New Data on Lactoferrin, the Iron-Binding Protein of Secretions

Masson, Pierre; Heremans, J. F.; Schonne, E.; Crabbé, Pierre

doi:10.1016/b978-0-08-013348-5.50083-1

Cited by 84 publications

(102 citation statements)

References 9 publications

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“…Since lactoferrin is a powerful chelator of iron (2, 6, 7) as well as of copper (8), it is tempting to speculate that this protein may be a valuable adjunct of lysozyme in the defense against bacterial invasion. Moreover, lactoferrin is by itself endowed with bacteriostatic properties which it owes to its iron-chelating capacity (21,23,28). It would also be interesting to clarify the possible relationship of lactoferrin with "phagocytin", the antimicrobial factor from polymorphonuclear leukocytes described by Hirsch (20).…”

Section: Discussionmentioning

confidence: 99%

“…In previous publications it has been reported that lactoferrin is present in the epithelial cells of glandular acini from human bronchi (23) and submaxillary glands (21), and that this protein is actively synthesized by tissue cultures from human rectal mucosa and uterine cervix (19).…”

Section: Discussionmentioning

confidence: 99%

“…The procedure employed for the isolation of human lactoferrin has been reported elsewhere (21). A detailed description on the chemical properties of guinea pig lactoferrin is in preparation.…”

Section: Analyt~almentioning

confidence: 99%

“…Recent investigations on guinea pig tissues have however shown that the spleen and bone marrow are rich sources of lactoferrin (unpublished). Furthermore, immunohistochemical observations on certain human tissues, the uterine cervix for example, suggest that glandular epithelia are not the only sites of origin for lactoferrin in external secretions and that certain blood cells may also be implicated in the production of this protein (19).…”

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confidence: 99%

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Lactoferrin, an Iron-Binbing Protein Ni Neutrophilic Leukocytes

Masson¹,

Heremans²,

Schonne³

1969

The Journal of Experimental Medicine

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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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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Analyt~almentioning

confidence: 99%

mentioning

confidence: 99%

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Lactoferrin, an Iron-Binbing Protein Ni Neutrophilic Leukocytes

Masson¹,

Heremans²,

Schonne³

1969

The Journal of Experimental Medicine

Self Cite

650

295

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“…The distribution of lactoferrin, studied mainly by immunological methods appears to vary considerably between species (Teng et al, 1989;Masson & Heremans, 1966;Roberts & Boursnell, 1975) with conflicting data that presumably reflects both experimental sensitivity (Pentecoste et al, 1987;Teng et al, 1989) and hormonal status of certain tissues. A 300-fold induction with oestrogen was observed in mouse uterus with virtually undetectable amounts in the rat organ (Pentecoste et al, 1987).…”

Section: Discussionmentioning

confidence: 99%

Isolation of a lactoferrin cDNA clone and its expression in human breast cancer

Campbell

Skilton²,

Coombes³

et al. 1992

Br J Cancer

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Summary A cDNA library constructed from mRNA from a human breast carcinoma metastasis was screened with a polyclonal antibody to deglycosylated human milk fat globule membrane, resulting in the isolation of eight clones from a total of 105 plaques. One of these (J16) was identified as lactoferrin. It was highly expressed (as a 2.5 Kb mRNA) in lactating breast and in both normal resting tissue taken from adjacent to carcinoma or from reduction mammoplasties. Immunoreactive lactoferrin was localised to ductal cells and their secretions in both normal and mildly hyperplastic ducts. In a normal tissue screen J16 was highly expressed in stomach, poorly in skin and lymphocytes and absent from other organs examined. It was variably expressed in 33/59 invasive primary breast tumours; lactoferrin protein in these was heterogeneously distributed in epithelial tumour foci. Presence of J16 was inversely related to expression of oestrogen receptor protein (P = 0.0001). There was no significant relationship to other clinical parameters. We also found immunoreactivity in 20/41 (49%) cases of ductal carcinoma in situ. Expression was not observed in any breast or gastric cell line examined. Thus lactoferrin appears to be down regulated in some forms of cancer. The presence of lactoferrin could be a contraindication for effective endocrine therapy.

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The relationship of lactoferrin to the anemia of renal cell carcinoma

Loughlin

Gittes

Partridge

et al. 1987

Cancer

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This study was designed to examine whether lactoferrin, a glycoprotein contained in neutrophils which binds free iron, mediates the anemia associated with renal cell carcinoma. Preoperative hematocrit, urinalysis, serum iron, total iron binding capacity, and ferritin levels were obtained in 24 patients with hypernephroma. At the time of radical nephrectomy, a tumor specimen was obtained from all 24 patients and corresponding normal renal tissue was obtained from eight patients. Fifteen patients had low serum iron, whereas nine patients had normal serum iron. All tissue samples were snap frozen at the time of surgery and were subsequently sectioned into 3-microns slices using the cryostat. Then all the sectioned specimens were stained with FITC (fluorescein isothiocyanate) and peroxidase conjugated rabbit derived anti-human lactoferrin. Ten of the 15 patients with low serum iron had positive anti-lactoferrin staining in both the FITC and peroxidase systems. None of the tumors from patients with normal serum iron and none of the normal renal parenchyma exhibited positive anti-lactoferrin uptake. Stains for iron in the bone marrow of two patients with low serum iron showed increased iron stores. These studies suggest that lactoferrin mediates the anemia often seen in association with renal cell carcinoma.

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New Data on Lactoferrin, the Iron-Binding Protein of Secretions

Cited by 84 publications

References 9 publications

Lactoferrin, an Iron-Binbing Protein Ni Neutrophilic Leukocytes

Lactoferrin, an Iron-Binbing Protein Ni Neutrophilic Leukocytes

Isolation of a lactoferrin cDNA clone and its expression in human breast cancer

The relationship of lactoferrin to the anemia of renal cell carcinoma

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