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Lactoferrin
Kinds of Lactoferrin Terms modified by Lactoferrin Selected AbstractsANTIOXIDATIVE AND ANTIMICROBIAL PROPERTIES OF LACTOFERRIN IN HOT-BONED GROUND PORK DURING STORAGEJOURNAL OF FOOD PROCESSING AND PRESERVATION, Issue 2 2007C.H. CHIU ABSTRACT The effect of lactoferrin concentration on the antioxidative and antimicrobial activities of hot-boned (4,5 h after death) ground pork during storage at 4C for 9 days was examined. The total iron content increased with the addition of lactoferrin. Meat samples with added lactoferrin (40 or 80 mg/kg) had lower thiobarbituric acid reactive substances (TBARS) than controls at 3, 6 and 9 days; however, the differences in TBARS between the 40- and 80-mg lactoferrin/kg treatments were not significant. With the addition of lactoferrin (40 or 80 mg/kg), ground pork had lower (P < 0.05) total plate counts than controls at 3, 6 and 9 days of storage. However, the differences in total plate counts between the 40- and 80-mg lactoferrin/kg treatments were only significant (P < 0.05) at days 3 and 6. The addition of lactoferrin (80 mg/kg) decreased lactic acid bacterial counts at days 0, 3 and 9. The pH values of hot-boned ground pork were unaffected by the addition of lactoferrin, but slightly increased with storage time. [source] ANTIBACTERIAL ACTIVITY AND BINDING ABILITY OF BOVINE LACTOFERRIN AGAINST PSEUDOMONAS SPP.JOURNAL OF FOOD SAFETY, Issue 1 2008WOAN-SUB KIM ABSTRACT The antibacterial activity of bovine lactoferrin was tested against Pseudomonas fluorescens and Pseudomonas syringae. The activity was studied by monitoring the growth of a Pseudomonas spp. in the presence or absence of bovine apo-lactoferrin, bovine holo-lactoferrin or native-lactoferrin in liquid media at different concentrations. Lactoferrin-binding proteins in the membrane fractions of Pseudomonas spp. were detected using far-Western blot analysis. The addition of bovine lactoferrin to the medium inhibited the growth of all tested strains. Furthermore, the growth of P. fluorescens and P. syringae was strongly inhibited by bovine apo-lactoferrin. The estimated molecular weights of lactoferrin-binding proteins in P. fluorescens were 70, 49, 47 and 25 kDa, and 70, 48 and 28 kDa in P. syringae. PRACTICAL APPLICATIONS Pseudomonas fluorescens is an important psychrotrophic bacterium responsible for undesirable flavors in milk and dairy products. Thus, flavor and texture defects, such as bitterness and running paste, were also reported. In addition, Pseudomonas syringae causes various diseases on many different susceptible plant species, generally producing chlorotic and necrotic lesions on leaves and fruits. The resultant bacterial spoilage causes considerable economic losses for the food and dairy industries. At present, antiseptics and agricultural chemicals are used for defense of foods and vegetables from these bacteria, but such substances are known to deleteriously affect the human body. The results of this study demonstrate that bovine lactoferrin significantly inhibits the growth of P. fluorescens and P. syringae. The results indicate that the incorporation of bovine lactoferrin is expected to protect dairy products, food and fruits from pathogenic bacteria. [source] Lactoferrin and anti-lactoferrin antibodies: Effects of ironloading of lactoferrin on albumin extravasation in different tissues in ratsACTA PHYSIOLOGICA, Issue 1 2000Erga Lactoferrin is a cationic iron-binding protein, which is released from activated neutrophils in concert with reactive oxygen species. In vitro, lactoferrin has both anti- and proinflammatory effects; many of them dependent on iron-binding. In vivo, only iron-free lactoferrin reduced inflammatory hyperpermeability in the lung. We therefore examined whether 1 mg iron-free (Apo-Lf) or iron-saturated lactoferrin (Holo-Lf) alone or followed by anti-lactoferrin antibodies (aLf) affected permeability evaluated by extravasation of radiolabelled bovine serum albumin (CBSA) in different tissues of anaesthetized rats. Fifteen minutes after i.v. injection of Lf, aLf or saline was given and circulatory arrest was induced 20 min thereafter. Measurements were performed in control, after Apo-Lf, Holo-Lf, Apo-Lf + aLf, Holo-Lf + aLf and aLf alone (n=6,8 in each group). No intergroup differences were found for plasma volume and haematocrit at the start and end of the 37 min extravasation period or for total tissue water in any of the six different tissues studied, excluding larger transcapillary fluid shifts. However, increases in CBSA were seen without differences in tissue intravascular volume. Iron-free lactoferrin and aLf alone did not change CBSA significantly. Iron-saturated lactoferrin significantly increased CBSA in skin (neck), trachea and left ventricle of the heart to 249 ± 9, 284 ± 16 and 160 ± 7% of control, respectively. When followed by aLf, both Apo- and Holo-Lf increased CBSA significantly in four and five of the tissues studied, respectively. However, no significant effect was seen for Holo-Lf + aLf compared with Holo-Lf alone. In conclusion, iron-saturated, but not iron-free lactoferrin increased CBSA, whereas antilactoferrin increased CBSA compared with lactoferrin alone only when following iron-free lactoferrin. [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] Surface nucleolin participates in both the binding and endocytosis of lactoferrin in target cellsFEBS JOURNAL, Issue 2 2004Dominique Legrand Lactoferrin (Lf), a multifunctional molecule present in mammalian secretions and blood, plays important roles in host defense and cancer. Indeed, Lf has been reported to inhibit the proliferation of cancerous mammary gland epithelial cells and manifest a potent antiviral activity against human immunodeficiency virus and human cytomegalovirus. The Lf-binding sites on the cell surface appear to be proteoglycans and other as yet undefined protein(s). Here, we isolated a Lf-binding 105 kDa molecular mass protein from cell extracts and identified it as human nucleolin. Medium,affinity interactions (, 240 nm) between Lf and purified nucleolin were further illustrated by surface plasmon resonance assays. The interaction of Lf with the cell surface-expressed nucleolin was then demonstrated through competitive binding studies between Lf and the anti-human immunodeficiency virus pseudopeptide, HB-19, which binds specifically surface-expressed nucleolin independently of proteoglycans. Interestingly, binding competition studies between HB-19 and various Lf derivatives in proteoglycan-deficient hamster cells suggested that the nucleolin-binding site is located in both the N- and C-terminal lobes of Lf, whereas the basic N-terminal region is dispensable. On intact cells, Lf co-localizes with surface nucleolin and together they become internalized through vesicles of the recycling/degradation pathway by an active process. Morever, a small proportion of Lf appears to translocate in the nucleus of cells. Finally, the observations that endocytosis of Lf is inhibited by the HB-19 pseudopeptide, and the lack of Lf endocytosis in proteoglycan-deficient cells despite Lf binding, point out that both nucleolin and proteoglycans are implicated in the mechanism of Lf endocytosis. [source] Antimicrobial Effects of Lactoferrin, Lysozyme, and the Lactoperoxidase System and Edible Whey Protein Films Incorporating the Lactoperoxidase System Against Salmonella enterica and Escherichia coli O157:H7JOURNAL OF FOOD SCIENCE, Issue 7 2005Seacheol Min ABSTRACT: Lactoferrin (LF), lysozyme (LZ), the lactoperoxidase system (LPOS), and edible whey protein isolate (WPI) films incorporating LPOS were studied for inhibition of Salmonella enterica and Escherichia coli O157:H7. Antimicrobial effects of LF (5 to 40 mg/mL), LZ (1 to 20 mg/mL), and LPOS (0.5% to 5.0% [w/v] [0.03,.25 g/g, dry basis]) were examined by measuring turbidity of antimicrobial-containing media after inoculation and by examining cell inhibition by WPI films incorporating LPOS (LPOS-WPI films) on an agar recovery medium. Elastic modulus (EM), tensile strength (TS), percent elongation (%E), oxygen permeability (OP), and Hunter L, a and b of WPI films incorporating 0.03 to 0.25 g/g of LPOS were compared with those of plain WPI films without LPOS. The growth of S. enterica and E. coli O157:H7 (4 log colony-forming units [CFU]/mL) in tryptic soy broth (TSB) was not prevented by LF at ,20 and ,40 mg/mL, respectively. S. enterica and E. coli O157:H7 in TSB were not inhibited by LZ at , 6 and , 20 mg/mL, respectively. LPOS at concentrations of 2.75% (w/v) and 1.0% (w/v) reduced S. enterica and E. coli O157:H7 to below the limit of detection (1 CFU/mL) in TSB, respectively. LPOS-WPI films (0.15 g/g) completely inhibited S. enterica and E. coli O157:H7 (4 log CFU/cm2), inoculated either onto agar before placing the film disc or onto top of the film disc. Incorporation of 0.25 g/g of LPOS decreased EM, TS, and %E. The oxygen barrier property of WPI films was improved with the incorporation of LPOS at 0.15 to 0.25 g/g. [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] Faecal lactoferrin , a novel test to differentiate between the irritable and inflamed bowel?ALIMENTARY PHARMACOLOGY & THERAPEUTICS, Issue 12 2010R. SIDHU Aliment Pharmacol Ther,31, 1365,1370 Summary Background, Distinguishing between inflammatory bowel disease (IBD) and irritable bowel syndrome (IBS) can be challenging. Aims, To investigate the utility of faecal lactoferrin as a marker of inflammation in patients with IBD, IBS and controls. Methods, Disease activity in IBD patients was assessed using the modified Harvey,Bradshaw Activity Index. Stool samples were analysed using an ELISA assay. Results, We recruited 137 patients with IBS, 126 with ulcerative colitis (UC) and 104 with Crohn's disease (CD), and 98 healthy volunteers. The median ± IQ lactoferrin concentration (,g/g faecal weight) was 0 ± 1.4 for IBS patients, 6.6 ± 42 for UC patients, 4 ± 12.7 for CD patients and 0.5 ± 2 for healthy controls. Lactoferrin levels were significantly higher in IBD patients compared with IBS/healthy controls (P < 0.001). The median lactoferrin concentrations were significantly higher in active UC & CD patients compared with inactive patients (P < 0.001 and P = 0.002 respectively). The sensitivity, specificity, positive and negative predictive values of lactoferrin in distinguishing active IBD from IBS/healthy controls were 67% and 96%, 87% and 86.8% respectively. Conclusions, Lactoferrin is useful to differentiate between IBD and IBS, and can be used as an adjunct to blood parameters to determine IBD patients who have ongoing inflammation. [source] Lactoferrin protects against concanavalin A-induced liver injury in miceLIVER INTERNATIONAL, Issue 4 2010Hao Yin Abstract Background: Liver diseases, caused by viral infection, autoimmune conditions, alcohol ingestion or the use of certain drugs, are a significant health issue, as many can develop into liver failure. Lactoferrin (Lac) is an iron-binding glycoprotein that belongs to the transferrin family. Owing to its multiple biological functions, Lac has been evaluated in a number of clinical trials to treat infections, inflammation and cancer. Aim: The present study aims to reveal a profound hepatoprotective effect of Lac, using a mouse model of Concanavalin A (Con A)-induced hepatitis, which mimics the pathophysiology of human viral and autoimmune hepatitis. Method: C57Bl/6J mice were injected with bovine Lac following Con A challenge. The effects of Lac on interferon (IFN)-, and interleukin (IL)-4 expression were determined. The roles of Lac on T-cell apoptosis and activation, and leukocytes infiltration were examined. Result: The data demonstrated that the protective effect of Lac was attributed to its ability to inhibit T-cell activation and production of IFN-,, as well as to suppress IL-4 production by hepatic natural killer T cells. Conclusion: These findings indicate a great therapeutic potential of Lac in treating in treating inflammatory hepatitis and possibly other inflammatory diseases. [source] Lactoferrin in Canine Sera: A Pyometra StudyREPRODUCTION IN DOMESTIC ANIMALS, Issue 2009A Bartoskova Contents The concentration of lactoferrin was measured in canine sera from groups of healthy male dogs as well as pregnant and non-pregnant female dogs and was compared with that of bitches with pyometra. Lactoferrin concentrations were higher in bitches with pyometra. The role of elevated lactoferrin concentrations in the suppression of lymphocyte activity was examined in sera from bitches with pyometra in a series of investigations. Although the sera from bitches with pyometra were capable of suppressing lymphocyte activity, lactoferrin was not found to be involved in this action. [source] Characterization of cryogel monoliths for extraction of minor proteins from milk by cation exchangeBIOTECHNOLOGY & BIOENGINEERING, Issue 6 2009Jagan M. Billakanti Abstract Extraction and purification of high-value minor proteins directly from milk without pre-treatment is a challenge for the dairy industry. Pre-treatment of milk before extraction of proteins by conventional packed-bed chromatography is usually necessary to prevent column blockage but it requires several steps that result in significant loss of yield and activity for many minor proteins. In this paper, we demonstrate that it is possible to pass 40,50 column volumes of various milk samples (raw whole milk, homogenized milk, skim milk and acid whey) through a 5 mL cryogel chromatographic column at 550 cm/h without exceeding its pressure limits if the processing temperature is maintained above 35°C. The dynamic binding capacity obtained for the cryogel matrix (2.1 mg/mL) was similar to that of the binding capacity (2.01 mg/mL) at equilibrium with 0.1 mg/mL of lactoferrin in the feed samples. The cryogel column selectively binds lactoferrin and lactoperoxidase with only minor leakage in flowthrough fractions. Lactoferrin was recovered from elution fractions with a yield of over 85% and a purity of more than 90%. These results, together with the ease of manufacture, low cost and versatile surface chemistry of cryogels suggest that they may be a good alternative to packed-bed chromatography for direct capture of proteins from milk. Biotechnol. Bioeng. 2009;103: 1155,1163. © 2009 Wiley Periodicals, Inc. [source] Chemopreventive Effects of Bovine Lactoferrin on N -Butyl- N -(4- hydroxybutyl)nitrosamine-induced Rat Bladder CarcinogenesisCANCER SCIENCE, Issue 6 2000Chikayoshi Masuda Chemopreventive effects of bovine lactoferrin (bLF), which is found at high concentrations in colostrum, on rat bladder carcinogenesis were investigated using a rat bladder medium-term bioassay. In experiment 1, a total of 80 F344 male rats, 6 weeks old, were divided into 5 groups. Groups 1 and 2 were treated with 0.05%N -butyl- N -(4-hydroxybutyl)nitrosamine (BBN) in the drinking water for 8 weeks and after a 1-week interval, received dietary supplementation with 2% and 0.2% bLF, respectively. Group 3 received 0.05% BBN for 8 weeks and then no treatment. Group 4 was administered 2% bLF alone from week 9, without prior carcinogen exposure. Group 5 was maintained without any treatment throughout the experiment. All rats were killed at the end of week 36. Group 1 demonstrated a significantly decreased multiplicity of the bladder tumors (carcinomas and papillomas) as compared with group 3, Maximum cut surface areas of bladder tumors were also significantly decreased in groups 1 and 2 compared with group 3. No bladder tumors were observed in groups 4 or 5. In experiment 2, a total of 60 rats were divided into two groups (30 rats each); both were treated with 0.05% BBN for 4 weeks and after a 1-week interval, one received 2% bLF (group 1) and the other, basal diet (group 2) for 4 weeks. Group 1 demonstrated a tendency for decrease of the 5-bromo-2,-deoxyuridine (BrdU) labeling index. bLF was detected in the urine of rats fed bLF by ELISA as well as western blot analysis. The findings indicate that 2% bLF can inhibit BBN-induced rat bladder carcinogenesis, and that this may be due to bLF in the urine. [source] Lactoferrin and anti-lactoferrin antibodies: Effects of ironloading of lactoferrin on albumin extravasation in different tissues in ratsACTA PHYSIOLOGICA, Issue 1 2000Erga Lactoferrin is a cationic iron-binding protein, which