]thymidine incorporation by U937 cells, except for Fe-lactoferrin heated at 85 °C for 20 min, which was inhibitory. These results suggest that heat treatment of lactoferrin under conditions used for industrial processing does not greatly affect its ability to interact with and stimulate monocytic cells, and that other milk proteins in general do not interfere with lactoferrin–monocyte interactions. It may thus be feasible to incorporate biologically active lactoferrin into infant formulas.
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2

Tomita, M., H. Wakabayashi, K. Yamauchi, S. Teraguchi, and H. Hayasawa. "Bovine lactoferrin and lactoferricin derived from milk: production and applications." Biochemistry and Cell Biology 80, no. 1 (February 1, 2002): 109–12. http://dx.doi.org/10.1139/o01-230.

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Bovine lactoferrin is produced on an industrial scale from cheese whey or skim milk. The safety of purified lactoferrin has been confirmed from the results of a reverse mutation test using bacteria, a 13-week oral repeated-dose toxicity study in rats, and clinical studies. In order to apply active lactoferrin to various products, a process for its pasteurization was developed. Subsequently, lactoferrin has been used in a wide variety of products since it was first added to infant formula in 1986. A pepsin hydrolysate of lactoferrin is also used in infant formula. This hydrolysate contains a potent antimicrobial peptide named lactoferricin that is derived from the lactoferrin molecule by pepsin digestion. Semilarge-scale purification of lactoferricin can be performed by hydrophobic interaction chromatography. Lactoferricin also exhibits several biological actions and appears to be the functional domain of lactoferrin. Recent studies have demonstrated that oral administration of lactoferrin or lactoferricin exerts a host-protective effect in various animals and in humans. The results of these studies strongly suggest that the effects of oral lactoferrin are mediated by modulation of the immune system. Further elucidation of the clinical efficacy and mechanism of action of lactoferrin will increase the value of lactoferrin-containing products.Key words: bovine, lactoferrin, lactoferricin.
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3

Wang, Ye, James D. Morton, Alaa EL-Din A. Bekhit, Alan Carne, and Susan L. Mason. "Amino Acid Sequences of Lactoferrin from Red Deer (Cervus elaphus) Milk and Antimicrobial Activity of Its Derived Peptides Lactoferricin and Lactoferrampin." Foods 10, no. 6 (June 7, 2021): 1305. http://dx.doi.org/10.3390/foods10061305.

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Although the bioactivities of bovine lactoferrin have been extensively investigated, little is known about deer milk lactoferrin bioactivity and its amino acid sequence. This research investigated the amino acid sequence of deer lactoferrin and the antimicrobial activities of two lactoferrin-encrypted peptides; lactoferricin (Lfcin) and lactoferrampin (Lfampin). Deer lactoferrin was found to have a molecular weight of 77.1 kDa and an isoelectric point of 7.99, which are similar to that of bovine lactoferrin, 78 kDa and pI 7.9. Deer lactoferrin contains 707 amino acids, one amino acid less than bovine lactoferrin, and has 92% homology with bovine lactoferrin. Deer lactoferricin exhibited strong antimicrobial activity against E. coli American Type Culture Collection (ATCC) 25922 and L. acidophilus ATCC 4356. The antimicrobial activities of deer and bovine Lfcin and Lfampin were compared. Based on MIC, deer Lfcin was found to be a more effective inhibitor of L. acidophilus ATCC 4356 than bovine Lfcin, but bovine Lfcin and Lfampin were more effective against E. coli ATCC 25922 than deer Lfcin and Lfampin. The deer Lfcin sequence differed at seven amino acids from bovine Lfcin and this decreased the net positive charge and increased the hydrophobicity. Deer Lfampin contained two differences in amino acid sequence compared to bovine Lfampin which decreased the net positive charge. These amino acid sequence differences likely account for differences in antibacterial activity. Positive charge and hydrophobic residues provide the amphipathic character of these helical peptides, and are considered important for binding of antimicrobial peptides. In silico modelling of deer Lfcin indicated an identical α-helical structure compared to bovine Lfcin.
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4

Steijns, Jan M., and A. C. M. van Hooijdonk. "Occurrence, structure, biochemical properties and technological characteristics of lactoferrin." British Journal of Nutrition 84, S1 (November 2000): 11–17. http://dx.doi.org/10.1017/s0007114500002191.

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The structure of the iron-binding glycoprotein lactoferrin, present in milk and other exocrine secretions, has been elucidated in great detail, both the three-dimensional protein structure and the attached N-glycans. Structure–function relationships are being established. From these studies a function for lactoferrin in host defence and modulation of iron metabolism emerges. This paper describes in some detail how iron and other cations may be bound by lactoferrins from human or bovine sources and elucidates parts of the molecule that are critical for interactions with cells and biomolecules. Furthermore, the technological aspects, more specifically the heat-sensitivity, of bovine lactoferrin in different matrices are described.
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5

Zaczyńska, Ewa, Jolanta Artym, Maja Kocięba, Timo Burster, Marian Kruzel, Maria Paprocka, and Michał Zimecki. "Antiviral Resistance of Splenocytes in Aged Mice." Polish Journal of Microbiology 66, no. 1 (March 30, 2017): 131–34. http://dx.doi.org/10.5604/17331331.1235002.

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We compared the susceptibility to viral infection of splenocytes, isolated from young versus old CBA mice, and evaluated the antiviral actions of lactoferrin in splenocytes infected with Encephalomyocarditis virus (EMCV). Recombinant mouse lactoferrin (rmLF) and bovine lactoferrin (bLF) were used. There were no differences in the susceptibility to EMCV infection in the studied age categories. Both types of lactoferrins were protective in young and old mice. The study confirmed the undisturbed viral resistance in old mice and the protective actions of lactoferrin in viral infection. The antiviral action of the homologous mouse lactoferrin was demonstrated for the first time.
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6

Yoo, Yung-Choon, Shikiko Watanabe, Ryosuke Watanabe, Katsusuke Hata, Kei-ichi Shimazaki, and Ichiro Azuma. "Bovine Lactoferrin and Lactoferricin, a Peptide Derived from Bovine Lactoferrin, Inhibit Tumor Metastasis in Mice." Japanese Journal of Cancer Research 88, no. 2 (February 1997): 184–90. http://dx.doi.org/10.1111/j.1349-7006.1997.tb00364.x.

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7

Kühnle, Andrea, Thomas Lütteke, Kim Bornhöfft, and Sebastian Galuska. "Polysialic Acid Modulates the Binding of External Lactoferrin in Neutrophil Extracellular Traps." Biology 8, no. 2 (March 28, 2019): 20. http://dx.doi.org/10.3390/biology8020020.

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Neutrophil extracellular traps (NETs) are formed by neutrophils during inflammation. Among other things, these DNA constructs consist of antimicrobial proteins such as lactoferrin and histones. With these properties, NETs capture and destroy invading microorganisms. The carbohydrate polysialic acid (polySia) interacts with both lactoferrin and histones. Previous experiments demonstrated that, in humans, lactoferrin inhibits the release of NET and that this effect is supported by polySia. In this study, we examined the interplay of lactoferrin and polySia in already-formed NETs from bovine neutrophils. The binding of polySia was considered to occur at the lactoferricin (LFcin)-containing domain of lactoferrin. The interaction with the peptide LFcin was studied in more detail using groups of defined polySia chain lengths, which suggested a chain-length-dependent interaction mechanism with LFcin. The LFcin domain of lactoferrin was found to interact with DNA. Therefore, the possibility that polySia influences the integration of lactoferrin into the DNA-structures of NETs was tested by isolating bovine neutrophils and inducing NETosis. Experiments with NET fibers saturated with lactoferrin demonstrated that polySia initiates the incorporation of external lactoferrin in already-loaded NETs. Thus, polySia may modulate the constituents of NET.
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8

Buchta, Richard. "Ovine lactoferrin: isolation from colostrum and characterization." Journal of Dairy Research 58, no. 2 (May 1991): 211–18. http://dx.doi.org/10.1017/s0022029900029757.

