Login Register Cart 0
Generic placeholder image

Current Pharmaceutical Design

Editor-in-Chief

ISSN (Print): 1381-6128
ISSN (Online): 1873-4286

Back
Journal Home About Journal Editorial Board Journal Insight Current Issue Volumes/Issues
Subscribe
Review Article

Novel Perspectives on Nanotechnological and Biomedical Implications of Monotherapy or Combination Regimen of Lactoferrin

Author(s): Kuo Chen, Jin Zhang, Narasimha M. Beeraka, Jialing Li, Mikhail Y. Sinelnikov, Xinliang Zhang, Yu Cao, Darya K. Zakharova, Vladimir N. Nikolenko, Igor V. Reshetov and Pengwei Lu*

Volume 29, Issue 20, 2023

Published on: 25 July, 2023

Page: [1579 - 1591] Pages: 13

DOI: 10.2174/1381612829666230622140926

Price: $65

Abstract

Lactoferrin (LF) is a protein molecule with a wide variety of physiological properties. LF has broadspectrum antibacterial, antiviral, antioxidant, and antitumor, and possesses immunomodulatory properties to regulate immunity and gastrointestinal function. The main aim of this review is to explore the recent investigations on the functional role of LF against several human disorders and diseases through monotherapy or combinatorial regimens with other biological/chemotherapeutic agents through novel nanoformulations. We significantly searched public databases such as Pubmed, National Library of Medicine, relemed, Scopus and collected published reports pertaining to these recent reports on lactoferrin as a monotherapy or combination therapy, and its nanoformulations. We have discussed vividly the role of LF as a growth factor with substantial potential that can promote cell growth and regeneration potential for repairing tissues such as bone, skin, mucosa, and tendons. In addition, we have discussed novel perspectives on the role of LF as an inductive factor for the proliferation of stem cells in tissue recovery and discussed its novel modulating effects in ameliorating cancer and microbial growth through several signaling cascades via monotherapy or combinatorial regimens. Furthermore, the regeneration potential of this protein is reviewed to explore the efficacy and prospects of new treatment methods. This review benefits various microbiologists, stem cell therapists, and oncologists to explore the efficacy of LF in several segments of medicine by examining its ability as a stem cell differentiation factor, and anticancer agent or antimicrobial agent through novel formulations in preclinical or clinical study.

« Previous Next »
[1]
Jacobsen LC, Sørensen OE, Cowland JB, Borregaard N, Theilgaard-Mönch K. The secretory leukocyte protease inhibitor (SLPI) and the secondary granule protein lactoferrin are synthesized in myelocytes, colocalize in subcellular fractions of neutrophils, and are coreleased by activated neutrophils. J Leukoc Biol 2008; 83(5): 1155-64.
[http://dx.doi.org/10.1189/jlb.0706442] [PMID: 18285402]
[2]
Sargent PJ, Farnaud S, Evans RW. Structure/function overview of proteins involved in iron storage and transport. Curr Med Chem 2005; 12(23): 2683-93.
[http://dx.doi.org/10.2174/092986705774462969] [PMID: 16305465]
[3]
García-Montoya IA, Cendón TS, Arévalo-Gallegos S, Rascón-Cruz Q. Lactoferrin a multiple bioactive protein: An overview. Biochim Biophys Acta, Gen Subj 2012; 1820(3): 226-36.
[http://dx.doi.org/10.1016/j.bbagen.2011.06.018]
[4]
González-Chávez SA, Arévalo-Gallegos S, Rascón-Cruz Q. Lactoferrin: structure, function and applications. Int J Antimicrob Agents 2009; 33(4): 301.e1-8.
[http://dx.doi.org/10.1016/j.ijantimicag.2008.07.020] [PMID: 18842395]
[5]
Shouldice SR, Skene RJ, Dougan DR, et al. Structural basis for iron binding and release by a novel class of periplasmic iron-binding proteins found in gram-negative pathogens. J Bacteriol 2004; 186(12): 3903-10.
[http://dx.doi.org/10.1128/JB.186.12.3903-3910.2004] [PMID: 15175304]
[6]
Baker EN, Baker HM. Lactoferrin. Cell Mol Life Sci 2005; 62(22): 2531-9.
[http://dx.doi.org/10.1007/s00018-005-5368-9] [PMID: 16261257]
[7]
Sharma S, Sinha M, Kaushik S, Kaur P, Singh TP. C-lobe of lactoferrin: the whole story of the half-molecule. Biochem Res Int 2013; 2013: 1-8.
[http://dx.doi.org/10.1155/2013/271641] [PMID: 23762557]
[8]
Baker E, Baker H. A structural framework for understanding the multifunctional character of lactoferrin. Biochimie 2009; 91(1): 3-10.
[http://dx.doi.org/10.1016/j.biochi.2008.05.006] [PMID: 18541155]
[9]
Mata L, Sánchez L, Headon DR, Calvo M. Thermal denaturation of human lactoferrin and its effect on the ability to bind iron. J Agric Food Chem 1998; 46(10): 3964-70.
[http://dx.doi.org/10.1021/jf980266d]
[10]
Pang X N, Hong X, Wei X, Chen X W, Liu J, Chen D F. Research progress in physicochemical characteristics of lactoferrin and its recombinant expression systems. Yi Chuan 2015; 37(9): 873-4.
[http://dx.doi.org/10.16288/j.yczz.15-146] [PMID: 26399527]
[11]
Amini AA, Nair LS. Lactoferrin: a biologically active molecule for bone regeneration. Curr Med Chem 2011; 18(8): 1220-9.
[http://dx.doi.org/10.2174/092986711795029744] [PMID: 21291364]
[12]
Icriverzi M, Dinca V, Moisei M, Evans RW, Trif M, Roseanu A. Lactoferrin in bone tissue regeneration. Curr Med Chem 2019; 27(6): 838-53.
[http://dx.doi.org/10.2174/0929867326666190503121546] [PMID: 31258057]
[13]
Shi P, Wang Q, Yu C, et al. Hydroxyapatite nanorod and microsphere functionalized with bioactive lactoferrin as a new biomaterial for enhancement bone regeneration. Colloids Surf B Biointerfaces 2017; 155: 477-86.
[http://dx.doi.org/10.1016/j.colsurfb.2017.04.042] [PMID: 28472751]
[14]
Montesi M, Panseri S, Iafisco M, Adamiano A, Tampieri A. Effect of hydroxyapatite nanocrystals functionalized with lactoferrin in osteogenic differentiation of mesenchymal stem cells. J Biomed Mater Res A 2015; 103(1): 224-34.
[http://dx.doi.org/10.1002/jbm.a.35170] [PMID: 24639083]
[15]
Bastos AR, da Silva LP, Maia FR, et al. Lactoferrin-hydroxyapatite containing spongy-like hydrogels for bone tissue engineering. Materials 2019; 12(13): 2074.
[http://dx.doi.org/10.3390/ma12132074] [PMID: 31252675]
[16]
Menghini L, Ferrante C, Leporini L, et al. A natural formula containing lactoferrin, Equisetum arvensis, soy isoflavones and vitamin D3 modulates bone remodeling and inflammatory markers in young and aged rats. J Biol Regul Homeost Agents 2016; 30(4): 985-6.
[PMID: 28078844]
[17]
Guo HY, Jiang L, Ibrahim SA, et al. Orally administered lactoferrin preserves bone mass and microarchitecture in ovariectomized rats. J Nutr 2009; 139(5): 958-64.
[http://dx.doi.org/10.3945/jn.108.100586] [PMID: 19321577]
[18]
Gao R, Watson M, Callon KE, et al. Local application of lactoferrin promotes bone regeneration in a rat critical-sized calvarial defect model as demonstrated by micro-CT and histological analysis. J Tissue Eng Regen Med 2018; 12(1): e620-6.
[http://dx.doi.org/10.1002/term.2348] [PMID: 27860377]
[19]
Yoshimaki T, Sato S, Tsunori K, et al. Bone regeneration with systemic administration of lactoferrin in non-critical-sized rat calvarial bone defects. J Oral Sci 2013; 55(4): 343-8.
[http://dx.doi.org/10.2334/josnusd.55.343] [PMID: 24351923]
[20]
Görmez U, Kürkcü M, E Benlidayi M, Ulubayram K, Sertdemir Y, Dağlioğlu K. Effects of bovine lactoferrin in surgically created bone defects on bone regeneration around implants. J Oral Sci 2015; 57(1): 7-15.
[http://dx.doi.org/10.2334/josnusd.57.7] [PMID: 25807903]
[21]
Eming SA, Koch M, Krieger A, et al. Differential proteomic analysis distinguishes tissue repair biomarker signatures in wound exudates obtained from normal healing and chronic wounds. J Proteome Res 2010; 9(9): 4758-66.
[http://dx.doi.org/10.1021/pr100456d] [PMID: 20666496]
[22]
Takayama Y, Aoki R. Roles of lactoferrin on skin wound healing 1 This article is part of Special Issue entitled Lactoferrin and has undergone the Journal’s usual peer review process. Biochem Cell Biol 2012; 90(3): 497-503.
[http://dx.doi.org/10.1139/o11-054] [PMID: 22332789]
[23]
Engelmayer J, Blezinger P, Varadhachary A. Talactoferrin stimulates wound healing with modulation of inflammation. J Surg Res 2008; 149(2): 278-86.
[http://dx.doi.org/10.1016/j.jss.2007.12.754] [PMID: 18619616]
[24]
Hewitt E, Mros S, Mcconnell M, Cabral J, Ali A. Melt-electrowriting with novel milk protein/PCL biomaterials for skin regeneration. Biomed Mater 2019; 14(5): 055013.
[http://dx.doi.org/10.1088/1748-605X/ab3344] [PMID: 31318339]
[25]
Jain R, Kim R, Waldvogel-Thurlow S, Hwang P, Cornish J, Douglas R. 2015; The effects of topical agents on paranasal sinus mucosa healing: A rabbit study. IntForum Allergy Rhinol 2015; 5(4): 310-7.
[http://dx.doi.org/10.1002/alr.21470]
[26]
Langhorst J, Boone J, Lauche R, Rueffer A, Dobos G. Faecal lactoferrin, calprotectin, PMN-elastase, CRP, and white blood cell count as indicators for mucosal healing and clinical course of disease in patients with mild to moderate ulcerative colitis: Post hoc analysis of a prospective clinical trial. J Crohn’s Colitis 2016; 10(7): 786-94.
[http://dx.doi.org/10.1093/ecco-jcc/jjw044] [PMID: 26874351]
[27]
Boon GJAM, Day AS, Mulder CJ, Gearry RB. Are faecal markers good indicators of mucosal healing in inflammatory bowel disease? World J Gastroenterol 2015; 21(40): 11469-80.
[http://dx.doi.org/10.3748/wjg.v21.i40.11469] [PMID: 26523111]
[28]
Lewis JD. The utility of biomarkers in the diagnosis and therapy of inflammatory bowel disease. Gastroenterology 2011; 140(6): 1817-26.e2.
[http://dx.doi.org/10.1053/j.gastro.2010.11.058] [PMID: 21530748]
[29]
Ibrahim Al-Mashahedah AM, Kanwar RK, Kanwar JR. Utility of nanomedicine targeting scar-forming myofibroblasts to attenuate corneal scarring and haze. Nanomedicine 2019; 14(8): 1049-72.
[http://dx.doi.org/10.2217/nnm-2017-0305] [PMID: 30901304]
[30]
Pattamatta U, Willcox M, Stapleton F, Garrett Q. Bovine lactoferrin promotes corneal wound healing and suppresses IL-1 expression in alkali wounded mouse cornea. Curr Eye Res 2013; 38(11): 1110-7.
[http://dx.doi.org/10.3109/02713683.2013.811259] [PMID: 23898919]
[31]
Pattamatta U, Willcox M, Stapleton F, Cole N, Garrett Q. Bovine lactoferrin stimulates human corneal epithelial alkali wound healing in vitro. Invest Ophthalmol Vis Sci 2009; 50(4): 1636-43.
[http://dx.doi.org/10.1167/iovs.08-1882] [PMID: 19060270]
[32]
Ashby B, Garrett Q, Willcox M. Bovine lactoferrin structures promoting corneal epithelial wound healing in vitro. Invest Ophthalmol Vis Sci 2011; 52(5): 2719-6.
[http://dx.doi.org/10.1167/iovs.10-6352] [PMID: 21282581]
[33]
Wiig M, Olmarker K, Håkansson J, Ekström L, Nilsson E, Mahlapuu M. A lactoferrin-derived peptide (PXL01) for the reduction of adhesion formation in flexor tendon surgery: an experimental study in rabbits. J Hand Surg Eur Vol 2011; 36(8): 656-62.
[http://dx.doi.org/10.1177/1753193411410823] [PMID: 21700648]
[34]
Edsfeldt S, Holm B, Mahlapuu M, Reno C, Hart DA, Wiig M. PXL01 in sodium hyaluronate results in increased PRG4 expression: A potential mechanism for anti-adhesion. Ups J Med Sci 2017; 122(1): 28-34.
[http://dx.doi.org/10.1080/03009734.2016.1230157] [PMID: 27658527]
[35]
Håkansson J, Mahlapuu M, Ekström L, Olmarker K, Wiig M. Effect of lactoferrin peptide (PXL01) on rabbit digit mobility after flexor tendon repair. J Hand Surg Am 2012; 37(12): 2519-.
[http://dx.doi.org/10.1016/j.jhsa.2012.09.019] [PMID: 23174064]
[36]
Wiig ME, Dahlin LB, Fridén J, et al. PXL01 in sodium hyaluronate for improvement of hand recovery after flexor tendon repair surgery: randomized controlled trial. PLoS One 2014; 9(10): e110735.
[http://dx.doi.org/10.1371/journal.pone.0110735] [PMID: 25340801]
[37]
Bae KS, Kim SY, Park SY, et al. Identification of lactoferrin as a human dedifferentiation factor through the studies of reptile tissue regeneration mechanisms. J Microbiol Biotechnol 2014; 24(6): 869-78.
[http://dx.doi.org/10.4014/jmb.1402.02009] [PMID: 24633229]
[38]
Taşlı PN, Şahin F. Effect of lactoferrin on odontogenic differentiation of stem cells derived from human 3rd molar tooth germ. Appl Biochem Biotechnol 2014; 174(6): 2257-66.
[http://dx.doi.org/10.1007/s12010-014-1204-8] [PMID: 25173676]
[39]
Wei L, Zhang X, Wang J, et al. Lactoferrin deficiency induces a pro-metastatic tumor microenvironment through recruiting myeloid-derived suppressor cells in mice. Oncogene 2020; 39(1): 122-35.
[http://dx.doi.org/10.1038/s41388-019-0970-8] [PMID: 31462711]
[40]
Arcella A, Oliva MA, Staffieri S, et al. In vitro and in vivo effect of human lactoferrin on glioblastoma growth. J Neurosurg 2015; 123(4): 1026-35.
[http://dx.doi.org/10.3171/2014.12.JNS14512] [PMID: 26186026]
[41]
Xu Y, Guo X, Tu L, et al. Lactoferrin-modified PEGylated liposomes loaded with doxorubicin for targeting delivery to hepatocellular carcinoma. Int J Nanomedicine 2015; 10: 5123-37.
