Effect of bile and bile acids on binding of intrinsic factor to cobalamin and intrinsic factor-cobalamin complex to ileal receptor.
Human bile or commercially available bile acids bind [57Co]cobalamin (Cbl) due to the presence of "R"-type binders, which are normally present in the former and present as a contaminant in the latter. The competition of these R proteins for the binding of Cbl by intrinsic factor (IF) could explain the in vivo inhibition attributed previously to the bile acids themselves. R protein seems to be involved in the inhibition of Cbl binding because protease digestion of either bile or bile acid abolishes the Cbl binding ability. Moreover, antibody to R protein abolishes the inhibition. Bile or bile acids do not have a direct effect on either purified IF or the IF-Cbl receptor molecule, even though bile acids increase the attachment of IF-[57Co]Cbl to ileal brush-border membranes. These data demonstrate two steps where components of bile could affect Cbl absorption: the binding of Cbl to IF and of IF-Cbl to its ileal receptor. It is not clear whether these in vitro phenomena are important for the normal absorption of Cbl in vivo.
D000818:Animals; D001646:Bile / Q000502:physiology*; D001647:Bile Acids and Salts / Q000378:metabolism / Q000494:pharmacology*; D004285:Dogs; D006801:Humans; D007082:Ileum / Q000378:metabolism*; D007437:Intrinsic Factor / Q000378:metabolism*; D011402:Pronase; D011956:Receptors, Cell Surface / Q000187:drug effects / Q000378:metabolism*; D018000:Receptors, Peptide; D013329:Structure-Activity Relationship; D013656:Taurocholic Acid / Q000378:metabolism; D014805:Vitamin B 12 / Q000378:metabolism*
D001647:Bile Acids and Salts; D011956:Receptors, Cell Surface; D018000:Receptors, Peptide; C028199:intrinsic factor receptor; D013656:Taurocholic Acid; D007437:Intrinsic Factor; D011402:Pronase; D014805:Vitamin B 12