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SummaryHighly purified lactoferrin was isolated from ovine colostrum by sequential purification on CM-Sephadex C-50 and Blue-Sepharose, with overall yield of 55%. The ovine lactoferrin was characterized by SDS-PAGE, its amino acid composition and N-terminal sequence to residue 30. Homology with bovine and human lactoferrins was greater than 80 and 50% respectively. Antibodies to ovine lactoferrin were raised in rabbits and used to develop an enzyme-linked immuno-sorbent assay (ELISA). The antiserum was not cross reactive with other colostrum proteins.
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9

Mirayanti, Ni Luh Wayan Yulia, I. Gusti Ngurah Kade Mahardika, and Made Pharmawati. "Produksi Rekombinan Bovine Lactoferrin pada Sistem Ekspresi Eschericihia coli." Jurnal Veteriner 23, no. 1 (March 31, 2022): 105–11. http://dx.doi.org/10.19087/jveteriner.2022.23.1.105.

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Lactoferrin merupakan glikoprotein berukuran 80 kDa yang memiliki keunggulan dalam aktivitas biologis sebagai antimikroba, antibakteri, antivirus, antiparasit, hingga imunomodulator. Kemajuan bidang teknologi rekombinan memungkinkan untuk menghasilkan protein lactoferrin dalam skala besar, sehingga produksi rekombinan lactoferrin dapat dilakukan di berbagai sistem ekspresi. Escherichia coli menjadi salah satu inang pada sistem ekspresi yang banyak digunakan dalam produksi protein rekombinan. Rekombinan protein bovine lactoferrin diproduksi dengan penyisipan gen bovine lactoferrin pada plasmid pET 11-a. Gen bovine lactoferrin yang telah disisipkan dalam plasmid pET, selanjutnya ditransformasikan dan diekspresikan ke dalam sel inang E. coli BL21. Ekspresi protein bovine lactoferrin diinduksi dengan penambahan chaperone salah satu koekspresi, yang mendampingi sistem sintesis E.coli untuk mencapai ekspresi protein yang diinginkan. Ekspresi plasmid pET11a – Bovlacto dalam bakteri E.coli didukung oleh induser L-arabinosa dan IPTG. Gen bovine lactoferrin yang tersisip di dalam plasmid rekombinan pET-11a telah mampu diekspresikan dengan baik di dalam bakteri E.coli BL21 dengan adanya sinyal hibridisasi pada uji metode dot blot dan pita spesifik target yaitu pada kisaran posisi 80-85 kDa hasil elektroforesis SDS-PAGE.
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10

Kühnle, Andrea, Christina E. Galuska, Kristina Zlatina, and Sebastian P. Galuska. "The Bovine Antimicrobial Peptide Lactoferricin Interacts with Polysialic Acid without Loss of Its Antimicrobial Activity against Escherichia coli." Animals 10, no. 1 (December 18, 2019): 1. http://dx.doi.org/10.3390/ani10010001.

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The lactoferrin-derived peptide lactoferricin (LFcin) belongs to the family of antimicrobial peptides, and its bovine form has already been successfully applied to counteract enterohemorrhagic Escherichia coli (EHEC) infection. Recently, it was described that LFcin interacts with the sugar polymer polysialic acid (polySia) and that the binding of lactoferrin to polySia is mediated by LFcin, included in the N-terminal domain of lactoferrin. For this reason, the impact of polySia on the antimicrobial activity of bovine LFcin was investigated. Initially, the interaction of LFcin was characterized in more detail by native agarose gel electrophoresis, demonstrating that a chain length of 10 sialic acid residues was necessary to bind LFcin, whereas approximately twice-as-long chains were needed to detect binding of lactoferrin. Remarkably, the binding of polySia showed, independently of the chain length, no impact on the antimicrobial effects of LFcin. Thus, LFcin binds polySia without loss of its protective activity as an antimicrobial peptide.
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11

Longhi, C., M. P. Conte, S. Ranaldi, M. Penta, P. Valenti, A. Tinari, F. Superti, and L. Seganti. "Apoptotic Death of Listeria Monocytogenes-Infected Human Macrophages Induced by Lactoferricin B, A Bovine Lactoferrin-Derived Peptide." International Journal of Immunopathology and Pharmacology 18, no. 2 (April 2005): 317–25. http://dx.doi.org/10.1177/039463200501800214.

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Listeria monocytogenes, an intracellular facultative food-borne pathogen, was reported to induce apoptosis in vitro and in vivo in a variety of cell types with the exception of murine macrophages. These cells represent the predominant compartment of bacterial multiplication and die as a result of necrosis. In this study we showed that human non-activated and IFN-γ-activated macrophagic-like (THP-1) cells infected with L. monocytogenes, mainly die by necrosis rather than by an apoptotic process. Two natural products derived from bovine milk, lactoferrin and its derivative peptide lactoferricin B, are capable of regulating the fate of infected human macrophages. Bovine lactoferrin treatment of macrophages protects them from L. monocytogenes-induced death whereas lactoferricin B, its derivative peptide, determines a shifting of the equilibrium from necrosis to apoptosis.
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12

Sayers, Edward John, Iwan Palmer, Lucy Hope, Paul Hope, Peter Watson, and Arwyn Tomos Jones. "Fluid-Phase Endocytosis and Lysosomal Degradation of Bovine Lactoferrin in Lung Cells." Pharmaceutics 14, no. 4 (April 13, 2022): 855. http://dx.doi.org/10.3390/pharmaceutics14040855.

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The iron-binding protein lactoferrin and the cell-penetrating peptides derived from its sequence utilise endocytosis to enter different cell types. The full-length protein has been extensively investigated as a potential therapeutic against a range of pathogenic bacteria, fungi, and viruses, including SARS-CoV-2. As a respiratory antiviral agent, several activity mechanisms have been demonstrated for lactoferrin, at the extracellular and plasma membrane levels, but as a protein that enters cells it may also have intracellular antiviral activity. Characterisation of lactoferrin’s binding, endocytic traffic to lysosomes, or recycling endosomes for exocytosis is lacking, especially in lung cell models. Here, we use confocal microscopy, flow cytometry, and degradation assays to evaluate binding, internalisation, endocytic trafficking, and the intracellular fate of bovine lactoferrin in human lung A549 cells. In comparative studies with endocytic probes transferrin and dextran, we show that lactoferrin binds to negative charges on the cell surface and actively enters cells via fluid-phase endocytosis, in a receptor-independent manner. Once inside the cell, we show that it is trafficked to lysosomes where it undergoes degradation within two hours. These findings provide opportunities for investigating both lactoferrin and derived cell-penetrating peptides activities of targeting intracellular pathogens.
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13

Cutone, Antimo, Luigi Rosa, Maria Carmela Bonaccorsi di Patti, Federico Iacovelli, Maria Pia Conte, Giusi Ianiro, Alice Romeo, et al. "Lactoferrin Binding to SARS-CoV-2 Spike Glycoprotein Blocks Pseudoviral Entry and Relieves Iron Protein Dysregulation in Several In Vitro Models." Pharmaceutics 14, no. 10 (October 3, 2022): 2111. http://dx.doi.org/10.3390/pharmaceutics14102111.

