methodology And Applications Of Redox Proteomics The Relatively New And Rapidly Changing Field Of Redox Proteomics Has The Potential To Revolutionize How We Diagnose Disease, Assess Risks, Determine Prognoses, And Target Therapeutic Strategies For People With Inflammatory And Aging-as
Cellular location of proteins related to iron absorption and transport
✍ Scribed by Marcia J. Simovich; Marcel E. Conrad; Jay N. Umbreit; Elizabeth G. Moore; Lucille N. Hainsworth; Hilary K. Smith
- Publisher
- John Wiley and Sons
- Year
- 2002
- Tongue
- English
- Weight
- 155 KB
- Volume
- 69
- Category
- Article
- ISSN
- 0361-8609
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
K562 erythroleukemia cells and IEC6 rat cells were examined using confocal microscopy and antibodies raised against DMT‐1 (Nramp‐2, DCT‐1), transferrin receptor (CD71), β~3~ integrin (CD61), mobilferrin (calreticulin), and Hephaestin. The cellular location of each of these proteins was identified by immunofluorescence in both saponin‐permeabilized and non‐permeabilized cells. Fluorescent reactivity was observed on or near the cell surface of each of these proteins, suggesting that they might participate in surface membrane transport of iron. Fluorescence was observed in the region of the cytoplasm with each antibody to include β~3~ integrin and transferrin receptor. It was pronounced in cells incubated with mobilferrin, Hephaestin, and DMT‐1 antibodies. Speckled nuclear fluorescence was observed in cells incubated with anti‐DMT‐1. While these observations are descriptive, they demonstrate that there are significant concentrations of DMT‐1, mobilferrin, and Hephaestin in the cytoplasmic region of cells. This suggests that there may be intracellular roles for these proteins in addition to their serving to transit iron across the cell surface membrane. Am. J. Hematol. 69:164–170, 2002. © 2002 Wiley‐Liss, Inc.
📜 SIMILAR VOLUMES