Colocalization of ferroportin‐1 with hephaestin on the basolateral membrane of human intestinal absorptive cells
Abstract
An iron exporter ferroportin‐1 (FPN‐1) and a multi‐copper oxidase hephaestin (Heph) are predicted to be expressed on the basolateral membrane of the enterocyte and involved in the processes of iron export across the basolateral membrane of the enterocyte. However, it is not clear where these proteins are exactly located in the intestinal absorptive cell. We examined cellular localization of FPN‐1 and Heph in the intestinal absorptive cells using the fully differentiated Caco‐2 cells. Confocal microscope study showed that FPN‐1 and Heph are located on the basolateral membrane and they are associated with the transferrin receptor (TfR) in fully differentiated Caco‐2 cells grown on microporous membrane inserts. However, Heph protein was not detected in the crypt cell‐like proliferating Caco‐2 cell. In stably transfected human intestinal absorptive cells expressing human FPN‐1 modified by the addition of GFP at the C‐terminus, we show that FPN‐1‐GFP is located on the basolateral membrane and it is associated with Heph suggesting the possibility that FPN‐1 might associate and interact with Heph in the process of iron exit across the basolateral membrane of intestinal absorptive cell. J. Cell. Biochem. 101: 1000–1010, 2007. © 2007 Wiley‐Liss, Inc.
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Total absence of Cp results in the autosomal-recessive disorder aceruloplasminemia, in which afflicted individuals have adult-onset neurodegeneration.
“The total absence of Cp results in an autosomal-recessive disorder, aceruloplasminemia, in which afflicted individuals have adult-onset neurodegeneration (124).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [124]
Mutations in aceruloplasminemia are nonsense mutations that result in early termination of translation, causing serum Cp deficiency.
“Mutations identified in aceruloplasminemia are nonsense mutations that result in the early termination of translation, causing serum Cp deficiency.”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [124]
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Evaluating Iron Flux in the Brain
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RESTAURANTE UNIVERSITÁRIO: UMA AVALIAÇÃO DO GRAU DE SATISFAÇÃO DOS COMENSAIS
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Le rôle de l'érythroferrone dans la régulation du métabolisme du fer
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- Authors
- Han, O., & Kim, E.
- Affiliations
- Pennsylvania State University (US)
- Corresponding author
- Han, Okhee
- ORCID
- Kim, Eun‐Young
- Venue
- Journal of Cellular Biochemistry
- Publisher
- Wiley
- Published
- 2007-05-07
- Volume
- 101
- Issue
- 4
- Pages
- 1000-1010
- ISSN
- 0730-2312 (ISSN-L)
- 1097-4644
- OpenAlex
- W2050280601
- Cited by
- 77
- References
- 35
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 2 · 2022: 1 · 2021: 6 · 2020: 3 · 2019: 4 · 2018: 4 · 2017: 3 · 2016: 3 · 2015: 2 · 2014: 9 · 2013: 5 · 2012: 5
- FWCI
- 4.71
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Cellular Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Pennsylvania State University
- Huck Institutes of the Life Sciences
- National Institute of Diabetes and Digestive and Kidney Diseases (R21DK069946)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Ferroptosis and cancer prognosis
- Keywords
- ferroportin 1, hephaestin, iron export, basolateral membrane, enterocytes, transferrin receptor, protein colocalization, Caco-2 cells, multicopper oxidase, iron metabolism
- MeSH terms
- Ferroportin, Cell Membrane, Electrophoresis, Polyacrylamide Gel, Fluorescent Antibody Technique, Humans, Membrane Proteins, Receptors, Transferrin, Recombinant Fusion Proteins, Transfection, Blotting, Western, Microscopy, Confocal, Caco-2 Cells, Cation Transport Proteins, Green Fluorescent Proteins
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