| pubmed-article:8617223 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8617223 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:8617223 | lifeskim:mentions | umls-concept:C0205378 | lld:lifeskim |
| pubmed-article:8617223 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8617223 | lifeskim:mentions | umls-concept:C0043481 | lld:lifeskim |
| pubmed-article:8617223 | lifeskim:mentions | umls-concept:C0443301 | lld:lifeskim |
| pubmed-article:8617223 | lifeskim:mentions | umls-concept:C0683598 | lld:lifeskim |
| pubmed-article:8617223 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:8617223 | pubmed:dateCreated | 1996-6-10 | lld:pubmed |
| pubmed-article:8617223 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8617223 | pubmed:abstractText | A cDNA encoding a second zinc transporter (ZnT-2) was isolated from a rat kidney cDNA expression library by complementation of a zinc-sensitive BHK cell line. The protein predicted from the open reading frame of ZnT-2 cDNA has 359 amino acids and initiates with a CTG codon. It resembles ZnT-1 (a plasma membrane protein that stimulates zinc efflux) in overall topology in that it has six membrane-spanning domains, a histidine-rich intracellular loop and a long C-terminal tail; however, the overall amino acid identity is only 26%. Unlike ZnT-1, which is in the plasma membrane and lowers cellular zinc by stimulating zinc efflux, ZnT-2 is localized on vesicles and allows the zinc-sensitive BHK cells to accumulate zinc to levels that are much higher than non-transformed cells can tolerate. Zinc was visualized within these vesicles with zinquin, a zinc-specific fluorescent probe. The intracellular compartment that accumulates zinc is acidic as revealed by staining with acridine orange or LysoTracker. Prolonged exposure of cells expressing ZnT-2 to zinc causes an accretion of intracellular vesicles. We suggest that ZnT-2 protects these cells from zinc toxicity by facilitating zinc transport into an endosomal/lysosomal compartment. | lld:pubmed |
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| pubmed-article:8617223 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8617223 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8617223 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8617223 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8617223 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:8617223 | pubmed:author | pubmed-author:PalmiterR DRD | lld:pubmed |
| pubmed-article:8617223 | pubmed:author | pubmed-author:FUZIMM | lld:pubmed |
| pubmed-article:8617223 | pubmed:author | pubmed-author:FindleyS DSD | lld:pubmed |
| pubmed-article:8617223 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8617223 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8617223 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:8617223 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8617223 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8617223 | pubmed:pagination | 1784-91 | lld:pubmed |
| pubmed-article:8617223 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8617223 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8617223 | pubmed:articleTitle | ZnT-2, a mammalian protein that confers resistance to zinc by facilitating vesicular sequestration. | lld:pubmed |
| pubmed-article:8617223 | pubmed:affiliation | Howard Hughes Medical Institute, University of Washington, Seattle 98195-7370, USA. | lld:pubmed |
| pubmed-article:8617223 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8617223 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8617223 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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