| pubmed-article:11226155 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11226155 | lifeskim:mentions | umls-concept:C0032105 | lld:lifeskim |
| pubmed-article:11226155 | lifeskim:mentions | umls-concept:C0042219 | lld:lifeskim |
| pubmed-article:11226155 | lifeskim:mentions | umls-concept:C1166717 | lld:lifeskim |
| pubmed-article:11226155 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:11226155 | lifeskim:mentions | umls-concept:C0034318 | lld:lifeskim |
| pubmed-article:11226155 | lifeskim:mentions | umls-concept:C0040557 | lld:lifeskim |
| pubmed-article:11226155 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:11226155 | pubmed:dateCreated | 2001-3-15 | lld:pubmed |
| pubmed-article:11226155 | pubmed:abstractText | Ca(2+)-ATPases are likely to play critical roles in the biochemistry of Toxoplasma gondii, since these protozoa are obligate intracellular parasites and the Ca(2+) concentration in their intracellular location is three orders of magnitude lower than in the extracellular medium. Here, we report the cloning and sequencing of a gene encoding a plasma membrane-type Ca(2+)-ATPase (PMCA) of T.gondii (TgA1). The predicted protein (TgA1) exhibits 32-36% identity to vacuolar Ca(2+)-ATPases of Trypanosoma cruzi, Saccharomyces cerevisiae, Entamoeba histolytica and Dictyostelium discoideum. Sequencing of both cDNA and genomic DNA from T.gondii indicated that TgA1 contains two introns near the C-terminus. A hydropathy profile of the protein suggests 10 transmembrane domains. TgA1 suppresses the Ca(2+) hypersensitivity of a mutant of S.cerevisiae that has a defect in vacuolar Ca(2+) accumulation. Indirect immunofluorescence and immunoelectron microscopy analysis indicate that TgA1 localizes to the plasma membrane and co-localizes with the vacuolar H(+)-pyrophosphatase to intracellular vacuoles identified morphologically and by X-ray microanalysis as the acidocalcisomes. This vacuolar-type Ca(2+)-ATPase could play an important role in Ca(2+) homeostasis in T.gondii. | lld:pubmed |
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| pubmed-article:11226155 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11226155 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11226155 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11226155 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11226155 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11226155 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:11226155 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:11226155 | pubmed:author | pubmed-author:GravesJJ | lld:pubmed |
| pubmed-article:11226155 | pubmed:author | pubmed-author:LuzDD | lld:pubmed |
| pubmed-article:11226155 | pubmed:author | pubmed-author:ZhongLL | lld:pubmed |
| pubmed-article:11226155 | pubmed:author | pubmed-author:MorenoS NSN | lld:pubmed |
| pubmed-article:11226155 | pubmed:author | pubmed-author:VieiraMM | lld:pubmed |
| pubmed-article:11226155 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11226155 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:11226155 | pubmed:volume | 20 | lld:pubmed |
| pubmed-article:11226155 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11226155 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11226155 | pubmed:pagination | 55-64 | lld:pubmed |
| pubmed-article:11226155 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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