is released from activated neutrophils in concert with reactive oxygen species. In vitro, lactoferrin has both anti- and proinflammatory effects; many of them dependent on iron-binding. In vivo, only iron-free lactoferrin reduced inflammatory hyperpermeability in the lung. We therefore examined whether 1 mg iron-free (Apo-Lf) or iron-saturated lactoferrin (Holo-Lf) alone or followed by anti-lactoferrin antibodies (aLf) affected permeability evaluated by extravasation of radiolabelled bovine serum albumin (CBSA) in different tissues of anaesthetized rats. Fifteen minutes after i.v. injection of Lf, aLf or saline was given and circulatory arrest was induced 20 min thereafter. Measurements were performed in control, after Apo-Lf, Holo-Lf, Apo-Lf + aLf, Holo-Lf + aLf and aLf alone (n=6,8 in each group). No intergroup differences were found for plasma volume and haematocrit at the start and end of the 37 min extravasation period or for total tissue water in any of the six different tissues studied, excluding larger transcapillary fluid shifts. However, increases in CBSA were seen without differences in tissue intravascular volume. Iron-free lactoferrin and aLf alone did not change CBSA significantly. Iron-saturated lactoferrin significantly increased CBSA in skin (neck), trachea and left ventricle of the heart to 249 ± 9, 284 ± 16 and 160 ± 7% of control, respectively. When followed by aLf, both Apo- and Holo-Lf increased CBSA significantly in four and five of the tissues studied, respectively. However, no significant effect was seen for Holo-Lf + aLf compared with Holo-Lf alone. In conclusion, iron-saturated, but not iron-free lactoferrin increased CBSA, whereas antilactoferrin increased CBSA compared with lactoferrin alone only when following iron-free lactoferrin. [source] Analysis of the sinusitis nasal lavage fluid proteome using capillary liquid chromatography interfaced to electrospray ionization-quadrupole time of flight- tandem mass spectrometryELECTROPHORESIS, Issue 9 2004Begona Casado Abstract The nasal lavage fluids (NLFs) from four subjects with acute sinusitis were analyzed to investigate the amount of proteins expressed in this pathology at the beginning of the event (day 1) and after 6 days of treatment with antibiotics and a nasal steroid spray. The protein identification was performed with capillary liquid chromatography-electrospray-quadrupole time of flight-(LC-ESI-Q-TOF)-mass spectrometry. The samples collected on the first day contained high-abundant plasma proteins, such as albumin and immunoglobulins, glandular serous cell proteins (lysozyme, lactoferrin, and polymeric immunoglobulin receptor), epithelial keratins, and inflammatory cell proteins (myeloperoxidase, IL-16, and IL-17E). After six days of therapy, the complexity of the proteome was reduced to plasma proteins and lysozyme with no inflammatory markers. The presence of hemoglobin, however, suggested that significant squamous metaplasia with breaches in the epithelial barrier, or nasal steroid-related bleeding, had occurred. The proteomic approach presented here allowed us to identify, in the high complexity of acute sinusitis nasal secretions, the proteins that respond to a pharmacological treatment and that could be suitable as markers of this pathology. [source] Enteric-formulated lactoferrin was more effectively transported into blood circulation from gastrointestinal tract in adult ratsEXPERIMENTAL PHYSIOLOGY, Issue 6 2006Takashi Takeuchi We have previously demonstrated that intestinally infused bovine lactoferrin (bLF) is transported into the blood circulation via the lymphatic pathway, not via the portal circulation. Therefore, in the present study, we further investigated whether intragastrically infused enteric-formulated bLF (EF-bLF) was more efficiently absorbed than bLF from the intestine in adult rats. The rats were randomly divided into three groups: 30 and 300 mg kg,1 non-enteric-formulated bLF (non-EF-bLF) groups and a 30 mg kg,1 EF-bLF group. Thoracic lymph was collected from a thoracic lymph duct under general anaesthesia. Bovine lactoferrin was infused into the stomach or duodenal lumen via a needle for a period of over 1 min in a volume of 1 ml kg,1. The bLF transported into the lymph was assayed quantitatively by double-antibody enzyme-linked immunosorbent assay (ELISA). Following the intragastric administration of bLF, the three groups showed almost the same lymph flow, but the bLF concentration in the lymph fluid in the EF-bLF group increased significantly and peaked 3 h after administration. With intraduodenal administration, the bLF concentration in the lymph fluid of the higher non-EF-bLF group was significantly higher than those of the other groups. The amount of absorbed bLF in the EF-bLF group was, however, about 10 times higher than that in the lower non-EF-bLF group, when it was administered intragastrically. These data show that enteric-formulated bLF is less susceptible to gastric pepsin and is more efficiently absorbed from the intestine than is non-enteric-formulated bLF. [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] Cell surface nucleolin on developing muscle is a potential ligand for the axonal receptor protein tyrosine phosphatase-,FEBS JOURNAL, Issue 20 2006Daniel E. Alete Reversible tyrosine phosphorylation, catalyzed by receptor tyrosine kinases and receptor tyrosine phosphatases, plays an essential part in cell signaling during axonal development. Receptor