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PubMed1991

Comparison between lactoferrin and subepithelial matrix protein binding in Staphylococcus aureus associated with bovine mastitis.

Staphylococcus aureus strains (n = 100) isolated from bovine mastitis were classified according to the presence of capsular polysaccharide serotype 5 (n = 46), type 8 (n = 26), and non-5/8 (n = 28). Strains from each type were tested for protein interaction in a 125I-labeled ligand binding assay. A majority of type 5 and type 8 strains showed a higher degree of binding to lactoferrin, fibronectin, and IgG than the non-5/8 strains. Fibrinogen binding was low in all serotypes. Most of the type 5 and non-5/8 strains bound less than 10% laminin, whereas type 8 strains bound laminin in the 11 to 20% range. Non-5/8 strains significantly differed from type 5 in lactoferrin, fibronectin, fibrinogen, and IgG and also from type 8 in fibrinogen and IgG binding. The differences in protein binding between type 5 and type 8 were nonsignificant. The degree of lactoferrin binding in all types positively correlated with laminin binding. Lactoferrin and fibrinogen bindings were correlated in type 5 and type 8 strains. Lactoferrin and fibronectin bindings were correlated only in type 5 strains. These data suggest that bovine lactoferrin binding is common and associated with subepithelial matrix protein interactions in certain serotypes of S. aureus.

Animals↗

PubMed1993

Iron-binding properties of bovine lactoferrin in iron-rich solution.

The iron-binding properties of bovine lactoferrin in iron-rich solution were investigated. Ferrous iron was not stable in solution and was easily changed to the insoluble ferric state, but solubility of ferrous iron was stabilized by the presence of lactoferrin. However, casein hydrolysate or BSA was not effective in stabilizing iron in solution. As indicated by use of cibacron blue affinity gel, iron bound to lactoferrin, and the charge of supersaturated lactoferrin was higher than that of normal iron-saturated lactoferrin according to native PAGE electrophoresis. The evidence suggests that lactoferrin can bind iron at sites other than its chelate-binding sites, thereby stabilizing iron in solution.

Animals↗

PubMed1996

Effect of supplemental lactoferrin with ferrous iron on iron status of newborn calves.

Data for 18 male and 18 female calves, born from primiparous and multiparous cows, were collected to determine the effect of supplemental lactoferrin and FeSO4 for 5 d after parturition on the Fe status of calves. Dietary treatments were 1) untreated, 2) 40 mg of Fe/d as FeSO4, and 3) 40 mg of Fe as FeSO4 plus 5 g of lactoferrin/d. Blood hematocrit and hemoglobin of calves born from primiparous cows at d 1 of age were lower than those of calves born from multiparous cows, but not different from those of their dams. Blood hematocrit and hemoglobin of male calves at d 1 of age were lower than those of female calves. Plasma Fe of primiparous cows at parturition was lower than that of multiparous cows, but plasma Fe of calves was not affected by parity of dam and sex of calf. Blood hematocrit and hemoglobin of untreated calves decreased from 1 to 10 d of age. Blood hematocrit and hemoglobin of calves treated with Fe of Fe plus lactoferrin increased from 2 to 10 d of age. Blood hematocrit and hemoglobin of calves treated with Fe plus lactoferrin were higher than those of calves treated with Fe at d 6 of age. Plasma Fe of calves treated with Fe or Fe plus lactoferrin increased temporarily at d 2 of age. Plasma Fe of calves treated with Fe plus lactoferrin at d 2 of age was lower than that of calves treated with Fe, but, at d 6 and 10 of age, plasma Fe of calves treated with Fe plus lactoferrin were higher.

Animals↗

PubMed2002

Multivalent metal-induced iron acquisition from transferrin and lactoferrin by myeloid cells.

We previously described a unique, high-capacity, ATP-independent mechanism through which myeloid cells acquire Fe from low-m.w. chelates. The rate of this Fe acquisition is markedly increased by cellular exposure to multivalent metal cations. Because most Fe in vivo is bound to transferrin or lactoferrin, we examined whether this mechanism also contributes to myeloid cell acquisition of Fe from transferrin and/or lactoferrin. Using HL-60 cells as a model system, we show cellular acquisition of (59)Fe from both lactoferrin and transferrin that was unaffected by conditions that depleted the cells of ATP or disrupted their cytoskeleton. Fe acquisition was dramatically increased by cell exposure to various metals including Ga(3+), Gd(3+), Al(3+), Fe(3+), La(3+), Zr(4+), Sn(4+), Cu(2+), and Zn(2+) by a process that was reversible. Exposure to these same metals also increased binding of both transferrin and lactoferrin to the cell surface by a process that does not appear to involve the well-described plasma membrane receptor for transferrin. Approximately 60% of the Fe acquired by the cells from transferrin and lactoferrin remained cell associated 18 h later. HL-60 cells possess a high-capacity multivalent metal-inducible mechanism for Fe acquisition from transferrin and lactoferrin that bears many similarities to the process previously described that allows these and other cell types to acquire Fe from low-m.w. Fe chelates. The biologic importance of this mechanism may relate to its high Fe acquisition capacity and the speed with which it is able to rapidly adapt to the level of extracellular Fe.

Adenosine Triphosphate↗

PubMed1993

Serum lactoferrin in lepromatous leprosy patients.

The serum concentrations of lactoferrin were determined by competitive enzyme immunoassay in the sera of 38 lepromatous leprosy patients and 16 healthy volunteers. Of the 38 lepromatous patients, 25 were without any sign of reactions while 13 were suffering from ENL type of reactions. The lactoferrin levels, in both types of patients, were observed to be significantly higher (P < 0.01 and < 0.001, respectively) than in that of healthy volunteers. The rise in lactoferrin level in reactive patients was also higher (P < 0.05) when compared to those without reactions. The serum lactoferrin levels were also found to be associated with bacterial load (r = 0.414; P < 0.01) indicating that in lepromatous leprosy patients, lactoferrin may not be very effective in preventing the growth of Mycobacterium leprae. Further studies to improve the understanding of the role of elevated levels of lactoferrin in pathogenesis of lepromatous leprosy patients and in establishing its possible use in predicting the occurrence of ENL type of reactions would be worthwhile pursuing.

Humans↗

PubMed1999

Lactoferrin inhibits G1 cyclin-dependent kinases during growth arrest of human breast carcinoma cells.

Lactoferrin inhibits cell proliferation and suppresses tumor growth in vivo. However, the molecular mechanisms underlying these effects remain unknown. In this in vitro study, we demonstrate that treatment of breast carcinoma cells MDA-MB-231 with human lactoferrin induces growth arrest at the G1 to S transition of the cell cycle. This G1 arrest is associated with a dramatic decrease in the protein levels of Cdk2 and cyclin E correlated with an inhibition of the Cdk2 kinase activity. Cdk4 activity is also significantly decreased in the treated cells and is accompanied by an increased expression of the Cdk inhibitor p21(CIP1). Furthermore, we show that lactoferrin maintains the cell cycle progression regulator retinoblastoma protein pRb in a hypophosphorylated form. Additional experiments with synchronized cells by serum depletion confirm the anti-proliferative activity of human lactoferrin. These effects of lactoferrin occur through a p53-independent mechanism both in MDA-MB-231 cells and other epithelial cell lines such as HBL-100, MCF-7, and HT-29. These findings demonstrate that lactoferrin induces growth arrest by modulating the expression and the activity of key G1 regulatory proteins.

Breast Neoplasms↗

PubMedDate not supplied

The status of lactoferrin and total iron binding capacity of human parotid saliva in Sjögren's syndrome.

UNLABELLED: Sjögren's syndrome (SS) is chronic salivary gland disorder characterized by a reduction in salivary and lacrimal secretion. Elevation in salivary lactoferrin has been reported in SS patients. Fluctuation in the iron binding capacity of lactoferrin has been associated with cellular damage. OBJECTIVE: The purpose of this study was to compare the levels of salivary lactoferrin, total iron, and iron binding capacity in Sjögren's syndrome (SS) patients and healthy controls. METHODS: SDS-PAGE was used to examine the presence of lactoferrin in 102 patients and 20 healthy controls. A colorimetric assay was used to examine the level of total salivary iron and iron binding capacity in patients and controls. RESULTS: A higher number of SS patients exhibited elevated levels of lactoferrin as compared to controls (86% vs. 20%, respectively). No significant difference was observed in the mean level of total iron in the saliva between patients and controls (12.6 micrograms/100 ml vs. 11.1 micrograms/100 ml, respectively). However, the total iron binding capacity of lactoferrin was significantly lower among SS patients than healthy controls (38.2 micrograms/100 ml vs. 61.8 micrograms/100 ml, respectively), p = 0.019. CONCLUSION: The overall results of this study suggest a possible impairment of the iron binding capacity of saliva in SS patients. Such impairment may contribute to the cellular damage of the salivary glands observed in SS patients.

Aged↗

PubMed1992

Lactoferrin binding properties of Vibrio cholerae.

The lactoferrin binding properties of Vibrio cholerae, a non-invasive pathogen were investigated. Screening of fifty V. cholerae strains of different serogroups and serotypes, showed that 10% of the V. cholerae strains bound to 125I-labelled lactoferrin, and 40% of the 125I-labelled lactoferrin bound to V. cholerae strain 623 could be displaced by unlabelled lactoferrin. Other iron-binding glycoproteins and ferroproteins like ferritin, transferrin, haemoglobin, and myoglobin inhibited the binding of 125I-lactoferrin to a lesser degree. Monosaccharides (GalNac, Man, Gal, and Fuc), and other glycoproteins such as fetuin and orosomucoid also inhibited the binding to a lesser extent. V. cholerae 623 showed a cell surface associated-proteolytic activity which cleaved off the cell-bound 125I-labelled lactoferrin. The generation of cryptotopes on the V. cholerae cell surface by proteolytic digestion favoured the binding of ferritin, transferrin, haemoglobin, and haemin, as well as Congo red, to cells of V. cholerae 623.

Animals↗

PubMed2004

[Producing human lactoferrin by high-density fermentation recombinant Pichia pastoris].

BACKGROUND: To evaluate expression of human lactoferrin gene by high-density fermentation in recombinant Pichia pastoris on the premise of maintaining its biological activities. METHODS: The neutrophil was isolated from human peripheral blood and its total RNA was prepared. Full-length cDNA of human lactoferrin gene was then obtained by RT-PCR, cloned into expression vector pPIC 3.5 K and transformed into Pichia pastoris strain KM71. With two-layer filter method, the transformants with high-productivity of human lactoferrin were screened out into fed-batch high-density fermentation. And later, the physical, chemical and biological activities of fermentation product were detected preliminarily. RESULTS: The strain p3.5-k-7 with better productivity of human lactoferrin was screened out into fed-batch high-density fermentation. The fermentation lasted nearly for nine days, with A-600 of culture once above 260 and the highest productivity of human lactoferrin being 115 mg/L, 7.67 times the amount of that in shake flask cultivation. CONCLUSION: The authors successfully realized high-density fermentation expression of human lactoferrin gene in recombinant Pichia pastoris.

Cloning, Molecular↗

PubMed2004

Mycobacterium leprae infection and serum lactoferrin levels.

Serum lactoferrin level, using competitive enzyme linked immunosorbent assay (ELISA) method, was estimated in 298 leprosy patients admitted into the hospital and attending the out-patient department of the Schieffelin Leprosy Research and Training Center. Serum from an equal number of non-leprosy individuals served as control. Mean (SD) of serum lactoferrin in non-leprosy individuals was 0.277 (0-092) microg/ml while in leprosy patients it was 0.494 (0.394) microg/ml, the difference being significant (P=0.0001). Serum lactoferrin levels were not significantly associated with type 2 reactions (P=0.613). Serum lactoferrin was significantly associated with age (P = 0.006), duration of the disease (P=0.0001), DDS monotherapy (P =0.007), deformity (P= 0.005), average bacterial index (BI) (P=0.01) and smear positivity (P=0.0001), orbicularis oculi weakness (P= 0.001), lagophthalmos (P = 0.002), corneal opacity (P = 0.001) and cataract (P=0.004) in simple regression analysis. All these variables, with the exception of smear positivity (P=0.019), lost their significance (P>0.05) when analysed using multiple regression. Serum lactoferrin showed poor association with type 1 (P = 0.286) and type II reactions (P = 0.613) and iridocyclitis (P = 0.207). We conclude that serum lactoferrin is strongly and inversely associated with increasing BI but does not show significant association with type 2 reactions.

Adolescent↗

PubMed1992

[Determination of lactoferrin in the diagnosis of pancreatopathy in patients with chronic kidney failure].

The authors investigated in patients with renal disease the lactoferrin content in duodenal aspirate. The aspirate was obtained after previous stimulation of the pancreas with pancreozymin. Lactoferrin estimation is described in the literature as a sensitive examination of changes of exocrine pancreatic secretion. The authors provided evidence that by assessing lactoferrin it is possible to detect initial changes of reduced exocrine pancreatic capacity already in subjects who are on the waiting list of chronic intermittent haemodialyzation programmes (CHIDP); maximum increase of the lactoferrin content in the duodenal aspirate corresponds with the severity of chronic renal failure. Transplantation of the kidneys leads to normalization of the amount of lactoferrin secreted by the pancreas which is evidence of normalization of pancreatic secretion. In patients with chronic renal failure lactoferrin is a sensitive marker of developing uraemic pancreatopathy.

Humans↗

PubMed1991

Binding and endocytosis of apo- and holo-lactoferrin by isolated rat hepatocytes.

