The store-operated calcium entry pathways in human carcinoma A431 cells: Functional properties and activation mechanisms
Journal of General Physiology, ISSN: 0022-1295, Vol: 122, Issue: 1, Page: 81-94
2003
- 33Citations
- 20Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations33
- Citation Indexes33
- 33
- CrossRef24
- Captures20
- Readers20
- 18
Article Description
Activation of phospholipase C (PLC)-mediated signaling pathways in nonexcitable cells causes the release of Ca from intracellular Ca stores and activation of Ca influx across the plasma membrane. Two types of Ca channels, highly Ca-selective I and moderately Ca-selective I, support store-operated Ca entry process. In previous patch-clamp experiments with a human carcinoma A431 cell line we described store-operated I/I plasma membrane Ca influx channels. In the present paper we use whole-cell and single-channel recordings to further characterize store-operated Ca influx pathways in A431 cells. We discovered that (a) I and I are present in A431 cells; (b) I currents are highly selective for divalent cations and fully activate within 150 s after initiation of Ca store depletion; (c) I currents are moderately selective for divalent cations (P/P 14.5) and require at least 300 s for full activation; (d) I and I currents are activated by PLC-coupled receptor agonists; (e) I currents are supported by I/I channels that display 8.5-10 pS conductance for sodium; (f) I single channel conductance for sodium is estimated at 0.9 pS by the noise analysis; (g) I/I channels are activated in excised patches by an amino-terminal fragment of InsPR1 (InsPR1N); and (h) InsP binding to InsPR1N is necessary for activation of I/I channels. Our findings provide novel information about store-operated Ca influx pathways in A431 cells.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0037488177&origin=inward; http://dx.doi.org/10.1085/jgp.200308815; http://www.ncbi.nlm.nih.gov/pubmed/12835472; https://rupress.org/jgp/article/122/1/81/44473/The-Store-operated-Calcium-Entry-Pathways-in-Human; https://dx.doi.org/10.1085/jgp.200308815
Rockefeller University Press
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