protein tyrosine phosphatase-, has been implicated in the growth, guidance and repair of retinal axons. This phosphatase has also been implicated in motor axon growth and innervation. Insect orthologs of receptor protein tyrosine phosphatase-, are also implicated in the recognition of muscle target cells. A potential extracellular ligand for vertebrate receptor protein tyrosine phosphatase-, has been previously localized in developing skeletal muscle. The identity of this muscle ligand is currently unknown, but it appears to be unrelated to the heparan sulfate ligands of receptor protein tyrosine phosphatase-,. In this study, we have used affinity chromatography and tandem MS to identify nucleolin as a binding partner for receptor protein tyrosine phosphatase-, in skeletal muscle tissue. Nucleolin, both from tissue lysates and in purified form, binds to receptor protein tyrosine phosphatase-, ectodomains. Its expression pattern also overlaps with that of the receptor protein tyrosine phosphatase-,-binding partner previously localized in muscle, and nucleolin can also be found in retinal basement membranes. We demonstrate that a significant amount of muscle-associated nucleolin is present on the cell surface of developing myotubes, and that two nucleolin-binding components, lactoferrin and the HB-19 peptide, can block the interaction of receptor protein tyrosine phosphatase-, ectodomains with muscle and retinal basement membranes in tissue sections. These data suggest that muscle cell surface-associated nucleolin represents at least part of the muscle binding site for axonal receptor protein tyrosine phosphatase-, and that nucleolin may also be a necessary component of basement membrane binding sites of receptor protein tyrosine phosphatase-,. [source] Surface nucleolin participates in both the binding and endocytosis of lactoferrin in target cellsFEBS JOURNAL, Issue 2 2004Dominique Legrand Lactoferrin (Lf), a multifunctional molecule present in mammalian secretions and blood, plays important roles in host defense and cancer. Indeed, Lf has been reported to inhibit the proliferation of cancerous mammary gland epithelial cells and manifest a potent antiviral activity against human immunodeficiency virus and human cytomegalovirus. The Lf-binding sites on the cell surface appear to be proteoglycans and other as yet undefined protein(s). Here, we isolated a Lf-binding 105 kDa molecular mass protein from cell extracts and identified it as human nucleolin. Medium,affinity interactions (, 240 nm) between Lf and purified nucleolin were further illustrated by surface plasmon resonance assays. The interaction of Lf with the cell surface-expressed nucleolin was then demonstrated through competitive binding studies between Lf and the anti-human immunodeficiency virus pseudopeptide, HB-19, which binds specifically surface-expressed nucleolin independently of proteoglycans. Interestingly, binding competition studies between HB-19 and various Lf derivatives in proteoglycan-deficient hamster cells suggested that the nucleolin-binding site is located in both the N- and C-terminal lobes of Lf, whereas the basic N-terminal region is dispensable. On intact cells, Lf co-localizes with surface nucleolin and together they become internalized through vesicles of the recycling/degradation pathway by an active process. Morever, a small proportion of Lf appears to translocate in the nucleus of cells. Finally, the observations that endocytosis of Lf is inhibited by the HB-19 pseudopeptide, and the lack of Lf endocytosis in proteoglycan-deficient cells despite Lf binding, point out that both nucleolin and proteoglycans are implicated in the mechanism of Lf endocytosis. [source] Whey-derived free fatty acids suppress the germination of Candida albicans in vitroFEMS YEAST RESEARCH, Issue 2 2007Martin Clément Abstract Bovine whey from the cheese-making industry contains several bioactive factors that promote health and prevent disease. Although many efforts have been made over the years to show that immunoglobulins, lactoperoxidase, lactoferrin, lysosyme and small peptides present in whey have antimicrobial activities against several pathogenic microorganisms, such activities have not been investigated so far for the lipid fraction of whey. Here, we have used an in vitro assay-based fractionation procedure to show that free fatty acids derived from whey cream specifically inhibit the germination of Candida albicans, a morphologic change associated with pathogenicity. Further fractionation by HPLC demonstrated that this activity can be mainly attributed to lauric acid, myristoleic acid, linoleic acid and arachidonic acid. [source] Evaluation of the clinical efficacy of a mouthwash and oral gel containing the antimicrobial proteins lactoperoxidase, lysozyme and lactoferrin in elderly patients with dry mouth , a pilot studyGERODONTOLOGY, Issue 1 2008Jose Antonio Gil-Montoya Objectives:, To evaluate the clinical efficacy of a mouthwash and oral gel containing the antimicrobial proteins lactoperoxidase, lactoferrin and lysozyme, in a sample of elderly individuals with dry mouth. Material and methods:, Twenty elderly institutionalised subjects with dry mouth and with a certain degree of independence for daily life activities were included in this pilot study. A randomised, double blind and cross-over design was used. The study variables comprised subjective dry mouth sensation, the severity of discomfort assessed by means of a