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celiac disease may unmask the contribution of the DMT1 (show DMRT1 Proteins) IVS4+44C>A polymorphism to the risk of anemia.
These results suggest that the increased expression of DMT1 (show DMRT1 Proteins) induces iron overload and iron overload induces osteoblast autophagy and apoptosis, thus affecting the pathological processes of osteoporosis. Clarifying the mechanisms underlying the effects of DMT1 (show DMRT1 Proteins) will allow the identification of novel targets for the prevention and treatment of osteoporosis.
the cellular iron importer, divalent metal transporter 1 (DMT1), is highly expressed in colorectal cancer through hypoxia-inducible factor 2alpha-dependent transcription.
Divalent metal transporter-1 overexpression in endometriosis patients' endometrium can increase iron influx to endometrial cells, inducing oxidative stress-mediated proinflammatory signaling. In turn, endometriosis-related conditions, as iron overload and inflammation (IL-1beta (show IL1B Proteins)), enhance endometriosis patients endometrial DMT1 (show DMRT1 Proteins) expression, creating a vicious circle on DMT-1 (show DMRT1 Proteins)-modulated pathways.
X-ray crystallographic analysis of a 4-component complex comprising the VPS26 (show VPS26A Proteins) & VPS35 (show vps35 Proteins) subunits of retromer, sorting nexin SNX3 (show SNX3 Proteins), & recycling signal from the divalent cation transporter DMT1 (show DMRT1 Proteins)-II; analysis identifies a binding site for canonical recycling signals at the interface between VPS26 (show VPS26A Proteins) & SNX3 (show SNX3 Proteins); shows cooperative interactions among the VPS subunits, SNX3 (show SNX3 Proteins) & cargo that couple signal-recognition to membrane recruitment.
Gene silencing of either CTR1 (show SLC31A1 Proteins) or DMT1 (show DMRT1 Proteins) did not affect copper accumulation in cells, but deficiency in both CTR1 (show SLC31A1 Proteins) and DMT1 (show DMRT1 Proteins) resulted in a complete inhibition of copper uptake.
These data suggest that iron uptake induces the production of ROS (show ROS1 Proteins), which modify DMT1 (show DMRT1 Proteins) endocytic cycling, thus changing the iron transport activity at the apical membrane.
We propose that DMT1 (show DMRT1 Proteins) deficiency negatively affects metabolism and life span of mature erythrocytes; two other aspects of defective erythropoiesis which contribute to the pathophysiology of the disease
Suggest role for divalent cation transporter DMT1 (show DMRT1 Proteins) in the entry of Hg(II) into the intestinal epithelium.
Six months after RYGB surgery, patients exhibit an increase in DMT1 (show DMRT1 Proteins) expression in the enterocytes of the tips of the villi at the proximal jejunum
Data suggest that maternal protein restriction during pregnancy and lactation influences growth of male and female offspring at weaning, reduces duodenum mucosal expression of iron transporters (DMT1 and FPN), and decreases serum Fe levels; serum ferritin (show FTL Proteins) levels tend to be lower, yet serum transferrin is greatly higher in male weaning piglets. (FPN = solute carrier (show SERTAD2 Proteins) family 40 [iron-regulated transporter (show SLC40A1 Proteins)] member 1)
IL-6 (show IL6 Proteins) likely up-regulates IRP1 (show ACO1 Proteins) and DMT1 expression and down-regulates FPN1 (show SLC40A1 Proteins) expression in BV2 microglial cells through JNK (show MAPK8 Proteins) signaling pathways
Ndfip2 (show NDFIP2 Proteins) controls DMT1 in the liver with female mice showing a greater response to altered dietary iron than the male mice
PrP(C (show PRNP Proteins)) promotes, and possibly regulates, the uptake of iron through DMT1 and Zip14 (show SLC39A14 Proteins) via its ferrireductase activity.
This study reveals a critical function for DMT1 in intestinal nonheme-iron absorption for normal growth and development, and that it is not required for the transport of copper, manganese, or zinc.
We propose that DMT1 deficiency negatively affects metabolism and life span of mature erythrocytes; two other aspects of defective erythropoiesis which contribute to the pathophysiology of the disease
Misregulation of DMT1 is implicated in Parkinson's disease.
Suggest role for divalent cation transporter DMT1 in the entry of Hg(II) into the intestinal epithelium.
The Cu uptake in HEK293 cells that over-expressed the 2/-IRE isoform of DMT1 transporter supports our earlier contention that DMT1 transports Cu as Cu(1+).
Hepatocyte divalent metal-ion transporter-1 is dispensable for hepatic iron accumulation and non-transferrin (show Tf Proteins)-bound iron uptake in mice.
The zebrafish mutant gene chardonnay (cdy) encodes divalent metal transporter 1 (DMT1). Whereas wild-type zebrafish DMT1 protein can transport iron, the truncated protein expressed in cdy mutants is not functional.
This gene encodes a member of the solute carrier family 11 protein family. The product of this gene transports divalent metals and is involved in iron absorption. Mutations in this gene are associated with hypochromic microcytic anemia with iron overload. A related solute carrier family 11 protein gene is located on chromosome 2. Multiple transcript variants encoding different isoforms have been found for this gene.
, NRAMP 2
, divalent cation transporter 1
, natural resistance-associated macrophage protein 2
, solute carrier family 11 (proton-coupled divalent metal ion transporters), member 2
, divalent metal transporter 1
, microcytic anemia, viable anaemia
, Solute carrier family 11 member 2 (natural resistance-associated macrophage protein 2)
, manganese transport protein