lactoferrin and Anemia--Hypochromic

Topics: Anemia, Hypochromic; Animals; Bacteria; Bacterial Infections; Bacterial Outer Membrane Proteins; Binding, Competitive; Biological Transport; Disease Susceptibility; Hemin; Humans; Hydroxamic Acids; Hydroxybenzoates; Iron; Lactoferrin; Macromolecular Substances; Protein Binding; Receptors, Cell Surface; Species Specificity; Transferrin; Virulence

The transferrins are iron-binding proteins with molecular weights of around 80,000, which interact with a maximum of two ferric atoms per each protein molecule. The best known transferrins are the serotransferrins from animal sera, lactoferrins from milk, and conalbumin from egg-white. The iron-deficient transferrins will inhibit the growth of certain bacteria and fungi by making iron unavailable for bacterial metabolism. Such activity is abolished if the transferrin is saturated with iron. Many organisms can produce small molecular-weight iron-binding compounds called siderophores that can successfully utilize the iron sequestered by the transferrins. Such organisms are very virulent. Overwhelming evidence is now available to indicate that the transferrins play an important role in mammalian host-defense mechanisms. Thus, iron injections into animals infected with virulent bacteria result in increased death rates, and parenteral iron administration to human infants predisposes them to fatal septicemia. On the other hand, in cases of systemic infection, the organism responds by lowering its total serum iron, so as to make the serotransferrin present less saturated with iron. This phenomenon is called nutritional immunity. The iron apparently moves into the storage tissues from the circulation, and furthermore, it is withheld from circulation by the reticuloendothelial system. Laboratory results in such cases indicate low total serum iron levels and high unsaturated iron-binding activity values, thus increasing the bacteriostatic effects of the serotransferrins. Increased lactoferrin levels are observed in the milks of mastitic cattle.

Topics: Anemia, Hypochromic; Animals; Bacteria; Bacterial Infections; Carrier Proteins; Conalbumin; Female; Fungi; Humans; Hydroxamic Acids; Immunity, Innate; Iron; Iron Chelating Agents; Iron-Binding Proteins; Lactoferrin; Leukemia; Milk, Human; Mycoses; Pregnancy; Siderophores; Transferrin; Transferrin-Binding Proteins

Iron, as participant of many biological processes is a prerequisite for life. Uptake, internal transport and storage by organisms is handled by highly specialized chemical systems endowed with strong metal binding affinities. Apart from the homeostatic function of iron-binding compounds they appear of significance for inter-species interactions. Thus, by tight binding transferrin withholds the iron from invading microorganisms required for their optimal growth. This bacteriostatic property of the iron transport protein is however partially overcome by small molecular substances synthesized by bacteria and successfully competing for the metal. The balance of such interaction is a complex one. Yet, strong evidence points to the crucial importance of the amount of iron offered by a host to infecting agents for determining the fate of bacterial disease.

Topics: Anemia, Hypochromic; Animals; Bacteria; Bacterial Infections; Biological Transport; Guinea Pigs; Humans; Iron; Lactoferrin; Mice; Rats; Siderosis; Transferrin

Topics: Anemia, Hypochromic; Animals; Bacteria; Blood Proteins; Bone Marrow; Diet; Female; Fungi; Hemochromatosis; Hemosiderosis; Humans; Intestinal Absorption; Intestinal Mucosa; Iron; Lactoferrin; Liver; Male; Metabolism, Inborn Errors; Mice; Rabbits; Rats; Reticulocytes; Spleen; Transferrin

Lactotransferrin was highly purified from lysates of human neutrophilic leucocytes by immuno-affinity chromatography. A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues. Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type. These results question a previously proposed mechanism for hyposideraemia in which the leucocyte lactotransferrin was involved and in which the fucose residues played a key role.

Topics: Anemia, Hypochromic; Carbohydrate Sequence; Fucose; Humans; Hydrazines; Lactoferrin; Lactoglobulins; Leukocytes; Magnetic Resonance Spectroscopy; Mass Spectrometry; Milk, Human; Molecular Sequence Data; Oligosaccharides; Polysaccharides

In healthy subjects normal plasmalactoferrin (PLf) concentrations were found to be 0.206 +/- 0.06 mg/l in 49 men and 0.148 +/- 0.06 mg/l in 62 women. A highly significant correlation of PLf with the number of circulating neutrophils (PMN) and a PLf/PMN relationship suggesting proportionality was demonstrated. Among 73 patients absolute PLf concentrations were significantly increased in septicemia, cirrhosis of the liver and tumors with liver metastases, decreased in localized infection, tumors without liver involvement, iron deficiency and acute hepatitis B, and normal in acute myocardial infarction. The PLf/PMN ratio, on the other hand, was normal in liver cirrhosis, hepatitis B and in a part of the patients with septicemia and tumor disease with liver involvement. The ratio was increased in a part of the septicemic patients, and decreased in the remaining disease types. Positive PLf/PMN correlations were found in myocardial infarction, septicemia and liver cirrhosis, whereas a very close, negative correlation existed in acute hepatitis B. These findings are discussed on the basis of existing knowledge on lactoferrin physiology, the intravascular fate of PMN and the RES function.

Topics: Anemia, Hypochromic; Female; Hepatitis B; Humans; Lactoferrin; Lactoglobulins; Leukocyte Count; Liver Cirrhosis; Liver Neoplasms; Male; Myocardial Infarction; Neutrophils; Reference Values; Sepsis; Sex Factors

Lactoferrin is an iron-binding protein present in high concentrations in human milk. The efficacy of supplementing iron bound to lactoferrin to iron-deficient and iron-sufficient young mice was evaluated in comparison with supplementation of iron as iron chloride. Mice fed a nonsupplemented milk diet (approximately 1 mg Fe/L) for 4 weeks had a microcytic, hypochromic anemia and low tissue iron concentrations. Iron supplementation of the diet with lactoferrin-iron, or iron chloride at a level of 5 mg Fe/L prevented the anemia and resulted in tissue iron levels similar to levels found for mice fed a stock commercial diet. There was no significant difference in any of the parameters analyzed between the groups of mice receiving the two iron supplements following a diet deficient in iron. Apolactoferrin when supplemented to the diet had no negative effect on the iron status of the mice. These results show that lactoferrin may be a useful vehicle for supplementation of iron.

Topics: Anemia, Hypochromic; Animals; Biological Availability; Cattle; Chlorides; Female; Ferric Compounds; Food, Fortified; Hematocrit; Iron; Lactoferrin; Lactoglobulins; Mice; Milk; Weaning

In order to evaluate the diagnostic and pathogenetic importance of s-ferritin and p-lactoferrin in the anemia of rheumatoid arthritis (RA), 38 patients were examined. Twenty-one out of 38 randomly selected anemic patients with classical or definite RA had iron deficiency, as estimated from the iron content in stained bone marrow aspiration. S-ferritin concentrations below 60 micrograms per litre had sensitivity and a specificity for iron deficiency of 86% and 88%, respectively, which was much better than such commonly used variables as s-iron, p-transferrin, MCV, and MCHC. Although this cut-off level is higher than in patients without inflammatory disease, s-ferritin was not correlated to disease activity. In 7 out of 8 patients, the s-ferritin level rose during iron therapy. P-lactoferrin values were within the normal range and did not vary with the anemia or with disease activity. Thus p-lactoferrin appears to be of no pathogenetic importance in the anemia of RA.

Topics: Adult; Aged; Anemia, Hypochromic; Arthritis, Rheumatoid; Bone Marrow Examination; Female; Ferritins; Ferrous Compounds; Humans; Lactoferrin; Male; Middle Aged; Radioimmunoassay; Random Allocation

Topics: Anemia, Hypochromic; Animals; Cattle; Escherichia coli Infections; Female; Food, Fortified; Gastroenteritis; Humans; Infant; Infant Nutritional Physiological Phenomena; Infant, Newborn; Infant, Premature, Diseases; Iron; Lactoferrin; Milk; Milk, Human; Protein Binding

Lactoferrin (LF), the iron-binding protein of external secretions and neutrophilic polymorphonuclear leukocytes (PMN), was studied in 27 patients during granulocytosis caused by acute inflammation and in disorders without granulocytosis (iron deficiency anemia, iron overload and liver diseases). During granulocytosis the LF concentration of PMN was significantly lower than in controls (p less than 0.001). This difference proved to be related to the number of PMN. A relation between the LF concentration of PMN and iron metabolism could be demonstrated: loss of iron by blood donation is accompanied by a significant decrease in the LF concentration in PMN, whereas iron therapy in patients with iron deficiency anemia is accompanied by a significant increase in the LF concentration in PMN.

Topics: Anemia, Hypochromic; Blood Transfusion; Female; Fluorescent Antibody Technique; Hepatitis; Humans; Immunodiffusion; Inflammation; Iron; Lactoferrin; Lactoglobulins; Leukocytosis; Liver Cirrhosis; Neutrophils

Topics: Anemia; Anemia, Hypochromic; Humans; Infections; Intestine, Small; Iron; Lactoferrin; Lactoglobulins; Milk, Human; Neutrophils; Phagocytosis

Topics: Anemia, Hypochromic; Biological Transport; Bone Marrow; Ferritins; Humans; Intestinal Absorption; Intestinal Mucosa; Iron; Lactoferrin; Liver; Spleen; Transferrin

Topics: Age Factors; Anemia, Hypochromic; Bacteria; Bacterial Infections; Humans; Infant Nutritional Physiological Phenomena; Infant, Newborn; Infant, Premature, Diseases; Iron; Lactoferrin; Milk, Human

Topics: Anemia, Hypochromic; Animals; Bacteria; Bacterial Infections; Binding, Competitive; Fungi; Humans; Immunity; Iron; Lactoferrin; Protein Binding; RNA, Bacterial; Transferrin