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Receptor-mediated transcytosis of lactoferrin through the blood-brain barrier

Abstract : Lactoferrin (Lf) is an iron-binding protein involved in host defense against infection and severe inflammation; it accumulates in the brain during neurodegenerative disorders. Before determining Lf function in brain tissue, we investigated its origin and demonstrate here that it crosses the blood-brain barrier. An in vitro model of the blood-brain barrier was used to examine the mechanism of Lf transport to the brain. We report that differentiated bovine brain capillary endothelial cells exhibited specific high (Kd = 37.5 nM; n = 90,000/cell) and low (Kd = 2 μM; n = 900,000 sites/cell) affinity binding sites. Only the latter were present on nondifferentiated cells. The surface-bound Lf was internalized only by the differentiated cell population leading to the conclusion that Lf receptors were acquired during cell differentiation. A specific unidirectional transport then occurred via a receptor-mediated process with no apparent intraendothelial degradation. We further report that iron may cross the bovine brain capillary endothelial cells as a complex with Lf. Finally, we show that the low density lipoprotein receptor-related protein might be involved in this process because its specific antagonist, the receptor-associated protein, inhibits 70% of Lf transport.
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Contributor : Wilfried Déplanques Connect in order to contact the contributor
Submitted on : Wednesday, November 3, 2010 - 4:34:36 PM
Last modification on : Wednesday, March 23, 2022 - 3:50:31 PM


  • HAL Id : hal-00531751, version 1



Carine Fillebeen, Laurence Descamps, Marie-Pierre Dehouck, Laurence Fenart, Monique Benaissa, et al.. Receptor-mediated transcytosis of lactoferrin through the blood-brain barrier. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1999, 274 (11), p. 7011-7017. ⟨hal-00531751⟩



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