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Human Lactoferrin (human + lactoferrin)
Selected AbstractsRecombinant Human Lactoferrin is Effective in the Treatment of Helicobacter felis -infected MiceJOURNAL OF PHARMACY AND PHARMACOLOGY: AN INTERNATI ONAL JOURNAL OF PHARMACEUTICAL SCIENCE, Issue 12 2000E. J. DIAL Recombinant human lactoferrin possesses in-vitro antibiotic and anti-inflammatory activity similar to the native form. It was tested for in-vivo activity in mice infected with the gastritis-inducing bacterium Helicobacter felis. A two-week course of treatment with lactoferrin was sufficient to partially reverse both infection-induced gastritis and the infection rate, and fully reverse gastric surface hydro-phobicity changes. A comparison of lactoferrin with amoxicillin and standard triple therapy revealed no differences in infection rate. These results show that recombinant human lactoferrin is effective in a mouse model of Helicobacter infection, and support further testing of this promising agent for this application. [source] Human lactoferrin activates NF-,B through the Toll-like receptor 4 pathway while it interferes with the lipopolysaccharide-stimulated TLR4 signalingFEBS JOURNAL, Issue 9 2010Ken Ando Lactoferrin (LF) has been implicated in innate immunity. Here we reveal the signal transduction pathway responsible for human LF (hLF)-triggered nuclear factor-,B (NF-,B) activation. Endotoxin-depleted hLF induces NF-,B activation at physiologically relevant concentrations in the human monocytic leukemia cell line, THP-1, and in mouse embryonic fibroblasts (MEFs). In MEFs, in which both tumor necrosis factor receptor-associated factor 2 (TRAF2) and TRAF5 are deficient, hLF causes NF-,B activation at a level comparable to that seen in wild-type MEFs, whereas TRAF6-deficient MEFs show significantly impaired NF-,B activation in response to hLF. TRAF6 is known to be indispensable in leading to NF-,B activation in myeloid differentiating factor 88 (MyD88)-dependent signaling pathways, while the role of TRAF6 in the MyD88-independent signaling pathway has not been clarified extensively. When we examined the hLF-dependent NF-,B activation in MyD88-deficient MEFs, delayed, but remarkable, NF-,B activation occurred as a result of the treatment of cells with hLF, indicating that both MyD88-dependent and MyD88-independent pathways are involved. Indeed, hLF fails to activate NF-,B in MEFs lacking Toll-like receptor 4 (TLR4), a unique TLR group member that triggers both MyD88-depependent and MyD88-independent signalings. Importantly, the carbohydrate chains from hLF are shown to be responsible for TLR4 activation. Furthermore, we show that lipopolysaccharide-induced cytokine and chemokine production is attenuated by intact hLF but not by the carbohydrate chains from hLF. Thus, we present a novel model concerning the biological function of hLF: hLF induces moderate activation of TLR4-mediated innate immunity through its carbohydrate chains; however, hLF suppresses endotoxemia by interfering with lipopolysaccharide-dependent TLR4 activation, probably through its polypeptide moiety. [source] Human lactoferrin stimulates skin keratinocyte function and wound re-epithelializationBRITISH JOURNAL OF DERMATOLOGY, Issue 1 2010L. Tang Summary Background, Human lactoferrin (hLF), a member of the transferrin family, is known for its antimicrobial and anti-inflammatory effects. Recent studies on various nonskin cell lines indicate that hLF may have a stimulatory effect on cell proliferation. Objectives, To study the potential role of hLF in wound re-epithelialization. Materials and methods, The effects of hLF on cell growth, migration, attachment and survival were assessed, with a rice-derived recombinant hLF (holo-rhLF), using proliferation analysis, scratch migration assay, calcein-AM/propidium iodide staining and terminal deoxynucleotidyl transferase-mediated dUTP nick-end labelling (TUNEL) method, respectively. The mechanisms of hLF on cell proliferation and migration were explored using specific pathway inhibitors. The involvement of lactoferrin receptor low-density lipoprotein receptor-related protein 1 (LRP1) was examined with RNA interference technique. An in vivo swine second-degree burn wound model was also used to assess wound re-epithelialization. Results, Studies revealed that holo-rhLF significantly stimulated keratinocyte proliferation which could be blocked by mitogen-activated protein kinase (MAPK) kinase 1 inhibitor. Holo-rhLF also showed strong promoting effects on keratinocyte migration, which could be blocked by either inhibition of the MAPK, Src and Rho/ROCK pathways, or downregulation of the LRP1 receptor. With cells under starving or 12- O -tetradecanoylphorbol-13-acetate exposure, the addition of holo-rhLF was found greatly to increase cell