Source:http://linkedlifedata.com/resource/pubmed/id/16467572
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 4
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pubmed:dateCreated |
2006-2-9
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pubmed:abstractText |
Keratinocyte differentiation, adhesion and motility are directed by extracellular Ca2+ concentration increases, which in turn increase intracellular Ca2+ levels. Normal keratinocytes, in contrast to most non-excitable cells, require Ca2+ release from both Golgi and endoplasmic reticulum Ca2+ stores for efficient Ca2+ signaling. Dysfunction of the Golgi human secretory pathway Ca2+-ATPase hSPCA1, encoded by ATP2C1, abrogates Ca2+ signaling and causes the acantholytic genodermatosis, Hailey-Hailey disease. We have examined the role of the endoplasmic reticulum Ca2+ store, established and maintained by the sarcoplasmic and endoplasmic reticulum Ca2+-ATPase SERCA2 encoded by ATP2A2, in Ca2+ signaling. Although previous studies have shown acute SERCA2 inactivation to abrogate Ca2+ signaling, we find that chronic inactivation of ATP2A2 in keratinocytes from patients with the similar acantholytic genodermatosis, Darier disease, does not impair the response to raised extracellular Ca2+ levels. This normal response is due to a compensatory upregulation of hSPCA1, as inactivating ATP2C1 expression with siRNA blocks the response to raised extracellular Ca2+ concentrations in both normal and Darier keratinocytes. ATP2C1 inactivation also diminishes Darier disease keratinocyte viability, suggesting that compensatory ATP2C1 upregulation maintains viability and partially compensates for defective endoplasmic reticulum Ca2+-ATPase in Darier disease keratinocytes. Keratinocytes thus are unique among mammalian cells in their ability to use the Golgi Ca2+ store to mediate Ca2+ signaling.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATP2A2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/ATP2C1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Transporting ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/Sarcoplasmic Reticulum...
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9533
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
119
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
671-9
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:16467572-Animals,
pubmed-meshheading:16467572-Calcium Signaling,
pubmed-meshheading:16467572-Calcium-Transporting ATPases,
pubmed-meshheading:16467572-Cell Survival,
pubmed-meshheading:16467572-Cells, Cultured,
pubmed-meshheading:16467572-Darier Disease,
pubmed-meshheading:16467572-Down-Regulation,
pubmed-meshheading:16467572-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:16467572-Golgi Apparatus,
pubmed-meshheading:16467572-Humans,
pubmed-meshheading:16467572-Keratinocytes,
pubmed-meshheading:16467572-Sarcoplasmic Reticulum Calcium-Transporting ATPases,
pubmed-meshheading:16467572-Up-Regulation
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pubmed:year |
2006
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pubmed:articleTitle |
Activity of the hSPCA1 Golgi Ca2+ pump is essential for Ca2+-mediated Ca2+ response and cell viability in Darier disease.
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pubmed:affiliation |
INSERM U563, Purpan Hospital, Place du Dr Baylac, BP 2028, 31034 Toulouse CEDEX 3 and Université Paul Sabatier, 31062 Toulouse, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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