visual analogical scale (VAS), the Oral Health Impact Profile (OHIP), the presence of signs and symptoms of dry mouth, sialometry and Candida albicans culture. All the variables were recorded before and after each of the two periods of the study. Results:, The 20 selected subjects we made up of 16 women and four men, with a mean age of 81.3 years. Improvement was observed on analysing the data between the first and second intervention period in terms of the OHIP values, the presence of dry mouth, and the need to drink fluids to swallow. However, the improvement in certain variables before and after treatment did not take a positive course in all cases, and some subjects even improved with placebo. Conclusions:, The evaluated mouthwash and oral gel improved some subjective and clinical aspects in elderly individuals with dry mouth, though a placebo effect cannot be entirely discarded. [source] Lactoferrin decreases pollen antigen-induced allergic airway inflammation in a murine model of asthmaIMMUNOLOGY, Issue 2 2006Marian L. Kruzel Summary Pollen grains contain reduced nicotinamide adenine dinucleotide phosphate (NAD(P)H) oxidases and in contact with mucosal surfaces generate superoxide anion (O2,,). In the presence of iron, O2,, may be converted to more reactive oxygen radicals, such as to H2O2 and/or ,OH, which may augment antigen-induced airway inflammation. The aim of the study was to examine the impact of lactoferrin (LF), an iron-binding protein, on ragweed (Ambrosia artemisiifolia) pollen extract (RWE)-induced cellular oxidative stress levels in cultured bronchial epithelial cells and accumulation of inflammatory and mucin-producing cells in airways in a mouse model of allergic airway inflammation. Results show that LF lowered RWE-induced increase in cellular reactive oxygen species (ROS) levels in bronchial epithelial cells. Most importantly, LF significantly decreased accumulation of eosinophils into airways and subepithelium of intranasally challenged, sensitized mice. LF also prevented development of mucin-producing cells. Amb a 1, the major allergenic ragweed pollen antigen lacking NAD(P)H oxidase activity, induced low-grade airway inflammation. When administered along with glucose oxidase (G-ox), a superoxide-generating enzyme, Amb a 1 induced robust airway inflammation, which was significantly lowered by LF. Surprisingly, LF decreased also inflammation caused by Amb a 1 alone. Iron-saturated hololactoferrin had only a marginal effect on RWE-induced cellular ROS levels and RWE- or Amb a 1 plus G-ox-induced inflammation. We postulate that free iron in the airways chemically reduces O2,, to more reactive species which augment antigen-induced inflammation in a mouse model of asthma. Our results suggest the utility of LF in human allergic inflammatory disorders. [source] Fecal calprotectin, lactoferrin, and endoscopic disease activity in monitoring anti-TNF-alpha therapy for Crohn's diseaseINFLAMMATORY BOWEL DISEASES, Issue 10 2008Taina Sipponen MD Abstract Background: Fecal calprotectin and lactoferrin are promising noninvasive biomarkers for intestinal inflammation. In Crohn's disease (CD), during anti-TNF-alpha (TNF-,) treatment, the clinical significance of these markers has, however, been insufficiently explored. Methods: Among CD patients receiving anti-TNF-, therapy we assessed the role of fecal calprotectin and lactoferrin as surrogate markers for mucosal healing. Before and 3 months after the beginning of anti-TNF-, induction, 15 patients underwent ileocolonoscopy with scoring of the Crohn's Disease Index of Severity (CDEIS). Fecal samples for calprotectin and for lactoferrin measurements were collected and the Crohn's Disease Activity Index (CDAI) was calculated at the time of the endoscopies and 2 and 8 weeks after the first treatment. Results: The median CDEIS fell from 13.0 to 4.8 (P = 0.002) and CDAI from 158 to 68 (P = 0.005). Accordingly, the median fecal calprotectin concentration fell from 1173 ,g/g to 130 ,g/g (P = 0.001) and fecal lactoferrin from 105.0 ,g/g to 2.7 ,g/g (P = 0.001). Of the 15 patients, 11 (73%) showed an endoscopic response to treatment and 5 of these achieved endoscopic remission (CDEIS < 3). In those 5 patients the fecal calprotectin concentration declined from 1891 ,g/g (range 813,2434) to 27 ,g/g (13,130) and lactoferrin from 92.4 ,g/g (35.5,235.6) to 1.9 ,g/g (0.0,2.1). Conclusions: Compared to pretreatment values, concentrations of fecal calprotectin and lactoferrin after the anti-TNF-, treatment were significantly lower. During anti-TNF-, therapy these fecal neutrophil-derived proteins may thus be useful surrogate markers for mucosal healing. (Inflamm Bowel Dis 2008) [source] Pilot study on the effect of reducing dietary FODMAP intake on bowel function in patients without a colonINFLAMMATORY BOWEL DISEASES, Issue 12 2007Catherine Croagh MB Abstract Background: Poorly absorbed short-chain carbohydrates (FODMAPs) in the diet should, by virtue of their osmotic effects, increase fecal output following colectomy and ileal pouch formation or ileorectal anastomosis (IRA). The aim was to perform a proof-of-concept evaluation of this hypothesis. Methods: Fifteen patients (13 pouch, 2 IRA) had dietary and symptomatic evaluation before and during a low FODMAP diet. Carbohydrate malabsorption was evaluated by breath tests. Pouchitis was assessed clinically/endoscopically or by fecal lactoferrin. Results: Of 8 patients with a breath hydrogen response to