viability and inhibit cell apoptosis. Additionally, holo-rhLF significantly increased the rate of wound re-epithelialization in swine second-degree burn wounds. Conclusions, Our studies demonstrate the direct effects of holo-rhLF on wound re-epithelialization including the enhancement of keratinocyte proliferation and migration as well as the protection of cells from apoptosis. The data strongly indicate its potential therapeutic applications in wound healing. [source] In vivo release of the antimicrobial peptide hLF1-11 from calcium phosphate cement,JOURNAL OF ORTHOPAEDIC RESEARCH, Issue 4 2008Hein P. Stallmann Abstract We studied the release of human lactoferrin 1-11 (hLF1-11), a potent antimicrobial peptide, in an animal model. Calcium phosphate cement with 50 mg/g hLF1-11 was injected into the femoral canal of 12 rabbits. One, 3, and 7 days later, four animals were terminated, and the femora excised. Sections of bone and cement were removed for histological analysis. We used liquid chromatography-mass spectrometry/mass spectrometry for semiquantitative determination of the hLF1-11 concentration. Blood samples were drawn for leukocyte count and differentiation to identify a potential immunomodulating effect of hLF1-11. After an initial burst release, the hLF1-11 concentration in cement and bone decreased steadily. This in vivo release profile is consistent with earlier in vitro studies. Tissue ingrowth into the cement, without signs of inflammation or necrosis, was observed. Leukocytosis or a shift in leukocyte differentiation did not occur. The carrier released over 99% of the hLF1-11, resulting in peak concentrations at the cement,bone interface. This indicates that hLF1-11 could become a valuable prophylactic agent in osteomyelitis treatment. © 2007 Orthopaedic Research Society. Published by Wiley Periodicals, Inc. J Orthop Res 26:531,538, 2008 [source] Recombinant Human Lactoferrin is Effective in the Treatment of Helicobacter felis -infected MiceJOURNAL OF PHARMACY AND PHARMACOLOGY: AN INTERNATI ONAL JOURNAL OF PHARMACEUTICAL SCIENCE, Issue 12 2000E. J. DIAL Recombinant human lactoferrin possesses in-vitro antibiotic and anti-inflammatory activity similar to the native form. It was tested for in-vivo activity in mice infected with the gastritis-inducing bacterium Helicobacter felis. A two-week course of treatment with lactoferrin was sufficient to partially reverse both infection-induced gastritis and the infection rate, and fully reverse gastric surface hydro-phobicity changes. A comparison of lactoferrin with amoxicillin and standard triple therapy revealed no differences in infection rate. These results show that recombinant human lactoferrin is effective in a mouse model of Helicobacter infection, and support further testing of this promising agent for this application. [source] Structure of buffalo lactoferrin at 3.3,Å resolution at 277,KACTA CRYSTALLOGRAPHICA SECTION D, Issue 6 2000S. Karthikeyan The three-dimensional structure of diferric buffalo lactoferrin has been determined at 3.3,Å resolution. The structure was solved by molecular replacement using the coordinates of diferric human lactoferrin as a search model and was refined by simulated annealing (X-PLOR). The final model comprises 5316 protein atoms for all 689 residues, two Fe3+ and two CO ions. The final R factor was 21.8% for 11,711 reflections in the resolution range 17.0,3.3,Å. The folding of buffalo lactoferrin is essentially similar to that of the other members of the transferrin family. The significant differences are found in the dimensions of the binding cleft and the interlobe orientation. The interlobe interactions are predominantly hydrophobic in nature, thus facilitating the sliding of two lobes owing to external forces. The interdomain interactions are comparable in the N and C lobes. [source] Human and bovine lactoferrins in the milk of recombinant human lactoferrin-transgenic dairy cows during lactationBIOTECHNOLOGY JOURNAL, Issue 4 2006Paula Hyvönen Abstract Seven Friesian human lactoferrin (hLf)-transgenic primiparous dairy cows expressing recombinant hLf (rhLf) in their milk were included in the study. After calving, concentrations of rhLf and bovine LF (bLf) in the milk, somatic cell count and milk yield were determined. The concentration of rhLf was found to be constant, about 2.9 mg/mL, throughout the early lactation period of 3 months. The concentration of bLf in colostrum was higher after calving, but decreased rapidly during the first days of lactation. The mean concentration of bLf was 0.15 mg/mL, but concentrations varied between cows from 0.07 mg/mL to 0.26 mg/mL. Based on that, it may be possible to improve the non-specific host defence mechanism in the mammary gland of dairy cows by enhancing the content of rhLf in the milk. [source] | ||||||||||||||||