[http://dx.doi.org/10.2147/IJN.S87011] [PMID: 26316745]
[42]
Deng M, Zhang W, Tang H, et al. Lactotransferrin acts as a tumor suppressor in nasopharyngeal carcinoma by repressing AKT through multiple mechanisms. Oncogene 2013; 32(36): 4273-83.
[http://dx.doi.org/10.1038/onc.2012.434] [PMID: 23069661]
[43]
Chea C, Miyauchi M, Inubushi T, et al. Bovine lactoferrin reverses programming of epithelial-to-mesenchymal transition to mesenchymal-to-epithelial transition in oral squamous cell carcinoma. Biochem Biophys Res Commun 2018; 507(1-4): 142-7.
[http://dx.doi.org/10.1016/j.bbrc.2018.10.193] [PMID: 30415774]
[44]
Tung YT, Chen HL, Yen CC, et al. Bovine lactoferrin inhibits lung cancer growth through suppression of both inflammation and expression of vascular endothelial growth factor. J Dairy Sci 2013; 96(4): 2095-106.
[http://dx.doi.org/10.3168/jds.2012-6153] [PMID: 23462173]
[45]
An J, Xu Y, Kong Z. Effect of lactoferrin and its digests on differentiation activities of bone mesenchymal stem cells. J Funct Foods 2019; 57: 202-10.
[http://dx.doi.org/10.1016/j.jff.2019.04.020]
[46]
Shi P, Fan F, Chen H, et al. A bovine lactoferrin–derived peptide induced osteogenesis via regulation of osteoblast proliferation and differentiation. J Dairy Sci 2020; 103(5): 3950-60.
[http://dx.doi.org/10.3168/jds.2019-17425] [PMID: 32197844]
[47]
Tingting S, Weihu Y, Xinkun S, et al. Polydopamine-assisted hydroxyapatite and lactoferrin multilayer on titanium for regulating bone balance and enhancing antibacterial property. ACS Biomater Sci Eng 2018; 4(9): 3211-23.
[http://dx.doi.org/10.1021/acsbiomaterials.8b00791]
[48]
Fan F, Shi P, Liu M, et al. Lactoferrin preserves bone homeostasis by regulating the RANKL/RANK/OPG pathway of osteoimmunology. Food Funct 2018; 9(5): 2653-60.
[http://dx.doi.org/10.1039/C8FO00303C] [PMID: 29666861]
[49]
Rusen L, Brajnicov S, Neacsu P, et al. Novel degradable biointerfacing nanocomposite coatings for modulating the osteoblast response. Surf Coat Technol 2017; 325: 397-409.
[http://dx.doi.org/10.1016/j.surfcoat.2017.06.045]
[50]
Elena S, Traian Z, Elena GH, et al. Lactoferrin-immobilized surfaces onto functionalized PLA assisted by the gamma-rays and nitrogen plasma to create materials with multifunctional properties. ACS Appl Mater Interfaces 2016; 8(46): 31902-15.
[http://dx.doi.org/10.1021/acsami.6b09069]
[51]
Li W, Zhu S, Hu J. Bone regeneration is promoted by orally administered bovine lactoferrin in a rabbit tibial distraction osteogenesis model. Clin Orthop Relat Res 2015; 473(7): 2383-93.
[http://dx.doi.org/10.1007/s11999-015-4270-5] [PMID: 25822454]
[52]
Vandrovcova M, Douglas TEL, Heinemann S, Scharnweber D, Dubruel P, Bacakova L. Collagen-lactoferrin fibrillar coatings enhance osteoblast proliferation and differentiation. J Biomed Mater Res A 2015; 103(2): 525-33.
[http://dx.doi.org/10.1002/jbm.a.35199] [PMID: 24737729]
[53]
James EN, Nair LS. Development and characterization of lactoferrin loaded poly(epsilon-caprolactone) nanofibers. J Biomed Nanotechnol 2014; 10(3): 500-7.
[http://dx.doi.org/10.1166/jbn.2014.1717] [PMID: 24730245]
[54]
Amini AA, Nair LS. Recombinant human lactoferrin as a biomaterial for bone tissue engineering: Mechanism of antiapoptotic and osteogenic activity. Adv Healthc Mater 2014; 3(6): 897-905.
[http://dx.doi.org/10.1002/adhm.201300496] [PMID: 24352833]
[55]
Kawazoe A, Inubushi T, Miyauchi M, et al. Orally administered liposomal lactoferrin inhibits inflammation-related bone breakdown without interrupting orthodontic tooth movement. J Periodontol 2013; 84(10): 1454-62.
[http://dx.doi.org/10.1902/jop.2012.120508] [PMID: 23136974]
[56]
Takaoka R, Hikasa Y, Hayashi K, Tabata Y. Bone regeneration by lactoferrin released from a gelatin hydrogel. J Biomater Sci Polym Ed 2011; 22(12): 1581-9.
[http://dx.doi.org/10.1163/092050610X517095] [PMID: 20663279]
[57]
Rasika M. The effect of oral administration of iron saturated-bovine lactoferrin encapsulated chitosan-nanocarriers on osteoarthritis. Biomaterials 2014; 35(26): 7522-34.
[http://dx.doi.org/10.1016/j.biomaterials.2014.04.109]
[58]
Tu Y, Huaming X, Wendy F, et al. Lactoferrin inhibits dexamethasone-induced chondrocyte impairment from osteoarthritic cartilage through up-regulation of extracellular signal-regulated kinase 1/2 and suppression of FASL, FAS, and Caspase 3. Biochem Biophys Res Commun 2013; 441(1): 249-55.
[http://dx.doi.org/10.1016/j.bbrc.2013.10.047]
[59]
Kim JS, Ellman MB, Yan D, et al. Lactoferricin mediates anti-inflammatory and anti-catabolic effects via inhibition of IL-1 and LPS activity in the intervertebral disc. J Cell Physiol 2013; 228(9): 1884-96.
[http://dx.doi.org/10.1002/jcp.24350] [PMID: 23460134]
[60]
Yan D, Chen D, Shen J, Xiao G, van Wijnen AJ, Im HJ. Bovine lactoferricin is anti-inflammatory and anti-catabolic in human articular cartilage and synovium. J Cell Physiol 2013; 228(2): 447-56.
[http://dx.doi.org/10.1002/jcp.24151] [PMID: 22740381]
[61]
Inubushi T, Kawazoe A, Miyauchi M, et al. Molecular mechanisms of the inhibitory effects of bovine lactoferrin on lipopolysaccharide-mediated osteoclastogenesis. J Biol Chem 2012; 287(28): 23527-36.
[http://dx.doi.org/10.1074/jbc.M111.324673] [PMID: 22593578]
[62]
Cornish J, Naot D. Lactoferrin as an effector molecule in the skeleton. Biometals 2010; 23(3): 425-30.
[http://dx.doi.org/10.1007/s10534-010-9320-6] [PMID: 20232111]
[63]
Brandl N, Zemann A, Kaupe I, et al. Signal transduction and metabolism in chondrocytes is modulated by lactoferrin. Osteoarthritis Cartilage 2010; 18(1): 117-25.
[http://dx.doi.org/10.1016/j.joca.2009.08.012] [PMID: 19747587]
[64]
Huang HC, Lin H, Huang MC. Lactoferrin promotes hair growth in mice and increases dermal papilla cell proliferation through Erk/Akt and Wnt signaling pathways. Arch Dermatol Res 2019; 311(5): 411-20.
[http://dx.doi.org/10.1007/s00403-019-01920-1] [PMID: 31006055]
[65]
Jiang R, Suzuki YA, Du X, Lönnerdal B. Lactoferrin and the lactoferrin–sophorolipids-assembly can be internalized by dermal fibroblasts and regulate gene expression. Biochem Cell Biol 2017; 95(1): 110-8.
[http://dx.doi.org/10.1139/bcb-2016-0090] [PMID: 28169552]
[66]
Takayama Y. Effects of lactoferrin on skin wound healing. Lactoferrin and its role in wound healing. Dordrecht: Springer 2012.
[http://dx.doi.org/10.1007/978-94-007-2467-9]
[67]
Tang L, Wu JJ, Ma Q, et al. Human lactoferrin stimulates skin keratinocyte function and wound re-epithelialization. Br J Dermato 2010; 163(1): 38-47.
[http://dx.doi.org/10.1111/j.1365-2133.2010.09748.x] [PMID: 20222924]
[68]
Tang L, Cui T, Wu JJ, Liu-Mares W, Huang N, Li J. A rice-derived recombinant human lactoferrin stimulates fibroblast proliferation, migration, and sustains cell survival. Wound Repair Regen 2010; 18(1): 123-31.
[http://dx.doi.org/10.1111/j.1524-475X.2009.00563.x] [PMID: 20082685]
[69]
Nadolska B, Frączek M, Kręcicki T, Kocięba M, Zimecki M. Lactoferrin inhibits the growth of nasal polyp fibroblasts. Pharmacol Rep 2010; 62(6): 1139-47.
[http://dx.doi.org/10.1016/S1734-1140(10)70376-5] [PMID: 21273671]
[70]
Liu J, Zhu H, Li B, et al. Lactoferrin reduces necrotizing enterocolitis severity by upregulating intestinal epithelial proliferation. Eur J Pediatr Surg 2020; 30(1): 090-95.
[http://dx.doi.org/10.1055/s-0039-1693728] [PMID: 31344710]
[71]
Zhao X, Xu XX, Liu Y, et al. The in vitro protective role of bovine lactoferrin on intestinal epithelial barrier. Molecules 2019; 24(1): 148.
[http://dx.doi.org/10.3390/molecules24010148] [PMID: 30609730]
[72]
Hering NA, Luettig J, Krug SM, et al. Lactoferrin protects against intestinal inflammation and bacteria-induced barrier dysfunction in vitro. Ann N Y Acad Sci 2017; 1405(1): 177-88.
[http://dx.doi.org/10.1111/nyas.13405] [PMID: 28614589]
[73]
Nirwana I, Indra S, Meircurius DCS. Role of lactoferrinin fibroblast growth factor 2 and vascular endothelial growth factor in gingival wounds. J Krishna Inst Medical Sci Univ 2019; 8(3): 38-45.
[74]
Mancinelli R, Olivero F, Carpino G, et al. Role of lactoferrin and its receptors on biliary epithelium. Biometals 2018; 31(3): 369-79.
[http://dx.doi.org/10.1007/s10534-018-0094-6] [PMID: 29550924]
[75]
Nguyen DN, Jiang P, Stensballe A, Bendixen E, Sangild PT, Chatterton DEW. Bovine lactoferrin regulates cell survival, apoptosis and inflammation in intestinal epithelial cells and preterm pig intestine. J Proteomics 2016; 139: 95-102.
[http://dx.doi.org/10.1016/j.jprot.2016.03.020]
[76]
Blais A, Fan C, Voisin T, et al. Effects of lactoferrin on intestinal epithelial cell growth and differentiation: An in vivo and in vitro study. Biometals 2014; 27(5): 857-74.
[http://dx.doi.org/10.1007/s10534-014-9779-7] [PMID: 25082351]
[77]
Jiang R, Lönnerdal B. Transcriptomic profiling of intestinal epithelial cells in response to human, bovine and commercial bovine lactoferrins. Biometals 2014; 27(5): 831-41.
[http://dx.doi.org/10.1007/s10534-014-9746-3] [PMID: 24831230]
[78]
Reznikov EA, Comstock SS, Yi C, Contractor N, Donovan SM. Dietary bovine lactoferrin increases intestinal cell proliferation in neonatal piglets. J Nutr 2014; 144(9): 1401-8.
[http://dx.doi.org/10.3945/jn.114.196568] [PMID: 25056692]
[79]
Zernii EY, Baksheeva VE, Yani EV, Philippov PP, Senin II. Therapeutic proteins for treatment of corneal epithelial defects. Curr Med Chem 2019; 26(3): 517-45.
[http://dx.doi.org/10.2174/0929867324666170609080920] [PMID: 28595546]
[80]
Hirayama M, Ko SB, Kawakita T, et al. Identification of transcription factors that promote the differentiation of human pluripotent stem cells into lacrimal gland epithelium-like cells. NPJ Aging Mech Dis 2017; 3(1): 1.
[http://dx.doi.org/10.1038/s41514-016-0001-8]
[81]
Uchida R, Aoki R, Aoki-Yoshida A, Tajima A, Takayama Y. Promoting effect of lactoferrin on barrier function and epithelial differentiation of human keratinocytes. Biochem Cell Biol 2017; 95(1): 64-8.
[http://dx.doi.org/10.1139/bcb-2016-0147] [PMID: 28165292]
[82]
Raghothama C, Hanjuan S, ASherri-Gae S, et al. The keratoconus corneal proteome: Loss of epithelial integrity and stromal degeneration. J Proteomics 2013; 87: 122-31.
[http://dx.doi.org/10.1016/j.jprot.2013.05.023] [PMID: 23727491]
[83]
Musson David S, Tay ML, Chhana A, et al. Lactoferrin and parathyroid hormone are not harmful to primary tenocytes in vitro, but PDGF may be. Muscles Ligaments Tendons J 2017; 7(2): 215-2.
[http://dx.doi.org/10.11138/mltj/2017.7.2.215] [PMID: 29264331]
[84]
Pajovich HT, Brown AM, Smith AM, et al. Development of multilayered chlorogenate-peptide based biocomposite scaffolds for potential applications in ligament tissue engineering - an in vitro study. J Biomim Biomater Biomed Eng 2017; 34: 37-56.
[http://dx.doi.org/10.4028/www.scientific.net/JBBBE.34.37]
[85]
Zhang Y, Wang X, Qiu Y, Cornish J, Carr AJ, Xia Z. Effect of indomethacin and lactoferrin on human tenocyte proliferation and collagen formation in vitro. Biochem Biophys Res Commun 2014; 454(2): 301-7.
[http://dx.doi.org/10.1016/j.bbrc.2014.10.061] [PMID: 25450393]
[86]
Sakai M, Matsushita T, Hoshino R, Ono H, Ikai K, Sakai T. Identification of the protective mechanisms of lactoferrin in the irradiated salivary gland. Sci Rep 2017; 7(1): 9753.
[http://dx.doi.org/10.1038/s41598-017-10351-9] [PMID: 28852132]
[87]
Park SY, Jeong AJ, Kim GY, et al. Lactoferrin protects human mesenchymal stem cells from oxidative stress-induced senescence and apoptosis. J Microbiol Biotechnol 2017; 27(10): 1877-84.
[http://dx.doi.org/10.4014/jmb.1707.07040] [PMID: 28870012]
[88]
Icriverzi M, Bonciu A, Rusen L, et al. Human mesenchymal stem cell response to lactoferrin-based composite coatings. Materials 2019; 12(20): 3414.
[http://dx.doi.org/10.3390/ma12203414] [PMID: 31635291]
[89]
Kim SE, Lee DW, Yun YP, et al. Heparin-immobilized hydroxyapatite nanoparticles as a lactoferrin delivery system for improving osteogenic differentiation of adipose-derived stem cells. Biomed Mater 2016; 11(2): 025004.
[http://dx.doi.org/10.1088/1748-6041/11/2/025004] [PMID: 26963891]
[90]
Chen Y, Zheng Z, Zhu X, et al. Lactoferrin promotes early neurodevelopment and cognition in postnatal piglets by upregulating the bdnf signaling pathway and polysialylation. Mol Neurobiol 2015; 52(1): 256-69.
[http://dx.doi.org/10.1007/s12035-014-8856-9] [PMID: 25146846]
[91]
Nakajima K, Itoh F, Nakamura M, et al. Short communication: Opposing effects of lactoferrin on the proliferation of fibroblasts and epithelial cells from bovine mammary gland. J Dairy Sci 2015; 98(2): 1069-77.
[http://dx.doi.org/10.3168/jds.2014-8430] [PMID: 25497822]
[92]
Ying X, Cheng S, Wang W, et al. Effect of lactoferrin on osteogenic differentiation of human adipose stem cells. Int Orthop 2012; 36(3): 647-53.
[http://dx.doi.org/10.1007/s00264-011-1303-x] [PMID: 21713451]
[93]
Moreno-Navarrete JM, Ortega F, Sabater M, Ricart W, Fernández-Real JM. Proadipogenic effects of lactoferrin in human subcutaneous and visceral preadipocytes. J Nutr Biochem 2011; 22(12): 1143-9.
[http://dx.doi.org/10.1016/j.jnutbio.2010.09.015] [PMID: 21295959]
[94]
Moreno-Navarrete JM, Ortega FJ, Ricart W, Fernandez-Real JM. Lactoferrin increases 172ThrAMPK phosphorylation and insulin-induced p473SerAKT while impairing adipocyte differentiation. Int J Obes 2009; 33(9): 991-1000.
[http://dx.doi.org/10.1038/ijo.2009.143] [PMID: 19652659]
[95]
Yeom M, Park J, Lee B, et al. Lactoferrin inhibits the inflammatory and angiogenic activation of bovine aortic endothelial cells. Inflamm Res 2011; 60(5): 475-82.
[http://dx.doi.org/10.1007/s00011-010-0294-1] [PMID: 21161563]
[96]
Karav Sercan, German BJ, Camille R, et al. Studying lactoferrin N-glycosylation. Int J Mol Sci 2017; 18(4): 870.
[http://dx.doi.org/10.3390/ijms18040870] [PMID: 28425960]
[97]
Teraguchi S, Wakabayashi H, Kuwata H, Yamauchi K, Tamura Y. Protection against infections by oral lactoferrin: Evaluation in animal models. Biometals 2004; 17(3): 231-4.
[http://dx.doi.org/10.1023/B:BIOM.0000027697.83706.32] [PMID: 15222470]
[98]
Kuhara T, Iigo M, Itoh T, et al. Orally administered lactoferrin exerts an antimetastatic effect and enhances production of IL-18 in the intestinal epithelium. Nutr Cancer 2000; 38(2): 192-9.
[http://dx.doi.org/10.1207/S15327914NC382_8] [PMID: 11525597]
[99]
Wakabayashi H, Takakura N, Yamauchi K, et al. Effect of lactoferrin feeding on the host antifungal response in guinea-pigs infected or immunised with Trichophyton mentagrophytes. J Med Microbiol 2002; 51(10): 844-50.
[http://dx.doi.org/10.1099/0022-1317-51-10-844] [PMID: 12435063]
[100]
Yamauchi K, Wakabayashi H, Shin K, Takase M. Bovine lactoferrin: Benefits and mechanism of action against infections. Biochem Cell Biol 2006; 84(3): 291-6.
[http://dx.doi.org/10.1139/o06-054] [PMID: 16936799]
[101]
Di Mario F, Aragona G, Dal Bò N, et al. Use of bovine lactoferrin for helicobacter pylori eradication. Dig Liver Dis 2003; 35(10): 706-10.
[http://dx.doi.org/10.1016/S1590-8658(03)00409-2] [PMID: 14620619]
[102]
Iwasa M, Kaito M, Ikoma J, et al. Lactoferrin inhibits hepatitis C virus viremia in chronic hepatitis C patients with high viral loads and HCV genotype 1b. Am J Gastroenterol 2002; 97(3): 766-67.
[http://dx.doi.org/10.1111/j.1572-0241.2002.05573.x] [PMID: 11922584]
[103]
Tanaka K, Ikeda M, Nozaki A, et al. Lactoferrin inhibits hepatitis C virus viremia in patients with chronic hepatitis C: A pilot study. Jpn J Cancer Res 1999; 90(4): 367-71.
[http://dx.doi.org/10.1111/j.1349-7006.1999.tb00756.x] [PMID: 10363572]
[104]
Wada T, Aiba Y, Shimizu K, Takagi A, Miwa T, Koga Y. The therapeutic effect of bovine lactoferrin in the host infected with Helicobacter pylori. Scand J Gastroenterol 1999; 34(3): 238-43.
[http://dx.doi.org/10.1080/00365529950173627] [PMID: 10232866]
[105]
Wang X, Hirmo S, Willén R, Wadström T. Inhibition of helicobacter pylori infection by bovine milk glycoconjugates in a BALB/cA mouse model. J Med Microbiol 2001; 50(5): 430-5.
[http://dx.doi.org/10.1099/0022-1317-50-5-430] [PMID: 11339250]
[106]
Yamauchi K, Hiruma M, Yamazaki N, et al. Oral administration of bovine lactoferrin for treatment of tinea pedis. A placebo-controlled, double-blind study. Mycoses 2000; 43(5): 197-202.
[http://dx.doi.org/10.1046/j.1439-0507.2000.00571.x] [PMID: 10948819]
[107]
Wakabayashi H, Oda H, Yamauchi K, Abe F. Lactoferrin for prevention of common viral infections. J Infect Chemother 2014; 20(11): 666-71.
[http://dx.doi.org/10.1016/j.jiac.2014.08.003] [PMID: 25182867]
[108]
Shin K, Wakabayashi H, Yamauchi K, et al. Effects of orally administered bovine lactoferrin and lactoperoxidase on influenza virus infection in mice. J Med Microbiol 2005; 54(8): 717-23.
[http://dx.doi.org/10.1099/jmm.0.46018-0] [PMID: 16014423]
[109]
Egashira M, Takayanagi T, Moriuchi M, Moriuchi H. Does daily intake of bovine lactoferrin-containing products ameliorate rotaviral gastroenteritis? Acta Paediatr 2007; 96(8): 1242-4.
[http://dx.doi.org/10.1111/j.1651-2227.2007.00393.x] [PMID: 17655624]
[110]
Kuhara T, Yamauchi K, Tamura Y, Okamura H. Oral administration of lactoferrin increases NK cell activity in mice via increased production of IL-18 and type I IFN in the small intestine. J Interferon Cytokine Res 2006; 26(7): 489-99.
[http://dx.doi.org/10.1089/jir.2006.26.489] [PMID: 16800788]
[111]
Arnold RR, Brewer M, Gauthier JJ. Bactericidal activity of human lactoferrin: Sensitivity of a variety of microorganisms. Infect Immun 1980; 28(3): 893-.
[http://dx.doi.org/10.1128/iai.28.3.893-898.1980] [PMID: 6772569]
[112]
Kalmar JR, Arnold RR. Killing of Actinobacillus actinomycetemcomitans by human lactoferrin. Infect Immun 1988; 56(10): 2552-7.
[http://dx.doi.org/10.1128/iai.56.10.2552-2557.1988] [PMID: 3417349]
[113]
Yamauchi K, Tomita M, Giehl TJ, Ellison RT III. Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect Immun 1993; 61(2): 719-28.
[http://dx.doi.org/10.1128/iai.61.2.719-728.1993] [PMID: 8423097]
[114]
Ellison RT III, Giehl TJ, LaForce FM. Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin. Infect Immun 1988; 56(11): 2774-81.
[http://dx.doi.org/10.1128/iai.56.11.2774-2781.1988] [PMID: 3169987]
[115]
Ellison RT III, LaForce FM, Giehl TJ, Boose DS, Dunn BE. Lactoferrin and transferrin damage of the Gram-negative outer membrane is modulated by Ca2+ and Mg2+. J Gen Microbiol 1990; 136(7): 1437-46.
[http://dx.doi.org/10.1099/00221287-136-7-1437] [PMID: 2230724]
[116]
Leitch EC, Willcox MDP. Elucidation of the antistaphylococcal action of lactoferrin and lysozyme. J Med Microbiol 1999; 48(9): 867-71.
[http://dx.doi.org/10.1099/00222615-48-9-867] [PMID: 10482299]
[117]
Zimecki M, Artym J, Kocieba M, Weber-Dabrowska B, Lusiak-Szelachowska M, Górski A. The concerted action of lactoferrin and bacteriophages in the clearance of bacteria in sublethally infected mice. Postepy Hig Med Dosw 2008; 62: 42-6.
[PMID: 18268472]
[118]
Weber-Dabrowska B, Zimecki M, Kruzel M, Kochanowska I, Lusiak-Szelachowska M. Alternative therapies in antibiotic-resistant infection. Adv Med Sci 2006; 51: 242-4.
[PMID: 17357317]
[119]
Qiu J, Hendrixson DR, Baker EN, Murphy TF, Geme JWS III, Plaut AG. Human milk lactoferrin inactivates two putative colonization factors expressed by Haemophilus influenzae. Proc Natl Acad Sci 1998; 95(21): 12641-6.
[http://dx.doi.org/10.1073/pnas.95.21.12641] [PMID: 9770539]
[120]
Ochoa TJ, Clearly TG. Lactoferrin disruption of bacterial type III secretion systems. Biometals 2004; 17(3): 257-60.
[http://dx.doi.org/10.1023/B:BIOM.0000027701.12965.d4] [PMID: 15222474]
[121]
Ochoa TJ, Noguera-Obenza M, Cleary TG. Lactoferrin blocks the initial host cell attachment mechanism of enteropathogenic E. coli (EPEC). Adv Exp Med Biol 2004; 554: 463-6.
[http://dx.doi.org/10.1007/978-1-4757-4242-8_65] [PMID: 15384625]
[122]
Ochoa TJ, Noguera-Obenza M, Ebel F, Guzman CA, Gomez HF, Cleary TG. Lactoferrin impairs type III secretory system function in enteropathogenic Escherichia coli. Infect Immun 2003; 71(9): 5149-5.
[http://dx.doi.org/10.1128/IAI.71.9.5149-5155.2003] [PMID: 12933858]
[123]
Oppenheim FG, Xu T, McMillian FM, et al. Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. J Biol Chem 1988; 263(16): 7472-.
[http://dx.doi.org/10.1016/S0021-9258(18)68522-9] [PMID: 3286634]
[124]
Pollock JJ, Denepitiya L, MacKay BJ, Iacono VJ. Fungistatic and fungicidal activity of human parotid salivary histidine-rich polypeptides on Candida albicans. Infect Immun 1984; 44(3): 702-.
[http://dx.doi.org/10.1128/iai.44.3.702-707.1984] [PMID: 6373615]
[125]
Wakabayashi H, Abe S, Okutomi T, Tansho S, Kawase K, Yamaguchi H. Cooperative anti-Candida effects of lactoferrin or its peptides in combination with azole antifungal agents. Microbiol Immunol 1996; 40(11): 821-5.
[http://dx.doi.org/10.1111/j.1348-0421.1996.tb01147.x] [PMID: 8985937]
[126]
Xu YY, Samaranayake YH, Samaranayake LP, Nikawa H. In vitro susceptibility of Candida species to lactoferrin. Med Mycol 1999; 37(1): 35-41.
[http://dx.doi.org/10.1080/02681219980000051] [PMID: 10200932]
[127]
Valenti P, Visca P, Antonini G, Orsi N. Antifungal activity of ovotransferrin towards genus candida. Mycopathologia 1985; 89(3): 169-75.
[http://dx.doi.org/10.1007/BF00447027] [PMID: 2985999]
[128]
Kuipers ME, de Vries HG, Eikelboom MC, Meijer DKF, Swart PJ. Synergistic fungistatic effects of lactoferrin in combination with antifungal drugs against clinical Candida isolates. Antimicrob Agents Chemother 1999; 43(11): 2635-41.
[http://dx.doi.org/10.1128/AAC.43.11.2635] [PMID: 10543740]
[129]
León-Sicairos N, Ordaz-Pichardo C, Carrero JC. Lactoferrin in the battle against intestinal parasites: A review. In: Hanem K, Govindarajan M, Giovanni B, Eds. Natural Remedies in the Fight against Parasites. (1st ed.). InTech 2017; pp. 155-82.
[http://dx.doi.org/10.5772/66819]
[130]
Ochoa TJ, Chea-Woo E, Campos M, et al. Impact of lactoferrin supplementation on growth and prevalence of Giardia colonization in children. Clin Infect Dis 2008; 46(12): 1881-3.
[http://dx.doi.org/10.1086/588476] [PMID: 18462105]
[131]
Tanaka T, Omata Y, Saito A, et al. Toxoplasma gondii: Parasiticidal effects of bovine lactoferricin against parasites. Exp Parasitol 1995; 81(4): 614-7.
[http://dx.doi.org/10.1006/expr.1995.1157] [PMID: 8543005]
[132]
Alimi D, Hajaji S, Rekik M, Abidi A, Gharbi M, Akkari H. First report of the in vitro nematicidal effects of camel milk. Vet Parasitol 2016; 228: 153-9.
[http://dx.doi.org/10.1016/j.vetpar.2016.09.003] [PMID: 27692318]
[133]
Baveye S, Elass E, Mazurier J, Spik G, Legrand D. Lactoferrin: A multifunctional glycoprotein involved in the modulation of the inflammatory process. Clin Chem Lab Med 1999; 37(3): 281-6.
[http://dx.doi.org/10.1515/CCLM.1999.049] [PMID: 10353473]
[134]
Kijlstra A, Jeurissen SH. Modulation of classical C3 convertase of complement by tear lactoferrin. Immunology 1982; 47(2): 263-70.
[PMID: 6922088]
[135]
Crouch SP, Slater KJ, Fletcher J. Regulation of cytokine release from mononuclear cells by the iron-binding protein lactoferrin. Blood 1992; 80(1): 235-40.
[http://dx.doi.org/10.1182/blood.V80.1.235.235] [PMID: 1535239]
[136]
Mattsby-Baltzer I, Roseanu A, Motas C, Elverfors J, Engberg I, Hanson LÅ. Lactoferrin or a fragment thereof inhibits the endotoxin-induced interleukin-6 response in human monocytic cells. Pediatr Res 1996; 40(2): 257-62.
[http://dx.doi.org/10.1203/00006450-199608000-00011] [PMID: 8827774]
[137]
Machnicki M, Zimecki M, Zagulski T. Lactoferrin regulates the release of tumour necrosis factor alpha and interleukin 6 in vivo. Int J Exp Pathol 1993; 74(5): 433-9.
[PMID: 8217778]
[138]
Zagulski T, Lipiński P, Zagulska A, Broniek S, Jarzabek Z. Lactoferrin can protect mice against a lethal dose of Escherichia coli in experimental infection in vivo. Br J Exp Pathol 1989; 70(6): 697-704.
[PMID: 2690922]
[139]
Britigan BE, Serody JS, Cohen MS. The role of lactoferrin as an anti-inflammatory molecule. Adv Exp Med Biol 1994; 357: 143-56.
[http://dx.doi.org/10.1007/978-1-4615-2548-6_14] [PMID: 7762426]
[140]
Zucali JR, Broxmeyer HE, Levy D, Morse C. Lactoferrin decreases monocyte-induced fibroblast production of myeloid colony-stimulating activity by suppressing monocyte release of interleukin-1. Blood 1989; 74(5): 1531-6.
[http://dx.doi.org/10.1182/blood.V74.5.1531.1531] [PMID: 2676016]
[141]
Mazurier J, Legrand D, Hu W, Montreuil J, Spik G. Expression of human lactotransferrin receptors in phytohemagglutinin-stimulated human peripheral blood lymphocytes. Isolation of the receptors by antiligand-affinity chromatography. Eur J Biochem 1989; 179(2): 481-7.
[http://dx.doi.org/10.1111/j.1432-1033.1989.tb14578.x] [PMID: 2537213]
[142]
Zimecki M, Mazurier J, Machnicki M, Wieczorek Z, Montreuil J, Spik G. Immunostimulatory activity of lactotransferrin and maturation of CD4− CD8− murine thymocytes. Immunol Lett 1991; 30(1): 119-23.
[http://dx.doi.org/10.1016/0165-2478(91)90099-V] [PMID: 1683650]
[143]
Duthille I, Masson M, Spik G, Mazurier J. Lactoferrin stimulates the mitogen-activated protein kinase in the human lymphoblastic T Jurkat cell line. Adv Exp Med Biol 1998; 443: 257-60.
[http://dx.doi.org/10.1007/978-1-4757-9068-9_31] [PMID: 9781367]
[144]
Cutone A, Rosa L, Ianiro G, et al. Lactoferrin’s anti-cancer properties: Safety, selectivity, and wide range of action. Biomolecules 2020; 10(3): 456.
[http://dx.doi.org/10.3390/biom10030456] [PMID: 32183434]

Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy