scholarly journals Addition of Exogenous α-Synuclein Oligomer up-regulates Divalent Metal Transporter-1 and Ferroportin-1 in BV2 Glial Cell Lines

2016 ◽  
Vol 2 (11) ◽  
pp. 54-60
Author(s):  
Chengkui Shi ◽  
Xinxing Du
Keyword(s):  
Glial Cell ◽  
Cell Lines ◽  
Divalent Metal ◽  
Divalent Metal Transporter 1 ◽  
Divalent Metal Transporter ◽  
Metal Transporter ◽  
Ferroportin 1

Expression of the duodenal iron transporters divalent-metal transporter 1 and ferroportin 1 in iron deficiency and iron overload

2001 ◽  
Vol 120 (6) ◽  
pp. 1412-1419 ◽  
Author(s):  
Heinz Zoller ◽  
Günter Weiss ◽  
Igor Theurl ◽  
Robert O. Koch ◽  
Wolfgang Vogel ◽  
...  
Keyword(s):  
Iron Deficiency ◽  
Iron Overload ◽  
Divalent Metal ◽  
Divalent Metal Transporter 1 ◽  
Divalent Metal Transporter ◽  
Metal Transporter ◽  
Ferroportin 1

scholarly journals Effect of DMT1 knockdown on iron, cadmium, and lead uptake in Caco-2 cells

2003 ◽  
Vol 284 (1) ◽  
pp. C44-C50 ◽  
Author(s):  
Desmond I. Bannon ◽  
Roger Abounader ◽  
Peter S. J. Lees ◽  
Joseph P. Bressler
Keyword(s):  
Cell Lines ◽  
Toxic Metals ◽  
Control Cell ◽  
Divalent Metal ◽  
Lead Uptake ◽  
Divalent Metal Transporter 1 ◽  
Divalent Metal Transporter ◽  
Metal Transporter ◽  
Ph Range ◽  
Cadmium And Lead

DMT1 (divalent metal transporter 1) is a hydrogen-coupled divalent metal transporter with a substrate preference for iron, although the protein when expressed in frog oocytes transports a broad range of metals, including the toxic metals cadmium and lead. Wild-type Caco-2 cells displayed saturable transport of lead and iron that was stimulated by acid. Cadmium and manganese inhibited transport of iron, but zinc and lead did not. The involvement of DMT1 in the transport of toxic metals was examined by establishing clonal DMT1 knockdown and control Caco-2 cell lines. Knockdown cell lines displayed much lower levels of DMT1 mRNA and a smaller Vmaxfor iron uptake compared with control cell lines. One clone was further characterized and found to display an ∼50% reduction in uptake of iron across a pH range from 5.5 to 7.4. Uptake for cadmium also decreased 50% across the same pH range, but uptake for lead did not. These results show that DMT1 is important in iron and cadmium transport in Caco-2 cells but that lead enters these cells through an independent hydrogen-driven mechanism.

Mechanisms of Iron Mediated Regulation of the Duodenal Iron Transporters Divalent Metal Transporter 1 and Ferroportin 1

2002 ◽  
Vol 29 (3) ◽  
pp. 488-497 ◽  
Author(s):  
Heinz Zoller ◽  
Igor Theurl ◽  
Robert Koch ◽  
Arthur Kaser ◽  
Günter Weiss
Keyword(s):  
Divalent Metal ◽  
Divalent Metal Transporter 1 ◽  
Divalent Metal Transporter ◽  
Metal Transporter ◽  
Ferroportin 1

scholarly journals Comparison of mammalian cell lines expressing distinct isoforms of divalent metal transporter 1 in a tetracycline-regulated fashion

2006 ◽  
Vol 398 (3) ◽  
pp. 539-546 ◽  
Author(s):  
Michael D. Garrick ◽  
Hung-Chieh Kuo ◽  
Farida Vargas ◽  
Steven Singleton ◽  
Lin Zhao ◽  
...  
Keyword(s):  
Cell Lines ◽  
Iron Uptake ◽  
Divalent Metal ◽  
Maximal Response ◽  
Divalent Metal Transporter 1 ◽  
Divalent Metal Transporter ◽  
Metal Transporter ◽  
Doxycycline Treatment ◽  
Mammalian Cell Lines ◽  
Toxicological Studies

DMT1 (divalent metal transporter; also known as SLC11A2, DCT1 or Nramp2) is responsible for ferrous iron uptake in the duodenum, iron exit from endosomes during the transferrin cycle and some transferrin-independent iron uptake in many cells. Four protein isoforms differ by starting in exon 1A or 2 and ending with alternative peptides encoded by mRNA that contains or lacks an IRE (iron responsive element; ±IRE). We have compared 1A/+IRE and 2/−IRE DMT1 during regulated ectopic expression. HEK-293-F (human embryonic kidney-293-fast growing variant) cells were stably transfected with each construct expressed from a tetracycline-regulated CMV promoter. Reverse transcriptase-PCR analysis showed that construct expression responded to doxycycline. Immunofluorescence staining of cells, using antibodies specific for DMT1 isoforms, confirmed an increase in expression in the plasma membrane and cytosolic vesicles after doxycycline treatment, but with isoform specific distributions. Immunoblotting also revealed stimulation of expression. Nevertheless, both DMT1 isoforms performed similarly in assays for functional properties based on 54Mn2+ and 59Fe2+ uptake. Mn incorporation after doxycycline treatment was ∼10-fold greater than that of untreated cells, while expression in the untreated cells was ∼5-fold greater than in the untransfected cells. Uptake of Mn depended on addition of doxycycline, with half maximal response at ∼1 nM doxycycline. Doxycycline-stimulated Mn and Fe uptake was linear with time for 10 min but not over longer periods. Transport exhibited a pH optimum at ∼5.5 and dependence on incubation temperature and Mn or Fe concentration. The new cell lines should prove useful for research on metal homoeostasis, toxicological studies and efforts to identify distinctive properties of the isoforms.

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