Linked Life Data

18974313

Source:http://linkedlifedata.com/resource/pubmed/id/18974313

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-12-30
pubmed:abstractText
Intestinal iron absorption involves proteins located in the brush border membrane (BBM), cytoplasm, and basolateral membrane (BLM) of duodenal enterocytes. Ferroportin 1 (FPN1) and hephaestin (Heph) are necessary for transport of iron out of enterocytes, but it is not known whether these two proteins interact during iron absorption. We first examined colocalization of the proteins by cotransfection of HEK293 cells with pDsRed-FPN1 with pEmGFP-Heph or with the COOH-terminal truncated pEmGFP-HephDelta43 or -HephDelta685 and found that FPN1 and Heph with or without the COOH terminus colocalized. In rat duodenal enterocytes, within 1 h of iron feeding prominent migration of FPN1 from the apical subterminal zone to the basal subnuclear zone of the BLM occurred and increased to at least 4 h after feeding. Heph exhibited a similar though less prominent migration after iron ingestion. Analysis using rat duodenal epithelial cell sheets demonstrated that 1) by velocity sedimentation ultracentrifugation, FPN1 and Heph occupied vesicles of different sizes prior to iron feeding and migrated to similar fractions 1 h after iron feeding; 2) by blue native/SDS-PAGE, FPN1, and Heph interacted to form two complexes, one containing dimeric FPN1 and intact Heph and the other consisting of monomeric FPN1 and a Heph fragment; and 3) by immunoprecipitation, anti-Heph or anti-FPN1 antiserum coimmunoprecipitated FPN1 and Heph. Thus the data indicate that FPN1 and Heph migrate and interact during iron feeding and suggest that dimeric FPN1 is associated with intact Heph.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0193-1857
pubmed:author
pubmed:issnType
Print
pubmed:volume
296
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
G55-65
pubmed:meshHeading
pubmed-meshheading:18974313-Animals, pubmed-meshheading:18974313-Antibody Specificity, pubmed-meshheading:18974313-Cation Transport Proteins, pubmed-meshheading:18974313-Cell Line, pubmed-meshheading:18974313-Centrifugation, Density Gradient, pubmed-meshheading:18974313-Cytoplasmic Vesicles, pubmed-meshheading:18974313-Duodenum, pubmed-meshheading:18974313-Enterocytes, pubmed-meshheading:18974313-Ferrous Compounds, pubmed-meshheading:18974313-Humans, pubmed-meshheading:18974313-Immune Sera, pubmed-meshheading:18974313-Immunoprecipitation, pubmed-meshheading:18974313-Intestinal Absorption, pubmed-meshheading:18974313-Iron, Dietary, pubmed-meshheading:18974313-Membrane Proteins, pubmed-meshheading:18974313-Microscopy, Fluorescence, pubmed-meshheading:18974313-Protein Multimerization, pubmed-meshheading:18974313-Protein Transport, pubmed-meshheading:18974313-Rats, pubmed-meshheading:18974313-Rats, Sprague-Dawley, pubmed-meshheading:18974313-Recombinant Fusion Proteins, pubmed-meshheading:18974313-Time Factors, pubmed-meshheading:18974313-Transfection
pubmed:year
2009
pubmed:articleTitle
Iron feeding induces ferroportin 1 and hephaestin migration and interaction in rat duodenal epithelium.
pubmed:affiliation
Dept. of Medicine, LSUHSC, 1501 Kings Highway, Shreveport, LA 71130, USA. kyeh@lsuhsc.edu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural