Lactoferrin from milk may have a physiological effect on the neonate by stimulating iron acquisition and/or mucosal growth. We have hypothesized that in order to achieve such an effect(s), lactoferrin will bind to a specific receptor located on the mucosal surface of the enterocyte. We have studied the presence of lactoferrin receptors in the brush border membrane from infant rhesus monkey intestine and from fetal and infant human intestine. The receptor exhibits saturation kinetics and the binding is specific for human and monkey lactoferrin-bovine lactoferrin or human transferrin do not bind to the receptor or compete with the binding of the primate lactoferrins. Enzymatic deglycosylation does not affect the binding of human lactoferrin to its receptor, suggesting that the glycan(s) is not needed for receptor recognition. Competitive binding experiments showed that holo-lactoferrin was more effective than less Fe-saturated forms of lactoferrin with regard to receptor binding, Mn-lactoferrin bound to the receptor, while we were unable to prepare Zn-lactoferrin in any physiological buffer. The human lactoferrin receptor was isolated and found to have a MW of ~110 kDa. This receptor has now been cloned and is being sequenced.
|Original language||English (US)|
|Number of pages||6|
|Journal||Advances in Experimental Medicine and Biology|
|State||Published - 1994|
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)