lactulose, 7 had fructose malabsorption, 3 with lactose malabsorption, and 1 had lactose malabsorption alone. Five of 7 studied retrospectively improved stool frequency (from median 8 to 4 per day; P = 0.02), this being sustained over 0.5,3 years of follow-up. Five of 8 patients completed a prospective arm of the study. One patient had sustained improvement in stool frequency and 1 had reduced wind production. Overall, none of 8 patients who had pouchitis improved. In contrast, median daily stool frequency fell from 8 to 4 (P = 0.001) in the 7 without pouchitis. The degree of change in FODMAP intake also predicted response. There was a tendency for pouchitis to be associated with low baseline FODMAP intake. Conclusions: There is a high prevalence of carbohydrate malabsorption in these patients. Reduction of the intake of FODMAPs may be efficacious in reducing stool frequency in patients without pouchitis, depending on dietary adherence and baseline diet. (Inflamm Bowel Dis 2007) [source] Prolonging microbial shelf life of foods through the use of natural compounds and non-thermal approaches , a reviewINTERNATIONAL JOURNAL OF FOOD SCIENCE & TECHNOLOGY, Issue 2 2009Maria Rosaria Corbo Summary This paper proposes a review of some alternative approaches for food stabilisation and shelf life prolonging (based on the use of natural compounds and/or non-thermal techniques). After a brief description of food structure implication on the way of using the alternative approaches, two paragraphs summarise the topics of natural molecules (essential oils, lysozyme, lactoferrin and lactoperoxidase system, fatty acids, chitosan) and non-thermal approaches (high hydrostatic and homogenisation pressures, pulsed electric fields, high power ultrasound and irradiation). Finally, the last sections deal with the use of combined hurdles (along with the proposal of three possible modes of action of a multi-target preservation), the mathematical approaches for shelf life evaluating and some critical issues to be addressed in the future for a real scaling up of the proposed techniques. [source] Distribution of mucins and antimicrobial substances lysozyme and lactoferrin in the laryngeal subglottic regionJOURNAL OF ANATOMY, Issue 4 2008Hannes Kutta Abstract The subglottic region of the larynx is of high clinical relevance with regard to infections and malignancies. Little is known about the distribution of mucins and antimicrobial substances in this area. In this study, we have investigated the mucin distribution in the normal subglottis of the larynx. Moreover, we analysed the expression of lysozyme and lactoferrin in this area. Therefore, the subglottic region of 34 larynges was investigated immunohistochemically with different antibodies to mucins and antimicrobial substances. The epithelium reacted positive with antibodies to mucins MUC1 (34/34), 5AC (26/34), 5B (10/34), 7 (8/34), 8 (10/34) and 16 (19/34); submucosal glands were positive to mucins MUC1 (34/34), 5B (10/34), 7 (8/34), and 16 (19/34); high columnar epithelial cells and serous parts of subepithelial seromucous glands were also positive for lysozyme (34/34) and lactoferrin (34/34). The results show that human subglottic epithelium and subepithelial submucosal glands produce a broad spectrum of mucins that is almost comparable with that in other areas of the respiratory tract. We hypothesize that the mucin diversity of the subglottis has an impact on positive functional consequences during vocal production and antimicrobial defence. This antimicrobial defence is supported by synthesis and secretion of antimicrobial substances such as lysozyme and lactoferrin. Moreover, knowledge of the observed distribution pattern of mucins in the subglottis can be a useful tool for a classification of subglottic laryngeal carcinomas. [source] Effects of a lactoperoxidase system and lactoferrin, added to a milk replacer diet, on severity of diarrhoea, intestinal morphology and microbiology of digesta and faeces in young calvesJOURNAL OF ANIMAL PHYSIOLOGY AND NUTRITION, Issue 1 2000P. Van Leeuwen The objective of the present study was to determine the effects of the combination of a lactoperoxidase system (LP-s) and lactoferrin (LF) added to a milk replacer diet on severity of diarrhoea, the morphology of the small intestinal mucosa, and the microbiology of digesta and faeces in young calves, in comparison with a control diet. The experiment was conducted with 30 young calves, 15 per treatment, during the period of 7,21 days of age. During this period, calves are sensitive to gastrointestinal disturbances that can cause diarrhoea. The results showed a significantly (p < 0.05) reduced severity of diarrhoea in the LP-s/LF group compared to the control group as assessed by faecal consistency scores. Numbers of CFU (colony forming units) of Escherichia coli in jejunal and colonic digesta and in faeces were lower in the LP-s/LF group compared with the control group. The differences were significant in both colonic digesta (p < 0.1) and in faeces (p < 0.05). Examination of the small intestinal mucosa, using a dissecting microscope, indicated more finger shaped villi in the distal jejunum of LP-s/LF-treated calves compared with the control group (p < 0.05). Histometrical measurements showed that these villi were significantly (p < 0.05) longer. [source] Evaluation of in vitro endocytosis and antibody synthesis by rainbow trout head kidney cells treated with bovine lactoferrinJOURNAL