Inability to detect transferrin receptors on P. falciparum parasitized red cells

Simeon Pollack, V. Schnelle

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

The mechanism by which P. falciparum takes up iron from transferrin has been explored. Binding of 125I labelled transferrin to parasitized red cells at 37°C is two-fold greater than to control cells; at 0°C there is no significant difference. The binding is non-specific as judged from the following: it is not saturable; it is not limited to transferrin as lactoferrin (which has iron binding domains) and bovine serum albumin (which does not) also bind in excess to parasitized red cells. A transferrin receptor complex could not be demonstrated when parasitized red cells, to which 125I transferrin was bound, were solubilized in Triton X100. Previous observation showed that uptake of transferrin iron by parasitized red cells is not accompanied by equimolar uptake of transferrin protein. We therefore suggest that non-specifically bound transferrin is endocytosed, that the protein is degraded and the iron selectively retained.

Original languageEnglish (US)
Pages (from-to)125-129
Number of pages5
JournalBritish Journal of Haematology
Volume68
Issue number1
StatePublished - 1988

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Transferrin Receptors
Transferrin
Iron
Lactoferrin
Octoxynol
Bovine Serum Albumin
Endocytosis
Proteins
Observation

ASJC Scopus subject areas

  • Hematology

Cite this

Inability to detect transferrin receptors on P. falciparum parasitized red cells. / Pollack, Simeon; Schnelle, V.

In: British Journal of Haematology, Vol. 68, No. 1, 1988, p. 125-129.

Research output: Contribution to journalArticle

Pollack, Simeon ; Schnelle, V. / Inability to detect transferrin receptors on P. falciparum parasitized red cells. In: British Journal of Haematology. 1988 ; Vol. 68, No. 1. pp. 125-129.
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