pubmed-article:8521803 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8521803 | lifeskim:mentions | umls-concept:C0150369 | lld:lifeskim |
pubmed-article:8521803 | lifeskim:mentions | umls-concept:C0682538 | lld:lifeskim |
pubmed-article:8521803 | lifeskim:mentions | umls-concept:C0086045 | lld:lifeskim |
pubmed-article:8521803 | lifeskim:mentions | umls-concept:C0014239 | lld:lifeskim |
pubmed-article:8521803 | lifeskim:mentions | umls-concept:C1996904 | lld:lifeskim |
pubmed-article:8521803 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
pubmed-article:8521803 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
pubmed-article:8521803 | lifeskim:mentions | umls-concept:C1880497 | lld:lifeskim |
pubmed-article:8521803 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
pubmed-article:8521803 | pubmed:issue | 22 | lld:pubmed |
pubmed-article:8521803 | pubmed:dateCreated | 1996-1-24 | lld:pubmed |
pubmed-article:8521803 | pubmed:abstractText | Direct monitoring of the free Ca2+ concentration in the lumen of the endoplasmic reticulum (ER) is an important but still unsolved experimental problem. We have shown that a Ca(2+)-sensitive photoprotein, aequorin, can be addressed to defined subcellular compartments by adding the appropriate targeting sequences. By engineering a new aequorin chimera with reduced Ca2+ affinity, retained in the ER lumen via interaction of its N-terminus with the endogenous resident protein BiP, we show here that, after emptying the ER, Ca2+ is rapidly re-accumulated up to concentrations of > 100 microM, thus consuming most of the reporter photoprotein. An estimate of the steady-state Ca2+ concentration was obtained using Sr2+, a well-known Ca2+ surrogate which elicits a significantly slower rate of aequorin consumption. Under conditions in which the rate and extent of Sr2+ accumulation in the ER closely mimick those of Ca2+, the steady-state mean lumenal Sr2+ concentration ([Sr2+]er) was approximately 2 mM. Receptor stimulation causes, in a few seconds, a 3-fold decrease of the [Sr2+]er, whereas specific inhibition of the ER Ca2+ ATPase leads to an approximately 10-fold drop in a few minutes. | lld:pubmed |
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pubmed-article:8521803 | pubmed:language | eng | lld:pubmed |
pubmed-article:8521803 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8521803 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8521803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8521803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:8521803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8521803 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8521803 | pubmed:month | Nov | lld:pubmed |
pubmed-article:8521803 | pubmed:issn | 0261-4189 | lld:pubmed |
pubmed-article:8521803 | pubmed:author | pubmed-author:PozzanTT | lld:pubmed |
pubmed-article:8521803 | pubmed:author | pubmed-author:AlvarezJJ | lld:pubmed |
pubmed-article:8521803 | pubmed:author | pubmed-author:SitiaRR | lld:pubmed |
pubmed-article:8521803 | pubmed:author | pubmed-author:MonteroMM | lld:pubmed |
pubmed-article:8521803 | pubmed:author | pubmed-author:BriniMM | lld:pubmed |
pubmed-article:8521803 | pubmed:author | pubmed-author:MarsaultRR | lld:pubmed |
pubmed-article:8521803 | pubmed:author | pubmed-author:RizzutoRR | lld:pubmed |
pubmed-article:8521803 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8521803 | pubmed:day | 15 | lld:pubmed |
pubmed-article:8521803 | pubmed:volume | 14 | lld:pubmed |
pubmed-article:8521803 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8521803 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8521803 | pubmed:pagination | 5467-75 | lld:pubmed |
pubmed-article:8521803 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:8521803 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:8521803 | pubmed:articleTitle | Monitoring dynamic changes in free Ca2+ concentration in the endoplasmic reticulum of intact cells. | lld:pubmed |
pubmed-article:8521803 | pubmed:affiliation | Department of Biomedical Sciences, University of Padova, Italy. | lld:pubmed |
pubmed-article:8521803 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8521803 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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