|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
8
|
|
pubmed:dateCreated |
1996-6-10
|
|
pubmed:databankReference |
|
|
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.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8617223-1459958,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8617223-1508175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8617223-1832676,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8617223-2678100,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8617223-2693940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8617223-6785259,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8617223-7482533,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8617223-7531563,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8617223-7854443,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8617223-7882967,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8617223-7919780,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8617223-8014471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8617223-8058041,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8617223-8075499,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8617223-8076608,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8617223-8108390,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8617223-8257431
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Apr
|
|
pubmed:issn |
0261-4189
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
15
|
|
pubmed:volume |
15
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1784-91
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:8617223-Amino Acid Sequence,
pubmed-meshheading:8617223-Animals,
pubmed-meshheading:8617223-Base Sequence,
pubmed-meshheading:8617223-Biological Transport, Active,
pubmed-meshheading:8617223-Carrier Proteins,
pubmed-meshheading:8617223-Cation Transport Proteins,
pubmed-meshheading:8617223-Cell Line,
pubmed-meshheading:8617223-Chromosome Mapping,
pubmed-meshheading:8617223-Cricetinae,
pubmed-meshheading:8617223-DNA, Complementary,
pubmed-meshheading:8617223-Membrane Proteins,
pubmed-meshheading:8617223-Mice,
pubmed-meshheading:8617223-Mice, Inbred C57BL,
pubmed-meshheading:8617223-Microscopy, Fluorescence,
pubmed-meshheading:8617223-Molecular Sequence Data,
pubmed-meshheading:8617223-Muridae,
pubmed-meshheading:8617223-Mutation,
pubmed-meshheading:8617223-Rats,
pubmed-meshheading:8617223-Sequence Homology, Amino Acid,
pubmed-meshheading:8617223-Subcellular Fractions,
pubmed-meshheading:8617223-Transfection,
pubmed-meshheading:8617223-Zinc
|
|
pubmed:year |
1996
|
|
pubmed:articleTitle |
ZnT-2, a mammalian protein that confers resistance to zinc by facilitating vesicular sequestration.
|
|
pubmed:affiliation |
Howard Hughes Medical Institute, University of Washington, Seattle 98195-7370, USA.
|
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
|
