Characterization of the binding of ferritin to the rat liver ferritin receptor

Mack U., Storey E.L., Powell L.W. and Halliday J.W. (1985) Characterization of the binding of ferritin to the rat liver ferritin receptor. BBA - General Subjects, 843 3: 164-170. doi:10.1016/0304-4165(85)90135-7


Author Mack U.
Storey E.L.
Powell L.W.
Halliday J.W.
Title Characterization of the binding of ferritin to the rat liver ferritin receptor
Journal name BBA - General Subjects   Check publisher's open access policy
ISSN 0304-4165
Publication date 1985-12-13
Sub-type Article (original research)
DOI 10.1016/0304-4165(85)90135-7
Open Access Status Not yet assessed
Volume 843
Issue 3
Start page 164
End page 170
Total pages 7
Subject 1303 Specialist Studies in Education
1304 Biophysics
1312 Molecular Biology
Abstract The binding characteristics and specificity of the rat hepatic ferritin receptor were investigated using ferritins prepared from rat liver, heart, spleen, kidney and serum, human liver and serum, guinea pig liver and horse spleen as well as ferritins enriched with respect to either H- or L-type subunit composition, prepared by chromatofocusing of rat liver ferritin on Mono-P or by reverse-phase chromatography of ferritin subunits on ProRPC 5/10. No significant difference was apparent in the binding of any of the tissue ferritins, or of ferritins of predominantly acidic or basic subunit composition. However, serum ferritin bound with a lower affinity. The effect of carbohydrate on the ferritin-receptor binding was examined by glycosidase treatment of tissue and serum ferritins. Tissue ferritin binding was unaffected, while serum ferritin binding affinity was increased to that of the tissue ferritins. Inhibition of ferritin binding by lactoferrin was not due to common carbohydrate moieties as previously suggested but was due to direct binding of lactoferrin to ferritin. Therefore, carbohydrate residues do not appear to facilitate receptor-ferritin binding, and sialic acid residues present on serum ferritin may in fact interfere with binding. The results indicate that the hepatic ferritin receptor acts preferentially to remove tissue ferritins from the circulation. The lower binding affinity of serum ferritin for the ferritin receptor explains its slower in vivo clearance relative to tissue ferritins.
Keyword (Rat liver)
Carbohydrate moiety
Ferritin binding
Ferritin receptor
Subunit composition
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
 
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Created: Tue, 28 Jun 2016, 12:47:34 EST by System User