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SARS-CoV-2 causes COVID-19, a predominantly pulmonary disease characterized by a burst of pro-inflammatory cytokines and an increase in free iron. The viral glycoprotein Spike mediates fusion to the host cell membrane, but its role as a virulence factor is largely unknown. Recently, the antiviral activity of lactoferrin against SARS-CoV-2 was demonstrated in vitro and shown to occur via binding to cell surface receptors, and its putative interaction with Spike was suggested by in silico analyses. We investigated the anti-SARS-CoV-2 activity of bovine and human lactoferrins in epithelial and macrophagic cells using a Spike-decorated pseudovirus. Lactoferrin inhibited pseudoviral fusion and counteracted the deleterious effects of Spike on iron and inflammatory homeostasis by restoring basal levels of iron-handling proteins and of proinflammatory cytokines IL-1β and IL-6. Using pull-down assays, we experimentally proved for the first time that lactoferrin binds to Spike, immediately suggesting a mechanism for the observed effects. The contribution of transferrin receptor 1 to Spike-mediated cell fusion was also experimentally demonstrated. In silico analyses showed that lactoferrin interacts with transferrin receptor 1, suggesting a multifaceted mechanism of action for lactoferrin. Our results give hope for the use of bovine lactoferrin, already available as a nutraceutical, as an adjuvant to standard therapies in COVID-19.
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14

Shimazaki, Kei-ichi, and Kazuhiro Kawai. "Advances in lactoferrin research concerning bovine mastitis." Biochemistry and Cell Biology 95, no. 1 (February 2017): 69–75. http://dx.doi.org/10.1139/bcb-2016-0044.

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Lactoferrin is a multifunctional, iron-binding glycoprotein found in milk and other exocrine secretions. Lactoferrin in milk plays vital roles in the healthy development of newborn mammals, and is also an innate resistance factor involved in the prevention of mammary gland infection by microorganisms. Inflammation of the udder because of bacterial infection is referred to as mastitis. There have been many investigations into the relationships between lactoferrin and mastitis, which fall into several categories. The main categories are fluctuations in the lactoferrin concentration of milk, lactoferrin activity against mastitis pathogens, elucidation of the processes underlying the onset of mastitis, participation of lactoferrin in the immune system, and utilization of lactoferrin in mastitis treatment and prevention. This minireview describes lactoferrin research concerning bovine mastitis. In the 1970s, many researchers reported that the lactoferrin concentration fluctuates in milk from cows with mastitis. From the late 1980s, many studies clarified the infection-defense mechanism in the udder and the contribution of lactoferrin to the immune system. After the year 2000, the processes underlying the onset of mastitis were elucidated in vivo and in vitro, and lactoferrin was applied for the treatment and prevention of mastitis.
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15

Brooks, Cory L., Elena Arutyunova, and M. Joanne Lemieux. "The structure of lactoferrin-binding protein B fromNeisseria meningitidissuggests roles in iron acquisition and neutralization of host defences." Acta Crystallographica Section F Structural Biology Communications 70, no. 10 (September 25, 2014): 1312–17. http://dx.doi.org/10.1107/s2053230x14019372.

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Pathogens have evolved a range of mechanisms to acquire iron from the host during infection. Several Gram-negative pathogens including members of the generaNeisseriaandMoraxellahave evolved two-component systems that can extract iron from the host glycoproteins lactoferrin and transferrin. The homologous iron-transport systems consist of a membrane-bound transporter and an accessory lipoprotein. While the mechanism behind iron acquisition from transferrin is well understood, relatively little is known regarding how iron is extracted from lactoferrin. Here, the crystal structure of the N-terminal domain (N-lobe) of the accessory lipoprotein lactoferrin-binding protein B (LbpB) from the pathogenNeisseria meningitidisis reported. The structure is highly homologous to the previously determined structures of the accessory lipoprotein transferrin-binding protein B (TbpB) and LbpB from the bovine pathogenMoraxella bovis. Docking the LbpB structure with lactoferrin reveals extensive binding interactions with the N1 subdomain of lactoferrin. The nature of the interaction precludes apolactoferrin from binding LbpB, ensuring the specificity of iron-loaded lactoferrin. The specificity of LbpB safeguards proper delivery of iron-bound lactoferrin to the transporter lactoferrin-binding protein A (LbpA). The structure also reveals a possible secondary role for LbpB in protecting the bacteria from host defences. Following proteolytic digestion of lactoferrin, a cationic peptide derived from the N-terminus is released. This peptide, called lactoferricin, exhibits potent antimicrobial effects. The docked model of LbpB with lactoferrin reveals that LbpB interacts extensively with the N-terminal lactoferricin region. This may provide a venue for preventing the production of the peptide by proteolysis, or directly sequestering the peptide, protecting the bacteria from the toxic effects of lactoferricin.
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16

Hoek, K. S., J. M. Milne, P. A. Grieve, D. A. Dionysius, and R. Smith. "Antibacterial activity in bovine lactoferrin-derived peptides." Antimicrobial Agents and Chemotherapy 41, no. 1 (January 1997): 54–59. http://dx.doi.org/10.1128/aac.41.1.54.

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Several peptides sharing high sequence homology with lactoferricin B (Lf-cin B) were generated from bovine lactoferrin (Lf) with recombinant chymosin. Two peptides were copurified, one identical to Lf-cin B and another differing from Lf-cin B by the inclusion of a C-terminal alanine (lactoferricin). Two other peptides were copurified from chymosin-hydrolyzed Lf, one differing from Lf-cin B by the inclusion of C-terminal alanyl-leucine and the other being a heterodimer linked by a disulfide bond. These peptides were isolated in a single step from chymosin-hydrolyzed Lf by membrane ion-exchange chromatography and were purified by reverse-phase high-pressure liquid chromatography (HPLC). They were characterized by N-terminal Edman sequencing, mass spectrometry, and antibacterial activity determination. Pure lactoferricin, prepared from pepsin-hydrolyzed Lf, was purified by standard chromatography techniques. This peptide was analyzed against a number of gram-positive and gram-negative bacteria before and after reduction of its disulfide bond or cleavage after its single methionine residue and was found to inhibit the growth of all the test bacteria at a concentration of 8 microM or less. Subfragments of lactoferricin were isolated from reduced and cleaved peptide by reverse-phase HPLC. Subfragment 1 (residues 1 to 10) was active against most of the test microorganisms at concentrations of 10 to 50 microM. Subfragment 2 (residues 11 to 26) was active against only a few microorganisms at concentrations up to 100 microM. These antibacterial studies indicate that the activity of lactoferricin is mainly, but not wholly, due to its N-terminal region.
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17

Uchida, Ryo, Reiji Aoki, Ayako Aoki-Yoshida, Atsushi Tajima, and Yoshiharu Takayama. "Promoting effect of lactoferrin on barrier function and epithelial differentiation of human keratinocytes." Biochemistry and Cell Biology 95, no. 1 (February 2017): 64–68. http://dx.doi.org/10.1139/bcb-2016-0147.

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The purpose of this study was to elucidate the effects of bovine lactoferrin on keratinocyte differentiation and barrier function. Addition of bovine lactoferrin to differentiating HaCaT human keratinocytes led to increased transepithelial electrical resistance (TER), a marker of epithelial barrier function. This elevation was followed by upregulation of two differentiation markers, involucrin and filaggrin. The expression level of sterol regulatory element-binding protein-1 was also enhanced by bovine lactoferrin. The lactoferrin-induced upregulation of involucrin and filaggrin expression were confirmed in normal human epidermal keratinocytes (NHEK). Treatment with SB203580, a p38 mitogen-activated protein kinase (MAPK) α inhibitor, impaired the upregulation of involucrin and filaggrin expression in response to lactoferrin. The elevation of p38 MAPK phosphorylation was further enhanced by lactoferrin in the initial stage of differentiation of HaCaT keratinocytes. The findings suggest that bovine lactoferrin promotes epithelial differentiation by a p38-MAPK-dependent mechanism.
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18

Plate, Kerstin, Sascha Beutel, Heinrich Buchholz, Wolfgang Demmer, Stefan Fischer-Frühholz, Oscar Reif, Roland Ulber, and Thomas Scheper. "Isolation of bovine lactoferrin, lactoperoxidase and enzymatically prepared lactoferricin from proteolytic digestion of bovine lactoferrin using adsorptive membrane chromatography." Journal of Chromatography A 1117, no. 1 (June 2006): 81–86. http://dx.doi.org/10.1016/j.chroma.2006.03.090.

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19

Dix, Clare, and Olivia Wright. "Bioavailability of a Novel Form of Microencapsulated Bovine Lactoferrin and Its Effect on Inflammatory Markers and the Gut Microbiome: A Pilot Study." Nutrients 10, no. 8 (August 17, 2018): 1115. http://dx.doi.org/10.3390/nu10081115.

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Bovine lactoferrin, extracted from milk or whey, is used in a range of products to enhance immunity and support digestive health, iron absorption, and homeostasis. This study examined the absorption and effect of Progel (Brisbane, Queensland, Australia) microencapsulated bovine lactoferrin (InferrinTM, Bega Bionutrients, Victoria, Australia) on immune markers and the microbiome. A double-blind randomised, cross-over trial was conducted with 12 healthy males randomised to one of two doses, equivalent to 200 mg or 600 mg lactoferrin, for two four-week supplementation arms, with a two-week washout period. Subjects received either standard bovine lactoferrin or InferrinTM for each arm. Baseline and post each trial arm, CD69+ activation on CD4+ and CD8+ cells was analysed, bovine and human lactoferrin contents of faecal and serum samples were reported, and the gut microbiome was analysed using 16S sequencing and metagenomic sequencing. The mean level of CD69+ activation on the CD4+ cells was lower after supplementation regardless of the form or dose of lactoferrin. This was statistically significant for the 200 mg dose. A higher level of bovine lactoferrin was found post-supplementation in those taking InferrinTM, although this was not statistically significant. Changes in phylum-level microbial community profiling were detected post-supplementation in the second trial arm, particularly in those receiving InferrinTM. Metagenomic sequencing showed changes in the volumes of the top 100 species of bacteria present before and after all treatment arms. Results suggest that lactoferrin supplementation may have beneficial effects on the microbiome and immune system, and that the use of InferrinTM improves absorption. Larger detailed studies are needed to ascertain the potential positive effects of bovine lactoferrin supplementation.
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20

Kong, Ying Ying, Meng Liu, Wei Di, Cong Wang, Ming Du, and Lan Wei Zhang. "Purification and Identification of Lactoferrin from Bovine Milk." Advanced Materials Research 524-527 (May 2012): 2290–93. http://dx.doi.org/10.4028/www.scientific.net/amr.524-527.2290.

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Lactoferrin has many kinds of bioactivities which have attracted more and more attention. In the present study, lactoferrin from bovine milk was isolated and purified by membrane filtration, series of chromatography on SP Sepharose Big Bead ion exchange column and Superdex 200 gel filtration column. The purified lactoferrin was identified by SDS-PAGE compared with the lactoferrin standard.
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21

León-Sicairos, Nidia, Magda Reyes-López, Cynthia Ordaz-Pichardo, and Mireya de la Garza. "Microbicidal action of lactoferrin and lactoferricin and their synergistic effect with metronidazole inEntamoeba histolyticaThis paper is one of a selection of papers published in this Special Issue, entitled 7th International Conference on Lactoferrin: Structure, Function, and Applications, and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 84, no. 3 (June 2006): 327–36. http://dx.doi.org/10.1139/o06-060.

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Lactoferrin (Lf), in its iron-free form, has been shown to inhibit the growth of pathogenic microorganisms. In the light of new agents to control amoebiasis, the microbicidal activity of human and bovine Lf and bovine lactoferricin (bLfcin, fragment 4–14), and of each combined with metronidazole, the main drug used in amoebiasis, was evaluated in trophozoites of Entamoeba histolytica. Both lactoferrins and bLfcin were able to kill amoebas in a concentration-dependent manner. This killing effect was modulated according to the culture age, pH, and temperature. Parasites obtained from the stationary phase were more susceptible to Lf than those from the early exponential phase. The effect of Lf and its derived peptide, bLfcin, was prevented by both Fe2+and Fe3+. However, the divalent cations Mg2+and Ca2+prevented the killing effect of Lf but not of bLfcin. A synergistic amoebicidal effect was found between metronidazole and human Lf, bovine Lf, or bLfcin. These data suggest that Lf and bLfcin might be used in amoebiasis if they are administered with a low dose of metronidazole to diminish the toxicity of this drug. Thus, Lf and bLfcin are therapeutically potential candidates for use as antiamoebics in patients.
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ANTONINI, GIOVANNI, MARIA ROSARIA CATANIA, RITA GRECO, CATIA LONGHI, MARIA GRAZIA PISCIOTTA, LUCILLA SEGANTI, and PIERA VALENTI. "Anti-Invasive Activity of Bovine Lactoferrin against Listeria monocytogenes." Journal of Food Protection 60, no. 3 (March 1, 1997): 267–71. http://dx.doi.org/10.4315/0362-028x-60.3.267.

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We have investigated the possible role of bovine lactoferrin in protecting the intestinal epithelium from bacterial infections, using as an in vitro model enterocyte-like cell lines HT-39 and Caco-2 infected with a food-borne pathogen, Listeria monocytogenes. When infection occurred in the presence of 1 mg/ml of bovine lactoferrin, in the form of apolactoferrin or iron- or manganese-saturated forms, the adhesion of bacteria to eukaryotk cells was unaffected, but the number of internalized bacteria was reduced by 42- to 125-fold. The possibility of a toxic effect of lactoferrin was excluded, because bovine lactoferrin was used at nonbactericidal and noncytotoxic concentrations.
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Dial, Elizabeth J., and Lenard M. Lichtenberger. "Effect of lactoferrin onHelicobacter felisinduced gastritis." Biochemistry and Cell Biology 80, no. 1 (February 1, 2002): 113–17. http://dx.doi.org/10.1139/o01-205.

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Lactoferrin possesses antibiotic, antiinflammatory, and immune-modulating properties that may be active against the gastritis-, ulcer- and cancer-inducing bacterium Helicobacter pylori. In vitro testing of bovine and human lactoferrin by several laboratories has shown significant bacteriostatic and bactericidal activity. Subsequent in vivo testing of bovine lactoferrin in animal models of H. pylori infection has shown beneficial effects of this agent. Our laboratory has utilized a mouse model that is infected with the feline strain of this bacterium, H. felis. The resulting gastritis that develops in this model and the effects of bovine lactoferrin and recombinant human lactoferrin (from Aspergillus niger var. awamori, Agennix Inc., Houston, Tex.) treatment were assessed by various measures. Infected animals treated with orally administered lactoferrin showed reversals in all parameters. In addition, when recombinant human lactoferrin was used in combination with low doses of amoxicillin or tetracycline, there was an enhancement in gastritis-reducing activity. Possible mechanisms for these effects of lactoferrin are discussed. Lactoferrin has significant, orally active in vivo actions and should be further investigated for clinical situations involving Helicobacter infections where it may have utility when administered alone and also when given in combination with established antibiotic agents.Key words: lactoferrin, Helicobacter, gastritis, surface hydrophobicity.
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Giansanti, Francesco, Paola Rossi, Maria Teresa Massucci, Dario Botti, Giovanni Antonini, Piera Valenti, and Lucilla Seganti. "Antiviral activity of ovotransferrin discloses an evolutionary strategy for the defensive activities of lactoferrin." Biochemistry and Cell Biology 80, no. 1 (February 1, 2002): 125–30. http://dx.doi.org/10.1139/o01-208.

