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HighlightsSLC39A1, also known as ZIP1, belongs to the SLC39 family that regulates zinc levels. It is expressed widely in mammalian tissues and cells, in both plasma membrane and intracellular vesicles. Specifically, it is the major zinc uptake transporter in K562 erythroleukemia cells and prostate cells, where it is localized to the plasma membrane. Its expression appears to be regulated by zinc status and by hormone treatment. Interestingly, when cells are cultured by zinc-replete media, ZIP1 is mainly present in intracellular organelles, while when zinc is limiting it translocates to the cell surface. Zinc uptake by ZIP has been found to be energy independent, stimulated by HCO3-. Structurally, it has eight predicted transmembrane domains. The functions of ZIP1 can be inhibited by Ni2+ ions but not Fe2+ ions.
| Basic Information of SLC39A1 | |
| Protein Name | Zinc transporter ZIP1 |
| Gene Name | SLC39A1 |
| Aliases | Solute carrier family 39 member 1, Zinc-iron-regulated transporter-like, Zrt- and Irt-like protein 1, IRT1, ZIP1, ZIRTL |
| Organism | Homo sapiens (Human) |
| UniProt ID | Q9NY26 |
| Transmembrane Times | 8 |
| Length (aa) | 324 |
| Sequence | MGPWGEPELLVWRPEAVASEPPVPVGLEVKLGALVLLLVLTLLCSLVPICVLRRPGANHEGSASRQKALSLVSCFAGGVFLATCLLDLLPDYLAAIDEALAALHVTLQFPLQEFILAMGFFLVLVMEQITLAYKEQSGPSPLEETRALLGTVNGGPQHWHDGPGVPQASGAPATPSALRACVLVFSLALHSVFEGLAVGLQRDRARAMELCLALLLHKGILAVSLSLRLLQSHLRAQVVAGCGILFSCMTPLGIGLGAALAESAGPLHQLAQSVLEGMAAGTFLYITFLEILPQELASSEQRILKVILLLAGFALLTGLLFIQI |
SLC39A1, a major regulator of prostate gland zinc, is responsible for the rapid uptake and accumulation of zinc in prostate cells. The down-regulation of SLC39A1 transporter decreases zinc to prevent its cytotoxic effects. Reduced accumulation of zinc in tumorigenic prostate epithelial cells might be partly due to the decreased expression or deficiency of SLC39A1 protein. As a result, studies have reported SLC39A1 has a role of tumor suppression in the prostate, and that zinc treatment approach has been proposed for prostate cancer treatment, using ionophore such as clioquinol.
This study identified a conserved region on the C terminus of the Zip1 transporter, and the phosphorylation of which was required for the crossover formation during yeast meiosis.
This study investigated the effects of zinc and ZIP1 on fluoride-induced apoptosis in mouse MC3T3-E1 cells as well as the underlying molecular mechanisms. The results showed that treatment with zinc significantly attenuated the apoptosis induced by fluoride and that overexpression of ZIP1 inhibited this process as well.
This article reviewed the studies that used the zinc ionophore (Clioquinol) approach for the treatment of human prostate cancer, providing strong support for this treatment approach that should be pursued with additional research.
To investigate whether the functionality of the zinc clearance system was altered under oxidative stress-loaded conditions, this study characterized zinc uptake by oxidative stress-loaded astrocytes using mouse astrocytes. The results indicated that the increased zinc clearance activity of astrocytes under oxidative stress-loaded conditions might be due to increased ZIP1 expression.
This study investigated the effects of melatonin in hypoxia-induced N2a cells and the results showed that melatonin activated the MAPK/ERK pathway via upregulating the expression of Zip1.
Creative Biolabs introduces our powerful Magic™ Membrane Protein Production Platform to provide our clients with both first-class membrane protein-related services and high-quality membrane protein products. We have quite flexible options for membrane protein expression, solubilization, reconstitution, purification, and characterization. We can provide membrane proteins in formats such as detergent micelles, proteoliposomes, nanodiscs, amphipols, and SMALPs.
Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-SLC39A1 antibody development services.
Contact us if you want to know more about our membrane protein preparation services.
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