| pubmed-article:3097504 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3097504 | lifeskim:mentions | umls-concept:C0006675 | lld:lifeskim |
| pubmed-article:3097504 | lifeskim:mentions | umls-concept:C1273518 | lld:lifeskim |
| pubmed-article:3097504 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
| pubmed-article:3097504 | lifeskim:mentions | umls-concept:C0018850 | lld:lifeskim |
| pubmed-article:3097504 | lifeskim:mentions | umls-concept:C0282498 | lld:lifeskim |
| pubmed-article:3097504 | lifeskim:mentions | umls-concept:C1441672 | lld:lifeskim |
| pubmed-article:3097504 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:3097504 | lifeskim:mentions | umls-concept:C0013139 | lld:lifeskim |
| pubmed-article:3097504 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:3097504 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:3097504 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:3097504 | pubmed:dateCreated | 1987-1-20 | lld:pubmed |
| pubmed-article:3097504 | pubmed:abstractText | Heat shock caused significant changes in intracellular pH (pHi) and intracellular free calcium concentration [( Ca2+]i) which occurred rapidly after temperature elevation. pHi fell from a resting level value at 25 degrees C of 7.38 +/- 0.02 (mean +/- standard error of the mean, n = 15) to 6.91 +/- 0.11 (n = 7) at 35 degrees C. The resting level value of [Ca2+]i in single Drosophila melanogaster larval salivary gland cells was 198 +/- 31 nM (n = 4). It increased approximately 10-fold, to 1,870 +/- 770 nM (n = 4), during a heat shock. When salivary glands were incubated in calcium-free, ethylene glycol-bis(beta-aminoethyl ether)-N,N',N'-tetraacetic acid (EGTA)-buffered medium, the resting level value of [Ca2+]i was reduced to 80 +/- 7 nM (n = 3), and heat shock resulted in a fourfold increase in [Ca2+]i to 353 +/- 90 nM (n = 3). The intracellular free-ion concentrations of Na+, K+, Cl-, and Mg2+ were 9.6 +/- 0.8, 101.9 +/- 1.7, 36 +/- 1.5, and 2.4 +/- 0.2 mM, respectively, and remained essentially unchanged during a heat shock. Procedures were devised to mimic or block the effects of heat shock on pHi and [Ca2+]i and to assess their role in the induction of heat shock proteins. We report here that the changes in [Ca2+]i and pHi which occur during heat shock are not sufficient, nor are they required, for a complete induction of the heat shock response. | lld:pubmed |
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| pubmed-article:3097504 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3097504 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3097504 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3097504 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3097504 | pubmed:month | May | lld:pubmed |
| pubmed-article:3097504 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:3097504 | pubmed:author | pubmed-author:TsienR YRY | lld:pubmed |
| pubmed-article:3097504 | pubmed:author | pubmed-author:SteinhardtR... | lld:pubmed |
| pubmed-article:3097504 | pubmed:author | pubmed-author:DrummondI AIA | lld:pubmed |
| pubmed-article:3097504 | pubmed:author | pubmed-author:PoenieMM | lld:pubmed |
| pubmed-article:3097504 | pubmed:author | pubmed-author:McClureS ASA | lld:pubmed |
| pubmed-article:3097504 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3097504 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:3097504 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3097504 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3097504 | pubmed:pagination | 1767-75 | lld:pubmed |
| pubmed-article:3097504 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:3097504 | pubmed:meshHeading | pubmed-meshheading:3097504-... | lld:pubmed |
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| pubmed-article:3097504 | pubmed:meshHeading | pubmed-meshheading:3097504-... | lld:pubmed |
| pubmed-article:3097504 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:3097504 | pubmed:articleTitle | Large changes in intracellular pH and calcium observed during heat shock are not responsible for the induction of heat shock proteins in Drosophila melanogaster. | lld:pubmed |
| pubmed-article:3097504 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3097504 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3097504 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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