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Ovotransferrin (formerly conalbumin) is an iron-binding protein present in birds. It belongs to the transferrin family and shows about 50% sequence homology with mammalian serum transferrin and lactoferrin. This protein has been demonstrated to be capable of delivering iron to cells and of inhibiting bacterial multiplication. However, no antiviral activity has been reported for ovotransferrin, although the antiviral activity of human and bovine lactoferrins against several viruses, including human herpes simplex viruses, has been well established. In this report, the antiviral activity of ovotransferrin towards chicken embryo fibroblast infection by Marek's disease virus (MDV), an avian herpesvirus, was clearly demonstrated. Ovotransferrin was more effective than human and bovine lactoferrins in inhibiting MDV infection and no correlation between antiviral efficacy and iron saturation was found. The observations reported here are of interest from an evolutionary point of view since it is likely that the defensive properties of transferrins appeared early in evolution. In birds, the defensive properties of ovotransferrin remained joined to iron transport functions; in mammals, iron transport functions became peculiar to serum transferrin, and the defensive properties towards infections were optimised in lactoferrin.Key words: ovotransferrin, lactoferrin, Marek disease's virus, herpes simplex virus, evolution.
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Perraudin, Jean-Paul, and Léo De Valck. "Lactoferrin Production from Bovine Milk or Cheese Whey." Journal of Engineering and Applied Sciences Technology 2, no. 1 (March 31, 2020): 1–9. http://dx.doi.org/10.47363/jeast/2020(2)103.

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Today, the industrial scale production of lactoferrin is carried out in one step by extraction from bovine milk or whey. As the role of lactoferrin in the milk is to protect the liquid against the bacterial contamination binding the lipopolysaccharides (LPS) of those bacteria, it is not surprising that the lactoferrin extracted from milk is covered by bacterial LPS, losing the most part of its biological activities. It is absolutely crucial that the production of Lactoferrin consists to a two steps process. The first step consists to extract from milk or from whey a solution that we called lactenin which contains different molecules including lactoferrin, lactoperoxidase, angiogenin and some other minor components. The second step consists to purify the lactoferrin from the other components including the LPS. Only under such conditions, we could recuperate a high level pure molecule with all its biological activities as it is not done actually.
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26

Hu, W. L., E. Regoeczi, P. A. Chindemi, and M. Bolyos. "Lactoferrin interferes with uptake of iron from transferrin and asialotransferrin by the rat liver." American Journal of Physiology-Gastrointestinal and Liver Physiology 264, no. 1 (January 1, 1993): G112—G117. http://dx.doi.org/10.1152/ajpgi.1993.264.1.g112.

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Intravenous injection of bovine or human lactoferrin (6.25 x 10(-2) mumol/100 g body wt) in rats resulted in marked reduction of hepatic iron uptake from transferrin and asialotransferrin. The effect was dose dependent, saturable at approximately 5 mg/100 g body wt, and independent of lactoferrin's iron content. At this dose level, iron uptake from transferrin was reduced by 28% and from asialotransferrin by 43% in experiments lasting 90 min. Bovine lactoperoxidase, another basic protein, was similarly effective. The clearance of asialofetuin and pinocytosis of polyvinylpyrrolidone remained unaffected. Perfusion of isolated rat livers at 4 degrees C showed a strong reduction in asialotransferrin binding in the presence of lactoferrin. Chromatography of hepatic heparan sulfate proteoglycan on immobilized lactoferrin, lactoperoxidase, asialotransferrin, and transferrin showed that it possessed affinity for each of these proteins, more for the first two than the latter two. Heparan sulfate proteoglycan binding and efficacy in reducing hepatic iron uptake were also studied after selective modifications of positively charged amino acids in these proteins. The data obtained are compatible with the hypothesis that lactoferrin and other proteins with similarly high affinity for hepatic heparan sulfate exert their negative effect on iron uptake by preventing transferrin binding to the proteoglycan. The possibility is thus raised that the large number of low-affinity transferrin binding sites reported by earlier investigators for the liver may be heparan sulfate molecules.
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Massucci, Maria Teresa, Francesco Giansanti, Giovanna Di Nino, Manola Turacchio, Maria Federica Giardi, Dario Botti, Rodolfo Ippoliti, et al. "Proteolytic activity of bovine lactoferrin." BioMetals 17, no. 3 (June 2004): 249–55. http://dx.doi.org/10.1023/b:biom.0000027700.90780.45.

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Massucci, Maria Teresa, Francesco Giansanti, Giovanna Di Nino, Manola Turacchio, Maria Federica Giardi, Dario Botti, Rodolfo Ippoliti, et al. "Proteolytic activity of bovine lactoferrin." BioMetals 17, no. 6 (November 2004): 745. http://dx.doi.org/10.1007/s10534-004-5667-x.

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29

Günther, Patrick S., Elfriede Mikeler, Klaus Hamprecht, Jürgen Schneider-Schaulies, Gerhard Jahn, and Kevin M. Dennehy. "CD209/DC-SIGN mediates efficient infection of monocyte-derived dendritic cells by clinical adenovirus 2C isolates in the presence of bovine lactoferrin." Journal of General Virology 92, no. 8 (August 1, 2011): 1754–59. http://dx.doi.org/10.1099/vir.0.030965-0.

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Adenovirus often causes respiratory infection in immunocompromised patients, but relevant attachment receptors have largely not been defined. We show that the antiviral protein bovine lactoferrin enhances infection of monocyte-derived dendritic cells (MDDC) by adenovirus species C serotype 2 (2C) isolates. Under the same conditions infection of MDDC by human cytomegalovirus was reduced. Adenoviral infection was prominently enhanced by bovine but not human lactoferrin, and was not prominently enhanced using blood monocyte-derived macrophages, suggesting that the relevant receptor is expressed on MDDC. Infection of MDDC in the presence of bovine lactoferrin was blocked by mannan, and an antibody to CD209/DC-SIGN but not isotype control or CD46 antibodies. Lastly, U937 macrophages ectopically expressing CD209/DC-SIGN, but not parental U937 cells, were efficiently infected by adenovirus 2C in the presence of bovine lactoferrin. These results may provide a tool, given the high efficiency of infection, to dissect responses by myeloid cells to clinical adenovirus isolates.
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30

Jańczuk, Anna, Aneta Brodziak, Tomasz Czernecki, and Jolanta Król. "Lactoferrin—The Health-Promoting Properties and Contemporary Application with Genetic Aspects." Foods 12, no. 1 (December 23, 2022): 70. http://dx.doi.org/10.3390/foods12010070.

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The aim of the study is to present a review of literature data on lactoferrin’s characteristics, applications, and multiple health-promoting properties, with special regard to nutrigenomics and nutrigenetics. The article presents a new approach to food ingredients. Nowadays, lactoferrin is used as an ingredient in food but mainly in pharmaceuticals and cosmetics. In the European Union, bovine lactoferrin has been legally approved for use as a food ingredient since 2012. However, as our research shows, it is not widely used in food production. The major producers of lactoferrin and the few available food products containing it are listed in the article. Due to anti-inflammatory, antibacterial, antiviral, immunomodulatory, antioxidant, and anti-tumour activity, the possibility of lactoferrin use in disease prevention (as a supportive treatment in obesity, diabetes, as well as cardiovascular diseases, including iron deficiency and anaemia) is reported. The possibility of targeted use of lactoferrin is also presented. The use of nutrition genomics, based on the identification of single nucleotide polymorphisms in genes, for example, FTO, PLIN1, TRAP2B, BDNF, SOD2, SLC23A1, LPL, and MTHFR, allows for the effective stratification of people and the selection of the most optimal bioactive nutrients, including lactoferrin, whose bioactive potential cannot be considered without taking into account the group to which they will be given.
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Wong, Henry, and Anthony B. Schryvers. "Bacterial lactoferrin-binding protein A binds to both domains of the human lactoferrin C-lobe." Microbiology 149, no. 7 (July 1, 2003): 1729–37. http://dx.doi.org/10.1099/mic.0.26281-0.

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Pathogenic bacteria in the family Neisseriaceae express surface receptors to acquire iron from the mammalian iron-binding proteins. Transferrins and lactoferrins constitute a family of iron-binding proteins highly related in both sequence and structure, yet the bacterial receptors are able to distinguish between these proteins and uphold a strict binding specificity. In order to understand the molecular basis for this specificity, the interaction between human lactoferrin (hLf) and the lactoferrin-binding protein A (LbpA) from Moraxella catarrhalis was studied. A periplasmic expression system was designed for the heterologous expression of LbpA, which enabled the investigation of its binding activity in the absence of lactoferrin-binding protein B (LbpB). To facilitate delineation of the LbpA-binding regions of hLf, chimeric proteins composed of hLf and bovine transferrin were made. Binding studies performed with the chimeric proteins and recombinant LbpA identified two binding regions within the C-terminus of hLf. Furthermore, native LbpA from Moraxella and Neisseria spp. bound the identical spectrum of hybrid proteins as the recombinant receptor, demonstrating a conserved binding interaction with the C-lobe of hLf.
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32

Ochoa, Theresa J., Eric L. Brown, Chase E. Guion, Jane Z. Chen, Robert J. McMahon, and Thomas G. Cleary. "Effect of lactoferrin on EnteroaggregativeE. coli(EAEC)This paper is one of a selection of papers published in this Special Issue, entitled 7th International Conference on Lactoferrin: Structure, Function, and Applications, and has undergone the Journal’s usual peer review process." Biochemistry and Cell Biology 84, no. 3 (June 2006): 369–76. http://dx.doi.org/10.1139/o06-053.

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We previously demonstrated that lactoferrin inhibits adherence of enteropathogenic Escherichia coli to HEp-2 cells and decreases invasiveness of Shigella flexneri in HeLa cells by disruption of the type III secretory system (TTSS) of both enteropathogens. To determine whether these effects were specific to the TTSS, we assessed the activity of bovine lactoferrin on enteroaggregative E. coli (EAEC), enteropathogens whose virulence is not TTSS dependent. Bovine lactoferrin at a concentration of 1.0 and 0.1 mg/mL inhibited EAEC growth. Saturation with iron reversed the bacteriostatic effect. Lactoferrin under nonbacteriostatic conditions decreased EAEC adherence to HEp-2 cells as evaluated by microscopy and CFUs; this effect was not iron dependent. Lactoferrin inhibited EAEC biofilm formation and increased autoagglutination. Lactoferrin blocks EAEC adherence by inducing release and degradation of aggregative adherence fimbria, a key element of EAEC pathogenesis. We hypothesized that lactoferrin binding to lipid A of lipopolysaccharide disrupts the virulence proteins anchored to the bacterial outermembrane. These data suggest that the effect of lactoferrin on surface proteins is not restricted to organisms having a TTSS.
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Ahmadinia, Kasra, Dongyao Yan, Michael Ellman, and Hee-Jeong Im. "The anti-catabolic role of bovine lactoferricin in cartilage." BioMolecular Concepts 4, no. 5 (October 1, 2013): 495–500. http://dx.doi.org/10.1515/bmc-2013-0013.

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AbstractBovine lactoferricin (LfcinB) is a multifunctional peptide derived from bovine lactoferrin that demonstrates antibacterial, antifungal, antiviral, antitumor, and immunomodulatory activities. Recently, studies have focused on the anti-catabolic and anti-inflammatory potential of LfcinB. LfcinB is able to modulate the effects cytokines such as IL-1 and fibroblast growth factor 2 as well as promote specific cartilage anabolic factors. These properties are particularly important in maintaining cartilage homeostasis and preventing a catabolic state, which leads to clinical pathology. This review focuses on the recent literature elucidating the role of LfcinB in preventing cartilage degradation.
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Newman, Kari A., Päivi J. Rajala-Schultz, Jeffrey Lakritz, and Fred J. DeGraves. "Lactoferrin concentrations in bovine milk prior to dry-off." Journal of Dairy Research 76, no. 4 (July 29, 2009): 426–32. http://dx.doi.org/10.1017/s0022029909990033.

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Concentration of natural protective factors (NPFs) which have the ability to inhibit growth of mastitis-causing pathogens increase rapidly following the cessation of milking of dairy cows. One such NPF is lactoferrin, an iron-binding protein present in high concentrations in dry-cow secretions. Earlier studies have demonstrated that intermittent milking at the end of lactation increases levels of NPFs in milk and may decrease prevalence of intramammary infections at calving; however, most of these studies date back several decades and may not apply to current high-producing cows. The objective of this study was to assess whether an intermittent milking schedule prior to dry-off increases the concentration of lactoferrin in mammary secretions at the end of lactation and what other factors influence lactoferrin concentration at dry-off. One week prior to dry-off (pre-dry), cows were randomly assigned to an intermittent milking schedule or they continued to be milked twice daily. Duplicate quarter milk samples for microbiological culture were taken at pre-dry and at dry-off to determine infection status of quarters. Quarter somatic cell counts (SCC) were measured on the day of dry-off. Lactoferrin concentrations were quantified by ELISA. Intermittent milking, mean SCC for the last three months prior to dry-off, SCC at dry-off, lactoferrin concentration at pre-dry, quarter infection status at pre-dry and dry-off, days in milk at dry-off, breed, parity, cumulative milk yield for the final week of lactation and season were considered as potential explanatory variables. Their effect on lactoferrin concentration at dry-off was assessed using a mixed-effects linear regression model. Lactoferrin concentration increased significantly during the final week of lactation for cows on an intermittent milking schedule and was significantly associated with initial lactoferrin concentration and infection status at dry-off.
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35

Vogel, Hans J. "Lactoferrin, a bird’s eye view." Biochemistry and Cell Biology 90, no. 3 (June 2012): 233–44. http://dx.doi.org/10.1139/o2012-016.

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Lactoferrin is an abundant iron-binding protein in milk. This 80 kDa bilobal glycoprotein is also present in several other secreted bodily fluids, as well as in the secondary granules of neutrophils. The potent iron-binding properties of lactoferrin can locally create iron deficiency, and this is an important factor in host defense as it prevents bacteria from growing and forming biofilms. In addition to having antibacterial activity, lactoferrin is now known to have a long list of other beneficial biological properties. It has direct antiviral, antifungal, and even some anticancer activities. It can also promote wound healing and bone growth, or it can act as an iron carrier. Moreover, lactoferrin displays a cytokine-like “alarmin” activity, and it activates the immune system. Simultaneously, it can bind endotoxin (lipopolysaccharide), and in doing so, it modulates the activity of the host immune response. The majority of these intriguing biological activities reside in the unique positively charged N-terminal region of the protein. Interestingly, several peptides, which retain many of the beneficial activities, can be released from this region of lactoferrin. An isoform of the human protein, known as delta-lactoferrin, is expressed inside many cells, where it acts as a transcription factor. Lactoferrin purified from human and bovine milk have very similar but not completely identical properties. Lactoferrin receptors have been identified on the surface of various cells, and some of these can bind both the human and the bovine protein. Because of the extensive health-promoting effects of lactoferrin, there has been considerable interest in the use of bovine or human lactoferrin as a “protein nutraceutical” or as a therapeutic protein. When lactoferrin is used as a “biologic drug”, it seems to be orally active in contrast to most other therapeutic proteins.
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Ningtyas, Endah Ariyati Eko, Oedijani Santoso, Udadi Sadhana, and Siti Sunarintyas. "ROLE OF COMBINATION CASEIN AND LACTOFERRIN BOVINE’S COLLOSTRUM AS A PULP CAPPING ON MACROPHAGE EXPRESSION IN MALE WISTAR RATS." ODONTO : Dental Journal 8, no. 2 (December 22, 2021): 156. http://dx.doi.org/10.30659/odj.8.2.156-164.