We characterized binding and endocytosis of 125I-bovine lactoferrin by isolated rat hepatocytes. Iron-depleted (apo-Lf), approximately 30% saturated (Lf), and iron-saturated (holo-Lf) lactoferrin were used. At 4 degrees C, cells bound 125I-apo-Lf and 125I-holo-Lf with nearly identical apparent first order kinetics (t1/2 = approximately 42 min). Holo-Lf and apo-Lf competed with each other for binding. Hepatocytes bound lactoferrin optimally at pH greater than or equal to 7 but poorly at pH less than or equal to 6. Ca2+ (greater than or equal to 100 microM) enhanced Lf binding to cells, and holo-Lf remained monomeric with Ca2+ present as determined by gel filtration chromatography. With Ca2+, cells exhibited approximately 10(6) high affinity sites (Kd approximately 20 nM) and approximately 10(7) low affinity sites (Kd approximately 700 nM) for both apo- and holo-Lf. Without Ca2+, cells bound 125I-holo-Lf by the low affinity component only. EGTA and dextran sulfate together released greater than or equal to 90% 125I-Lf prebound at 4 degrees C, but individually removed separate populations of surface-bound 125I-Lf. Cells bound 125I-Lf in a Ca(2+)-dependent manner with dextran sulfate present. We conclude that the high affinity but not the low affinity sites require Ca2+; only the low affinity sites are dextran sulfate-sensitive. Neither transferrin nor asialo-orosomucoid blocked lactoferrin binding to hepatocytes. Some cationic proteins but not others inhibited lactoferrin binding. At 37 degrees C, hepatocytes endocytosed 125I-apo-Lf and 125I-holo-Lf similarly, and hyperosmolality (greater than 500 mmol/kg) blocked uptake by approximately 90%. These data support the proposal that hepatocytes regulate blood lactoferrin concentration by receptor-mediated endocytosis.

Animals↗

PubMed1991

Characterization of estrogen-responsive mouse lactoferrin promoter.

Mouse lactoferrin is expressed in a variety of tissues under different types of control. To understand how molecular mechanisms govern the mode of lactoferrin expression, we isolated and characterized the 5'-flanking region of the lactoferrin gene. Several clones containing lactoferrin gene fragments were isolated from a mouse (129/J) genomic library including clone lambda J14, which contains a 7.5-kilobase pair 5'-flanking sequence. Sequence analysis of the region flanking the transcription initiation site revealed the following: a TATA-like sequence, two CAAT boxes, three GC boxes including one within the first intron, an AP2 site, seven PU boxes, an AC-rich region, a B1 sequence, and an estrogen-responsive element consensus sequence over-lapping with a chicken ovalbumin upstream promoter-binding element. Footprinting analysis demonstrated that several regions, including the putative estrogen-responsive element region, in the 5'-flanking sequence were protected from DNase I digestion. Promoter fragments were cloned into a chloramphenicol acetyltransferase receptor plasmid to study functional activity. The mouse lactoferrin gene promoter was active in human endometrium carcinoma RL 95-2 cells and in rat glioma C6 cells. Multiple upstream elements modulated the basal transcriptional promoter activity. The transcription level directed by this minimal promoter was controlled by both positive (between -1739 and -922) and negative (between -2644 and -1739, and between -589 and -291) regulatory sequences. A tissue-specific regulatory sequence was critical for the establishment of lactoferrin expression in human endometrium carcinoma cells, but not in rat glioma cells located between -1739 and -922. Reporter plasmid 0.6 mL14-CAT, containing the estrogen-responsive element sequence, was estrogen-responsive in the presence of estrogen receptor in human endometrium carcinoma RL 95-2 cells.

Amino Acid Sequence↗

PubMedDate not supplied

The role of lactoferrin in the nonspecific immune response on the ocular surface.

Lactoferrin is an iron binding glycoprotein which is abundantly present in human tear fluid. It is also present in other secretions and in the specific granules of the polymorphonuclear leucocyte. The main biological properties of lactoferrin can be ascribed to its very strong binding of iron cations. Receptors for lactoferrin have been found in the intestinal brush border, suggesting that it may play a role in iron absorption from the gut. Macrophages also have a receptor for lactoferrin, which are possibly involved in the transfer of iron to ferritin. More important may be the fact that deprivation of iron from the gut or from the ocular surface limits the availability of iron to microorganisms and thus exerts firm control of the bacterial flora at these sites. Sequestration of iron by this protein can also inhibit the iron catalyzed production of hydroxyl radicals thereby protecting mucosal surfaces from oxydative damage. Lactoferrin has furthermore been shown to play a role in myelopoiesis, primary antibody response, lymphocyte proliferation, cytokine production, ADCC, NK cell activity, and regulation of complement activation. The observations described above indicate that lactoferrin, besides control of the bacterial flora, may regulate inflammatory reactions occurring on the ocular surface.

Animals↗

PubMedDate not supplied

[Quantitative immunoenzyme determination of lactoferrin in the serum and plasma].

A procedure for quantitative estimation of lactoferrin is developed using the "sandwich" type of immunoenzymatic assay. Preparation of lactoferrin was purified from women colostrum by means of ion exchange chromatography; the sorbent (a ligand-containing complex of lactoferrin) was synthesized; the antibody conjugate against lactoferrin and peroxidase from horseradish was prepared; optimal conditions of the immunoenzymatic assay were selected. Concentration of lactoferrin in donor blood serum or plasma constituted 0.5-3.3 mg/ml; distinct alterations of the lactoferrin content were not found in blood of patients maintained on artificial circulation or in the blood used for transfusion.

Humans↗

PubMed1988

Biosynthesis and processing of lactoferrin in bone marrow cells, a comparison with processing of myeloperoxidase.

The processing and intracellular transport of lactoferrin of the neutrophil specific granules was investigated by biosynthetic labeling with (14C)leucine of bone marrow cells from healthy individuals and patients with chronic myeloid leukemia. Lactoferrin was precipitated with antilactoferrin serum and the immunoprecipitates were analyzed by sodium dodecyl sulfate (SDS), polyacrylamide gel electrophoresis (PAGE) followed by fluorography. In contrast to myeloperoxidase of azurophil granules, lactoferrin was not synthesized as a larger precursor, and it was not found to be phosphorylated. The transfer to granules of newly synthesized lactoferrin was demonstrated in pulse-chase labeling experiments followed by centrifugation of cell homogenate in a Percoll gradient. Monensin, which exchanges protons for Na+ and NH4+ cation, blocked the transfer completely, indicating a need for acidification mechanisms. Unlike myeloperoxidase, newly synthesized lactoferrin rapidly became resistant to endoglycosidase H, indicating a transport through the medial and transcisternae of the Golgi apparatus with conversion of "high mannose" to "complex" oligosaccharide side chains. Intracellular transfer of some major neutrophil azurophil and specific granule constituents is obviously regulated differently. Lactoferrin seems to be processed like proteins destined for secretion, while myeloperoxidase is processed more or less like lysosomal enzymes.

Ammonium Chloride↗

PubMed1988

Enhanced antimicrobial activity of lactoferrin by binding to the bacterial surface.

In order to elucidate the mechanisms involved in the antibacterial activity of lactoferrin, quantitative determinations of siderophore production and lactoferrin adsorption on various bacterial species were performed. The binding of lactoferrin took place both on Gram-positive and Gram-negative species and occurred with bacterial cells grown in stress or in excess of iron. The different degrees of sensitivity to lactoferrin observed could not be directly related to the type and amount of siderophores produced. However, it was possible to find a correlation between the capacity of some strains to bind lactoferrin and their sensitivity to this protein. These data suggest that the binding of lactoferrin on the cell surface can result in an antibacterial activity additional to iron witholding.

Adsorption↗

PubMed1988

[Comparative immunohistochemical study of lysozyme and lactoferrin in human neonate and adult parotid glands].

Lysozyme and lactoferrin, substances of the non-specific defense system of the salivary glands, were studied in normal human parotid glands of neonates and adults using the immunoperoxidase method. To our knowledge, the immunohistochemical detection and distribution of lysozyme and lactoferrin in neonate parotid glands have not been previously reported. In neonate parotid glands, a monotonous positive reaction for lysozyme was found in the acini, in the intercalated ducts and in a few cells of large ducts. On the contrary, lysozyme was observed mainly in the intercalated ducts of the adult parotid glands. Three staining patterns for lactoferrin were found in neonate parotid glands. The first pattern was identical to that of lysozyme in neonates, the second was similar to that of lactoferrin in adults, and in the third extremely few acinar and intercalated duct cells were positive. In adult parotid glands, lactoferrin was detected in groups of acini and intercalated ducts and rarely striated duct cells. In adult parotid glands, our findings are discussed in correlation with those of other investigators. The results of our study indicate that lysozyme and lactoferrin have an important role in the defense mechanism of neonate parotid gland. There is also a distinct immunohistochemical difference between neonate and adult parotid gland. Since it is known that there is a morphological differentiation of the parotid gland postnatally, it is presumably suggested that an immunohistochemical differentiation also occurs.

Adult↗