OF FISH BIOLOGY, Issue 3 2005S. Cecchini Bovine lactoferrin (LF) was evaluated for its capacity to modulate the in vitro endocytosis (phagocytosis and pinocytosis) and antibody synthesis by head kidney cells of rainbow trout Oncorhynchus mykiss. Phagocytic activity and phagocytic index of head kidney macrophages, determined by measurement of ingested yeast, were influenced by bovine LF starting from the LF concentration of 1 and 0·1 ,g ml,1, respectively. Endocytosis, determined by the evaluation of droplet uptake of neutral red dye solution, was significantly enhanced by 10 ,g ml,1 of LF. In contrast, antibody synthesis by head kidney cells, evaluated by immunoenzymatic assay, from fish immunized against human-,-globulins (HGG)in vivo was not affected by bovine LF. Although these results showed that bovine LF had no effect on specific immunoglobulin production in vitro, an enhancement of the acquired immune response may be assumed in LF-treated fish in vivo, as observed in higher vertebrates. [source] Adjuvant effect of mushroom glucan and bovine lactoferrin upon Aeromonas hydrophila vaccination in catla, Catla catla (Hamilton)JOURNAL OF FISH DISEASES, Issue 6 2006D Kamilya Abstract Mushroom glucan and bovine lactoferrin (Lf), known for their immunostimulatory potential, were used as adjuvant in conjunction with a formalin-killed Aeromonas hydrophila vaccine in catla, Catla catla. In vitro antigen-specific responsiveness of catla leucocytes and protective responses against experimental challenge with homologous antigen were monitored following immunization. Antigen-specific proliferation, ,macrophage activating factor' (MAF) production and antibody production were significantly higher in fish injected with glucan adjuvanted vaccine. Lf adjuvanted preparations showed a weak proliferative response and MAF production, although the antibody production was significantly higher than the controls. A good degree of protection was achieved with the glucan adjuvanted vaccine. However, in spite of producing significant anti- A. hydrophila antibody, Lf adjuvanted vaccine did not confer any protection following challenge with A. hydrophila. The potential of adjuvanticity of mushroom glucan and bovine Lf in intraperitoneal vaccination is discussed. [source] ANTIOXIDATIVE AND ANTIMICROBIAL PROPERTIES OF LACTOFERRIN IN HOT-BONED GROUND PORK DURING STORAGEJOURNAL OF FOOD PROCESSING AND PRESERVATION, Issue 2 2007C.H. CHIU ABSTRACT The effect of lactoferrin concentration on the antioxidative and antimicrobial activities of hot-boned (4,5 h after death) ground pork during storage at 4C for 9 days was examined. The total iron content increased with the addition of lactoferrin. Meat samples with added lactoferrin (40 or 80 mg/kg) had lower thiobarbituric acid reactive substances (TBARS) than controls at 3, 6 and 9 days; however, the differences in TBARS between the 40- and 80-mg lactoferrin/kg treatments were not significant. With the addition of lactoferrin (40 or 80 mg/kg), ground pork had lower (P < 0.05) total plate counts than controls at 3, 6 and 9 days of storage. However, the differences in total plate counts between the 40- and 80-mg lactoferrin/kg treatments were only significant (P < 0.05) at days 3 and 6. The addition of lactoferrin (80 mg/kg) decreased lactic acid bacterial counts at days 0, 3 and 9. The pH values of hot-boned ground pork were unaffected by the addition of lactoferrin, but slightly increased with storage time. [source] ANTIBACTERIAL ACTIVITY AND BINDING ABILITY OF BOVINE LACTOFERRIN AGAINST PSEUDOMONAS SPP.JOURNAL OF FOOD SAFETY, Issue 1 2008WOAN-SUB KIM ABSTRACT The antibacterial activity of bovine lactoferrin was tested against Pseudomonas fluorescens and Pseudomonas syringae. The activity was studied by monitoring the growth of a Pseudomonas spp. in the presence or absence of bovine apo-lactoferrin, bovine holo-lactoferrin or native-lactoferrin in liquid media at different concentrations. Lactoferrin-binding proteins in the membrane fractions of Pseudomonas spp. were detected using far-Western blot analysis. The addition of bovine lactoferrin to the medium inhibited the growth of all tested strains. Furthermore, the growth of P. fluorescens and P. syringae was strongly inhibited by bovine apo-lactoferrin. The estimated molecular weights of lactoferrin-binding proteins in P. fluorescens were 70, 49, 47 and 25 kDa, and 70, 48 and 28 kDa in P. syringae. PRACTICAL APPLICATIONS Pseudomonas fluorescens is an important psychrotrophic bacterium responsible for undesirable flavors in milk and dairy products. Thus, flavor and texture defects, such as bitterness and running paste, were also reported. In addition, Pseudomonas syringae causes various diseases on many different susceptible plant species, generally producing chlorotic and necrotic lesions on leaves and fruits. The resultant bacterial spoilage causes considerable economic losses for the food and dairy industries. At present, antiseptics and agricultural chemicals are used for defense of foods and vegetables from these bacteria, but such substances are known to deleteriously affect the human body. The results of this study demonstrate that bovine lactoferrin significantly inhibits the growth of P. fluorescens and P. syringae. The results indicate that the incorporation of bovine lactoferrin is expected to protect dairy products, food and fruits from pathogenic bacteria. 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