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ABSTRACTBackground: Inflammatory and/or non-inflammatory processes play a role in stimulating pulp repair and the formation of hard tissue, namely reparative dentin. Macrophages play a role in the pathogenesis and chronic inflammatory disorders. The combination casein lactoferrin of bovine colostrum as an immunomodulator has therapeutic potential. This study aims to determine the therapeutic effect and duration of application of the combination of casein lactoferrin of bovine colostrum, on the expression of macrophages as pulp capping.Method: This study was a true experimental laboratories post test only control group design, consisting of three groups of 60 male wistar rats with 4 observation times, namely day to day 7, 14, 21 and 28 each of 5 mice. The maxillary 1st molars were prepared until the roof of the pulp was exposed. Three groups, namely the combination of casein and lactoferrin bovine colostrum (CKL) and calcium hydroxide (K1) and the untreated group (K0). Each group was filled with glassionomer as a permanent restoration. The tissue was made histological preparations with hematoxylin-eosin staining and the number of macrophages were counted, then analyzed by two way ANOVA and post hoc LSD tests.Result: The results showed that the therapeutic effect and duration of application of the combination of casein and lactoferrin bovine colostrum on the expression of macrophages as pulp cappingConclusion: The combination of casein and lactoferrin of bovine colostrum as capping material can increase the number of macrophages in the healing process of dental pulp.
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WAKABAYASHI, HIROYUKI, KOJI YAMAUCHI, and MITSUNORI TAKASE. "Inhibitory Effects of Bovine Lactoferrin and Lactoferricin B on Enterobacter sakazakii." Biocontrol Science 13, no. 1 (2008): 29–32. http://dx.doi.org/10.4265/bio.13.29.

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Iqomah, Meta, Alek Arisona, Imawan Daru Prasetya, Adretta Soedarmanto, Yanuartono, and Soedarmanto Indarjulianto. "Mini Review: Lactoferrin-binding protein of Streptococcus in Bovine Mastitis." BIO Web of Conferences 49 (2022): 01008. http://dx.doi.org/10.1051/bioconf/20224901008.

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Bovine mastitis is an udder inflammation mostly found in dairy cattle that causes enormous economic losses. Streptococcus is a bacterium that is often found in mastitis, including Streptococcus agalactiae, Streptococcus dysgalactiae, and Streptococcus uberis. These three species have lactoferrinbinding protein (LBP) as one of their virulence factors. Lactoferrin is a host innate immune protein that acts as antibacterial, immunomodulator, anti-adhesion, and has iron-binding properties. The LBP on the surface of Streptococcus could bind to lactoferrin produced by host cells. Uniquely, the three Streptococcus bacteria showed different responses to lactoferrin. The lactoferrin-LBP bound on S. agalactiae and S. dysgalactiae was known to inhibit their penetration ability into the host epithelial cells, on the contrary, in S. uberis it could enhance their ability to invade the cells. This paper aims to review the role of the lactoferrin-binding protein of Streptococcus in bovine mastitis.
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Kawakami, H., S. Dosako, and B. Lonnerdal. "Iron uptake from transferrin and lactoferrin by rat intestinal brush-border membrane vesicles." American Journal of Physiology-Gastrointestinal and Liver Physiology 258, no. 4 (April 1, 1990): G535—G541. http://dx.doi.org/10.1152/ajpgi.1990.258.4.g535.

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Interaction of 59Fe-labeled rat transferrin, human lactoferrin, and bovine lactoferrin with rat small intestinal brush-border membrane vesicles was investigated with the use of a rapid filtration technique. Specific binding of 59Fe-labeled rat transferrin and bovine lactoferrin to brush-border membrane vesicles from suckling and adult rats was identified. In contrast, no binding of human lactoferrin occurred. The presence of transferrin receptors on the brush-border membrane of suckling rats was confirmed by immunoblotting, and the molecular mass of the receptor was 96 kDa under nonreducing conditions. Scatchard plot analysis indicated 2.4 x 10(14) binding sites/mg of membrane protein with an affinity constant (Ka) of 4.9 x 10(6) M-1 for rat milk transferrin and 2.2 x 10(14) bi
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40

Wróbel, Małgorzata, Joanna Małaczewska, and Edyta Kaczorek-Łukowska. "Antiviral Effect of Bovine Lactoferrin against Enterovirus E." Molecules 27, no. 17 (August 29, 2022): 5569. http://dx.doi.org/10.3390/molecules27175569.

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Enterovirus E (EV-E), a representative of the Picornaviridae family, endemically affects cattle across the world, typically causing subclinical infections. However, under favorable conditions, severe or fatal disorders of the respiratory, digestive, and reproductive systems may develop. There is no specific treatment for enterovirus infections in humans or animals, and only symptomatic treatment is available. The aim of this study was to determine the in vitro antiviral effect of bovine lactoferrin (bLF) against enterovirus E using virucidal, cytopathic effect inhibition, and viral yield reduction assays in MDBK cells. The influence of lactoferrin on the intracellular viral RNA level was also determined. Surprisingly, lactoferrin did not have a protective effect on cells, although it inhibited the replication of the virus during the adsorption and post-adsorption stages (viral titres reduced by 1–1.1 log). Additionally, a decrease in the viral RNA level in cells (by up to 75%) was observed. More detailed studies are needed to determine the mechanism of bovine lactoferrin effect on enterovirus E. However, this highly biocompatible protein ensures some degree of protection against infection by bovine enterovirus, which is particularly important for young animals that receive this protein in their mother’s milk.
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41

Teng, Christina T. "Lactoferrin gene expression and regulation: an overview." Biochemistry and Cell Biology 80, no. 1 (February 1, 2002): 7–16. http://dx.doi.org/10.1139/o01-215.

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Lactoferrin is highly conserved among human, mouse, bovine, and porcine species. The numbers of amino acids encoded by 15 of the 17 exons in these species are identical, and in 12 locations, they have identical codon interruptions at the intron-exon splice junctions. However, lactoferrin expression is both ubiquitous and species, tissue, and cell-type specific. It is differentially regulated through multiple signaling pathways such as steroid hormone, growth factor, and kinase cascade pathways. Comparing the lactoferrin gene promoters from different species, common and different characteristics are observed. The human, mouse, bovine, porcine, and bubaline (African antelope) promoters all contain a noncanonical TATA box with an adjacent Sp1 site. Both human and mouse have multiple steroid hormone response elements, while none are found in the other species studied, suggesting that the lactoferrin gene is differentially regulated among different species by steroid hormones. Several transcription factors have been identified that are crucial for the expression of the lactoferrin gene during differentiation of the myeloid cells and in estrogen and epidermal growth factor regulation. This article provides an overview on lactoferrin expression and regulation in different species.Key words: lactoferrin, gene promoter, transcription factor, estrogen, xenoestrogen.
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42

Rainard, Pascal. "Binding of bovine lactoferrin toStreptococcus agalactiae." FEMS Microbiology Letters 98, no. 1-3 (November 1992): 235–39. http://dx.doi.org/10.1111/j.1574-6968.1992.tb05520.x.

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43

Wakabayashi, Hiroyuki, Koji Yamauchi, and Fumiaki Abe. "Quality control of commercial bovine lactoferrin." BioMetals 31, no. 3 (April 4, 2018): 313–19. http://dx.doi.org/10.1007/s10534-018-0098-2.

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44

Norris, G. E., B. F. Anderson, E. N. Baker, H. M. Baker, A. L. Gärtner, J. Ward, and S. V. Rumball. "Preliminary crystallographic studies on bovine lactoferrin." Journal of Molecular Biology 191, no. 1 (September 1986): 143–45. http://dx.doi.org/10.1016/0022-2836(86)90432-8.

