Document Detail

Lactoferrin and its hydrolysate bind directly to the oleate-activated form of the lipolysis stimulated lipoprotein receptor.
MedLine Citation:
PMID:  23050782     Owner:  NLM     Status:  Publisher    
The hepatic removal of triglyceride-rich chylomicrons during the postprandial phase represents an important step towards determining the bioavailability of dietary lipids amongst the peripheral tissues. Indeed, elevated postprandial lipemia is often associated with obesity and increased risk of coronary heart disease. The milk protein, lactoferrin, has been shown to inhibit hepatic chylomicron remnant removal by the liver, resulting in increased postprandial lipemia. Despite numerous studies on potential targets for lactoferrin, the molecular mechanisms underlying the effect of lactoferrin remained unclear. We recently demonstrated that the lipolysis stimulated lipoprotein receptor (LSR) contributes to the removal of triglyceride-rich lipoproteins during the postprandial phase. Here, we report that while lactoferrin does not have any significant effect on LSR protein levels in mouse Hepa1-6 cells, this protein co-localizes with LSR in cells, but only in the presence of oleate, which is needed to obtain LSR in its active form as lipoprotein receptor. Ligand blotting using purified LSR revealed that lactoferrin binds directly to the receptor in the presence of oleate and prevents the binding of triglyceride-rich lipoproteins. Both C- and N- lobes of lactoferrin, as well as a mixture of peptides derived from its hydrolysis retained the ability to bind LSR in its active form. We propose then that the elevated postprandial lipemia observed upon lactoferrin treatment in vivo is mediated in part by its direct interaction with FFA-activated LSR, thus preventing clearance of chylomicrons and their remnants through the LSR pathway. © 2012 The Authors Journal compilation © 2012 FEBS.
Nazir Ahmad; Jean-Michel Girardet; Samina Akbar; Marie-Claire Lanhers; Cédric Paris; Frances T Yen; Catherine Corbier
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-10-11
Journal Detail:
Title:  The FEBS journal     Volume:  -     ISSN:  1742-4658     ISO Abbreviation:  FEBS J.     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-11     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101229646     Medline TA:  FEBS J     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
© 2012 The Authors Journal compilation © 2012 FEBS.
Université de Lorraine, Unité de Recherche Animal et Fonctionnalités des Produits Animaux (UR AFPA), Unité Sous Contrat INRA 340, Vandœuvre-lès-Nancy Cedex, F-54506, France; Université de Lorraine, LIPIDOMIX,, EA 4422, Vandœuvre-lès-Nancy Cedex, F-54500, France.
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