Authors: Hemalatha Jegasothy Rangika Weerakkody Sophie SelbyPham Louise E Bennett
Publish Date: 2014/10/04
Volume: 27, Issue: 6, Pages: 1371-1382
Abstract
Lactoferrin Lf present in colostrum and milk is a member of the transferrin family of ironbinding glycoproteins with stronger binding capacity to ferric iron than hemoglobin myoglobin or transferrin Unlike hemoglobin and myoglobin ironbound Lf is reasonably stable to gastric and duodenal digestive conditions Unlike ferrous iron ferric iron is not directly reactive with oxygen supporting the capacity of Lf capture of heme iron to suppress reactive oxygen species ROS production We therefore hypothesized that bovine Lf could capture and thereby terminate the cycle of ROS production by heme iron The transfer of heme iron from either intact or digested forms of hemoglobin and myoglobin and from intact ferritin was demonstrated by in vitro methods monitoring Fesaturation status of Lf by changes in absorptivity at 465 nm The results are discussed in the context of new proposed opportunities for orally administered Lf to regulate oxidative damage associated with heme iron In addition to potentially suppressing oxidative heme–ironmediated tissue damage in the lumen Lf is expected to also reverse the overload of ferritinbound iron that accompanies chronic inflammation and aging These new proposed uses of Lf are additional to known host defense functions that include antimicrobial antiviral properties immune and cancer cell growth regulation The findings and interpretations presented require clinical substantiation and may support important additional protective and therapeutic uses for Lf in the future
Keywords: