Skip to main content
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1969 Sep 1;130(3):643–658. doi: 10.1084/jem.130.3.643

LACTOFERRIN, AN IRON-BINBING PROTEIN NI NEUTROPHILIC LEUKOCYTES

P L Masson 1, J F Heremans 1, E Schonne 1
PMCID: PMC2138704  PMID: 4979954

Abstract

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.

Full Text

The Full Text of this article is available as a PDF (984.6 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BLANC B., BUJARD E., MAURON J. The amino acid composition of human and bovine lactotransferrins. Experientia. 1963 Jun 15;19:299–301. doi: 10.1007/BF02150417. [DOI] [PubMed] [Google Scholar]
  2. BLANC B., ISLIKER H. [Isolation and characterization of the red siderophilic protein from maternal milk: lactotransferrin]. Bull Soc Chim Biol (Paris) 1961;43:929–943. [PubMed] [Google Scholar]
  3. Bennett W. E., Cohn Z. A. The isolation and selected properties of blood monocytes. J Exp Med. 1966 Jan 1;123(1):145–160. doi: 10.1084/jem.123.1.145. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. DERECHIN S. S., JOHNSON P. Red proteins from bovine milk. Nature. 1962 May 5;194:473–474. doi: 10.1038/194473a0. [DOI] [PubMed] [Google Scholar]
  5. GORDON W. G., GROVES M. L., BASCH J. J. BOVINE MILK "RED PROTEIN": AMINO ACID COMPOSITION AND COMPARISON WITH BLOOD TRANSFERRIN. Biochemistry. 1963 Jul-Aug;2:817–820. doi: 10.1021/bi00904a033. [DOI] [PubMed] [Google Scholar]
  6. HIRSCH J. G. Phagocytin: a bactericidal substance from polymorphonuclear leucocytes. J Exp Med. 1956 May 1;103(5):589–611. doi: 10.1084/jem.103.5.589. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Loisillier F., Burtin P., Grabar P. Isolement et caractérisation de l'auto-antigène responsable de la formation d'auto-anticorps chez les malades atteints de lésions mammaires (cancéruses ou non) Ann Inst Pasteur (Paris) 1968 Nov;115(5):829–840. [PubMed] [Google Scholar]
  8. MONTREUIL J., MULLET S. [Isolation of lactosiderophilin from human milk]. C R Hebd Seances Acad Sci. 1960 Feb 29;250:1736–1737. [PubMed] [Google Scholar]
  9. MONTREUIL J., TONNELAT J., MULLET S. [Preparation and properties of lactosiderophilin (lactotransferrin) of human milk]. Biochim Biophys Acta. 1960 Dec 18;45:413–421. doi: 10.1016/0006-3002(60)91478-5. [DOI] [PubMed] [Google Scholar]
  10. Mancini G., Carbonara A. O., Heremans J. F. Immunochemical quantitation of antigens by single radial immunodiffusion. Immunochemistry. 1965 Sep;2(3):235–254. doi: 10.1016/0019-2791(65)90004-2. [DOI] [PubMed] [Google Scholar]
  11. Masson P. L., Heremans J. F. Metal-combining properties of human lactoferrin (red milk protein). 1. The involvement of bicarbonate in the reaction. Eur J Biochem. 1968 Dec 5;6(4):579–584. doi: 10.1111/j.1432-1033.1968.tb00484.x. [DOI] [PubMed] [Google Scholar]
  12. Masson P. L., Heremans J. F., Prignot J. J., Wauters G. Immunohistochemical localization and bacteriostatic properties of an iron-binding protein from bronchial mucus. Thorax. 1966 Nov;21(6):538–544. doi: 10.1136/thx.21.6.538. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Montreuil J., Spik G., Monsigny M., Descamps J., Biserte G., Dautrevaux M. Etude comparée de la composition en oses et en amino-acides de la transferrine et de la lactotransferrine humaines. Experientia. 1965 May 15;21(5):254–256. doi: 10.1007/BF02297009. [DOI] [PubMed] [Google Scholar]
  14. Oram J. D., Reiter B. Inhibition of bacteria by lactoferrin and other iron-chelating agents. Biochim Biophys Acta. 1968 Dec 23;170(2):351–365. doi: 10.1016/0304-4165(68)90015-9. [DOI] [PubMed] [Google Scholar]
  15. Phillips M. E., Thorbecke G. J. Studies on the serum proteins of chimeras. I. Identification and study of the site of origin of donor type serum proteins in adult rat-into-mouse chimeras. Int Arch Allergy Appl Immunol. 1966;29(6):553–contd. [PubMed] [Google Scholar]
  16. REPASKE R. Lysis of gram-negative bacteria by lysozyme. Biochim Biophys Acta. 1956 Oct;22(1):189–191. doi: 10.1016/0006-3002(56)90240-2. [DOI] [PubMed] [Google Scholar]
  17. Spik G., Montreuil J. Etudes comparatives de la structure de la transferrine et de la lactotransferrine humaines. "Finger printing" des hydrolysats protéasiques des deux glycoprotéides. C R Seances Soc Biol Fil. 1966;160(1):94–98. [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES