|Name:||solute carrier family 39 (zinc transporter), member 1|
|Old Name:||zinc/iron regulated transporter-like|
|PubMed (10610721):|| Lioumi M, Ferguson CA, Sharpe PT, Freeman T, Marenholz I, Mischke D,Heizmann C, Ragoussis J. Isolation and characterization of human and mouse ZIRTL, a member of the IRT1family of transporters, mapping within the epidermal differentiation complex.Genomics. 1999 Dec 1;62(2):272-80. PMID: 10610721 [PubMed - indexed for MEDLINE]|
We report the precise mapping and characterization of ZIRTL (zinc-iron regulated transporter-like) gene, the first mammalian member of an extensive family of divalent metal ion transporters, comprising IRT1 and ZIP1, ZIP2, ZIP3, and ZIP4 in plants and ZRT1 and ZRT2 in yeast. The human gene maps at the telomeric end of the epidermal differentiation complex (EDC), within chromosomal band 1q21, while the mouse gene maps within the mouse EDC, on mouse chromosome 3, between S100A9 and S100A13. The structure of the human gene has been determined, and message was detected in most adult and fetal tissues including the epidermis. The mouse gene is developmentally regulated and found expressed in fetal and adult suprabasal epidermis, osteoblasts, small intestine, and salivary gland.
|PubMed (10681536):|| Gaither LA, Eide DJ. Functional expression of the human hZIP2 zinc transporter.J Biol Chem. 2000 Feb 25;275(8):5560-4. PMID: 10681536 [PubMed - indexed for MEDLINE]|
Zinc is an essential nutrient for humans, yet we know little about how this metal ion is taken up by mammalian cells. In this report, we describe the characterization of hZip2, a human zinc transporter identified by its similarity to zinc transporters recently characterized in fungi and plants. hZip2 is a member of the ZIP family of eukaryotic metal ion transporters that includes two other human genes, hZIP1 and hZIP3, and genes in mice and rats. To test whether hZip2 is a zinc transporter, we examined (65)Zn uptake activity in transfected K562 erythroleukemia cells expressing hZip2 from the CMV promoter. hZip2-expressing cells accumulated more zinc than control cells because of an increased initial zinc uptake rate. This activity was time-, temperature-, and concentration-dependent and saturable with an apparent K(m) of 3 microM. hZip2 zinc uptake activity was inhibited by several other transition metals, suggesting that this protein may transport other substrates as well. hZip2 activity was not energy-dependent, nor did it require K(+) or Na(+) gradients. Zinc uptake by hZip2 was stimulated by HCO(3)(-) treatment, suggesting a Zn(2+)-HCO(3)(-) cotransport mechanism. Finally, hZip2 was exclusively localized in the plasma membrane. These results indicate that hZip2 is a zinc transporter, and its identification provides one of the first molecular tools to study zinc uptake in mammalian cells.