Source:http://linkedlifedata.com/resource/pubmed/id/10378087
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rdf:type | |
lifeskim:mentions |
umls-concept:C0006675,
umls-concept:C0014834,
umls-concept:C0392747,
umls-concept:C0439834,
umls-concept:C0441712,
umls-concept:C0443172,
umls-concept:C0521119,
umls-concept:C0596235,
umls-concept:C0871261,
umls-concept:C1383501,
umls-concept:C1704632,
umls-concept:C1706817,
umls-concept:C1880497,
umls-concept:C1996904,
umls-concept:C2911692
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pubmed:issue |
3
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pubmed:dateCreated |
1999-8-20
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pubmed:abstractText |
Free intracellular Ca2+ ([Ca2+]i) in Escherichia coli was measured using the bioluminescent protein aequorin. Overall, the bacteria maintained a tight control on their free [Ca2+]i. The results indicated a slow Ca2+ influx, the magnitude of the initial rise in free [Ca2+]i being dependent upon the concentrations of external Ca2+. This was followed by the slow removal of free Ca2+ until normal levels were restored. Specifically, addition of external Ca2+ (0.25-10 mM) resulted in a gradual rise in intracellular free Ca2+ from a basal level of approximately 272 nM, maximally reaching a peak of 0.85-5.4 microM within 30-40 min. This was followed by a slow fall over the next 30 min, culminating in an oscillatory pattern of free [Ca2+]i (range 0.3-0.7 microM for 0.25 mM external Ca2+). In the presence of EGTA, free [Ca2+]i was dramatically reduced. Neither the influx of Ca2+ nor restoration of intracellular free Ca2+ required protein synthesis. Moreover, preincubation with Ca2+ increased the rising phase of intracellular Ca2+ in response to further exposure to external Ca2+. This was further evidence against a specific adaptation process such as the synthesis of calcium exporters. A putative Ca2+ influx channel was demonstrated in stationary phase cells in particular, which could be blocked by La3+. This channel was consistent with the voltage-activated poly-3-hydroxybutyrate/polyphosphate Ca2+ channels previously detailed by Reusch et al. [23] Even in the presence of La3+, however, the free [Ca2+]i of log phase and stationary phase bacteria still increased two-fold over resting values in response to external Ca2+. This suggested the presence of at least two Ca2+ influx processes, one inhibited by La3+ and the other not.
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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/Aequorin,
http://linkedlifedata.com/resource/pubmed/chemical/Apoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/apoaequorin
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0143-4160
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
265-74
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10378087-Aequorin,
pubmed-meshheading:10378087-Apoproteins,
pubmed-meshheading:10378087-Calcium,
pubmed-meshheading:10378087-Calcium Signaling,
pubmed-meshheading:10378087-Cell Division,
pubmed-meshheading:10378087-Cytosol,
pubmed-meshheading:10378087-Escherichia coli,
pubmed-meshheading:10378087-Luminescent Measurements,
pubmed-meshheading:10378087-Recombinant Proteins,
pubmed-meshheading:10378087-Time Factors
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pubmed:year |
1999
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pubmed:articleTitle |
Slow changes in cytosolic free Ca2+ in Escherichia coli highlight two putative influx mechanisms in response to changes in extracellular calcium.
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pubmed:affiliation |
Department of Medical Biochemistry, University of Wales College of Medicine, Cardiff, UK. joneshe3@cardiff.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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