Isolation of an Iron-Containing Red Protein from Human Milk.

Johanson, Bengt; Virtanen, Artturi I.; Tweit, Robert C.; Dodson, R. M.

doi:10.3891/acta.chem.scand.14-0510

Cited by 274 publications

(110 citation statements)

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“…Lactoferrin was first isolated by Sorensen andSorensen from bovine milk in 1939. In 1960 it was concurrently determined to be the main iron binding protein in human milk by three independent laboratories (Groves, 1960;Johanson, 1960;Montreuil et al, 1960).…”

Section: Introductionmentioning

confidence: 99%

Lactoferrin: a review

Adlerova¹,

Bartošková²,

Faldyna³

2008

Vet. Med.

265

217

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This review discusses the biological properties of the glycoprotein lactoferrin. Lactoferrin has been identified in secretions from exocrine glands and in specific granules of neutrophils. After degranulation, neutrophils become the main source of lactoferrin in blood plasma. Lactoferrin possesses various biological functions, including roles in iron metabolism, cell proliferation and differentiation, and antibacterial, antiviral, and antiparasitic activity. Many of these functions do not appear to be connected with its iron binding ability. Of late, lactoferrin concentrations have been measured mostly in humans but also in some other species. However, the relationship between its concentration and physiological or pathological effects on body functions is not yet well characterised.

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Section: Introductionmentioning

confidence: 99%

Lactoferrin: a review

Adlerova¹,

Bartošková²,

Faldyna³

2008

Vet. Med.

265

217

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“…By their amino acid composition (14) they are clearly related, although they fail to show any immunological cross-reaction unless denatured (16). Lactoferrin further differs from transferrin by its affinity for iron being largely retained at pH values below 4.0 (11)(12)(13)17), whereas under such conditions transferrin completely releases its iron. Yet another difference resides in the histological distribution of the two proteins.…”

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confidence: 99%

The Involvement of Lactoferrin in the Hyposideremia of Acute Inflammation

Snick

Masson

Heremans

1974

The Journal of Experimental Medicine

280

129

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The hyposideremia of inflammation was found to be based on a three-step mechanism involving lactoferrin, the iron-binding protein from the specific granules of neutrophilic leukocytes. (a) Lactoferrin is Released from Neutrophils in an Iron-Free Form. When phagocytosis was induced in neutrophils by zymosan or bacteria, lactoferrin was recovered in the incubation medium together with other constituents of the specific granules, such as alkaline phosphatase and lysozyme. Lactoferrin extracted from leukocytes was able to bind the amount of iron corresponding to its theoretical iron-binding capacity. After injection of endotoxin into rats, lactoferrin was detected in various tissues where it was normally absent, or in the plasma when the reticuloendothelial system (RES) had previously been blocked by injections of India ink or aggregated albumin. (b) Lactoferrin is Able to Remove the Iron from Transferrin. Significant exchange of iron from transferrin to lactoferrin was observed in vitro only at a pH below 7.0 or in the presence of a high concentration of citrate. However, the fast elimination of lactoferrin in vivo, when saturated with iron, might account for the observed transfer of iron to endogenous or administered apolactoferrin. Intravenous injection of human apolactoferrin into rats caused a marked decrease of the plasma iron level. The kinetics of this process, as well as controls with other proteins, ruled out the possibility of a secondary inflammatory effect due to phlogogenic contaminants. (c) Fe-Lactoferrin is Taken-up by the RES. By immunofluorescence, lactoferrin was shown to be bound and ingested by monocytes. The rate of elimination of human Fe-lactoferrin injected into rats was particularly fast when compared to that of human apolactoferrin, succinylated Fe-lactoferrin, or other human proteins. Blockade of the RES slowed down the rate of clearance of Fe-lactoferrin and was also found to retard the elimination of endogenous rat lactoferrin released by endotoxin. These experiments suggest the existence of specific receptors for Fe-lactoferrin on the membrane of macrophages.

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“…It has recently been isolated and its physicochemical features were described by several workers who investigated the bovine component (2,3), as well as its human homologue (4)(5)(6)(7)(8). This protein has been given various names, such as lactoferrin (9), lactotransferrin (10), lactosiderophilin (10), or ekkrinosiderophilin (11).…”

mentioning

confidence: 99%

Lactoferrin, an Iron-Binbing Protein Ni Neutrophilic Leukocytes

Masson¹,

Heremans²,

Schonne³

1969

The Journal of Experimental Medicine

657

295

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Lactoferrin, an iron-binding protein previously shown to occur in many external secretions, is identified as one of the major proteins present in human and guinea pig neutrophilic polymorphonuclear leukocytes. The identification of this protein in leukocyte extracts was based upon a comparison of its electrophoretic, antigenic, and iron-combining properties with the corresponding properties of the same protein isolated from human and guinea pig milk. Immunochemical quantitations showed that lactoferrin occurs in human neutrophilic leukocytes at the concentration of 3 µg per 106 cells. Tissue cultures from guinea pig bone marrow and spleen actively synthesized the protein, as shown both by net production of lactoferrin and incorporation of labeled amino acids into the protein. Immunohistochemical data indicate that lactoferrin first appears in myeloid cells at the stage of the promyelocyte.

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Isolation of an Iron-Containing Red Protein from Human Milk.

Cited by 274 publications

References 0 publications

Lactoferrin: a review

Lactoferrin: a review

The Involvement of Lactoferrin in the Hyposideremia of Acute Inflammation

Lactoferrin, an Iron-Binbing Protein Ni Neutrophilic Leukocytes

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