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45

Hurley, W. "Bovine lactoferrin in involuting mammary tissue." Cell Biology International 17, no. 3 (March 1993): 283–90. http://dx.doi.org/10.1006/cbir.1993.1064.

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46

Shimamura, Mariko, Yukio Yamamoto, Hiromi Ashino, Tsutomu Oikawa, Tadahiko Hazato, Hiroyuki Tsuda, and Masaaki Iigo. "Bovine lactoferrin inhibits tumor-induced angiogenesis." International Journal of Cancer 111, no. 1 (2004): 111–16. http://dx.doi.org/10.1002/ijc.20187.

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47

Givens, M., M. Marley, P. Galik, K. Riddell, and D. Stringfellow. "211 LACTOFERRIN INHIBITS BOVINE HERPESVIRUS-1 IN CELL CULTURE AND ALLOWS NORMAL DEVELOPMENT OF IN VITRO-PRODUCED EMBRYOS." Reproduction, Fertility and Development 18, no. 2 (2006): 213. http://dx.doi.org/10.1071/rdv18n2ab211.

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Lactoferrin is an iron-binding glycoprotein found in milk, saliva, tears, and other exocrine secretions. It is known to have in vitro antiviral effects against human, feline, and canine herpesviruses. In addition, lactoferrin is known to be safe in cell culture. Bovine herpesvirus-1 (BHV-1) is a likely contaminant of in vitro embryo production. Further, trypsin treatment is not completely effective in removing the virus from these embryos. We hypothesized that a nontoxic concentration of lactoferrin might prevent replication of BHV-1 within in vitro embryo production systems. Thus, the specific objectives of this research were to determine if lactoferrin from bovine milk would inhibit BHV-1 in cell culture and to determine if in vitro-produced embryos could develop normally when cultured in lactoferrin. Two-fold dilutions of lactoferrin (from 10 to 0.625 mg/mL) were added to Madin Darby bovine kidney cells, followed in 15 min by the addition 104 PFU/mL of BHV-1 (Colorado strain). Samples of cell lysate were taken at Day 2 and virus was quantified by plaque assay. The percent of virus inhibited by the antiviral agent at each concentration was determined by comparison to equivalent samples from temporal control cultures in which no compound was added before or after inoculation (Percentage of virus inhibited = [Quantity of virus in the control sample - Quantity of virus in the compound sample]/Quantity of virus in the control sample � 100). Next, the effect of lactoferrin was determined on in vitro-produced embryos. Cumulus oocyte complexes were received from an abattoir, matured in transit, placed in fertilization drops for 6 h, and then placed in culture drops containing lactoferrin (10, 5, and 2.5 mg/mL). At Day 3.5, embryos > 4 cell stage were placed into fresh culture drops containing lactoferrin. On Day 7.5, blastocyst development was noted and the developed embryos were stained to count viable cells. Blastocyst development rate and nucleated cell count of the treated embryos were compared to those of the controls using Chi square test, and ANOVA and Tukey-Kramer HSD, respectively. Lactoferrin (10 mg/mL) inhibited 2 to 5 logs of virus. At concentrations of 5 and 2.5 mg/mL, 1 to 3 logs of virus were inhibited, and concentrations of 1.25 and 0.625 mg/mL inhibited 0 to 2 logs of virus. Lactoferrin did not affect the nucleated cell count of the treated embryos. In addition, unlike 10 and 5 mg/mL, 2.5 mg/mL of lactoferrin did not affect blastocyst development. These preliminary results indicate that lactoferrin from bovine milk can significantly inhibit BHV-1 in cell culture. Furthermore, supplementation of in vitro culture with 2.5 mg/mL of lactoferrin does not affect blastocyst development or cell count of in vitro-produced embryos.
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48

Kieckens, E., J. Rybarczyk, L. De Zutter, L. Duchateau, D. Vanrompay, and E. Cox. "Clearance of Escherichia coli O157:H7 Infection in Calves by Rectal Administration of Bovine Lactoferrin." Applied and Environmental Microbiology 81, no. 5 (December 19, 2014): 1644–51. http://dx.doi.org/10.1128/aem.03724-14.

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ABSTRACTEnterohemorrhagicEscherichia coli(EHEC) strains, of whichE. coliO157:H7 is the best-studied serotype, are an important group of foodborne pathogens causing severe illness in humans worldwide. The main reservoirs for EHEC are ruminants, mostly cattle, which harbor the bacteria in their intestinal tracts without showing clinical symptoms. In this study, we used bovine lactoferrin, a natural occurring bactericidal and immunomodulating protein, as an antibacterial agent against EHEC infection in cattle. Nine 3-month-old Holstein-Friesian calves were experimentally infected with EHEC (strain NCTC12900). Three animals received a daily rectal spray treatment with bovine lactoferrin, three animals received an oral treatment, and three animals served as a control group. Blood samples were collected weekly and fecal samples twice weekly to monitor antibody responses and fecal excretion, respectively. Animals in the rectal group ceased shedding within 26 days of the experimental treatment and remained negative. This beneficial effect of bovine lactoferrin was not observed in the oral group, where animals were still shedding at the time of euthanasia (day 61). All groups developed serum responses, but no clear differences could be observed between the groups. However, the results indicate that the use of bovine lactoferrin as a rectal treatment can be a useful strategy to preclude further transmission of EHEC infections from cattle to humans.
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49

Prgomet, Christian, Solveig Peters, and Michael W. Pfaffl. "Influence of bovine lactoferrin and lactoferricin on cytokine expression in LPS-treated cultivated bovine blood cells." Journal of the Science of Food and Agriculture 86, no. 4 (2006): 640–47. http://dx.doi.org/10.1002/jsfa.2377.

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50

Almehdar, Hussein A., Nawal Abd El-Baky, Ehab H. Mattar, Raed Albiheyri, Atif Bamagoos, Abdullah Aljaddawi, Vladimir N. Uversky, and Elrashdy M. Redwan. "Exploring the mechanisms by which camel lactoferrin can kill Salmonella enterica serovar typhimurium and Shigella sonnei." PeerJ 11 (January 30, 2023): e14809. http://dx.doi.org/10.7717/peerj.14809.

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There is a continuously increasing pressure associated with the appearance of Salmonella enterica Serovar typhimurium (S. typhimurium) and Shigella sonnei (S. sonnei) that have developed pathogenic multiple antibiotic resistance and the cost of cure and control of these enterobacteriaceae infections increases annually. The current report for first time demonstrated the distinguished antimicrobial action of camel lactoferrin (cLf) obtained from the milk of different clans of camel in Saudi Arabia against S. typhimurium and S. sonnei. These cLf subtypes showed comparable antimicrobial potential when tested against the two bacterial strains but were superior to either bovine (bLf) or human lactoferrin (hLf). The synergism between lactoferrins and antibiotics concerning their antibacterial efficacies against the two bacterial strains was evident. Exploring mechanisms by which camel lactoferrin can kill S. typhimurium and S. sonnei revealed that cLf affects bacterial protein profile. Besides, it interacts with bacterial lipopolysaccharides (LPS) and numerous membrane proteins of S. typhimurium and S. sonnei, with each bacterial strain possessing distinctive binding membrane proteins for lactoferrin. Furthermore, as evidenced by electron microscopy analysis, cLf induces extracellular and intracellular morphological changes in the test bacterial strains when used alone or in combination treatment with antibiotics. Lactoferrin and antibiotics combination strongly disrupts the integrity of the bacterial cells and their membranes. Therefore, cLf can kill S. typhimurium and S. sonnei by four different mechanisms, such as iron chelation, affecting some bacterial proteins, binding to bacterial LPS and membrane proteins, and impairing the integrity of the bacterial cells and their membranes.
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