The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Regulation of Cardiac Na + ,Ca 2+ Exchange and K ATP Potassium Channels by PIP 2
Abstract
Cardiac Na + ,Ca 2+ exchange is activated by a mechanism that requires hydrolysis of adenosine triphosphate (ATP) but is not mediated by protein kinases. In giant cardiac membrane patches, ATP acted to generate phosphatidylinositol-4,5-bisphosphate (PIP 2 ) from phosphatidylinositol (PI). The action of ATP was abolished by a PI-specific phospholipase C (PLC) and recovered after addition of exogenous PI; it was reversed by a PIP 2 -specific PLC; and it was mimicked by exogenous PIP 2 . High concentrations of free Ca 2+ (5 to 20 μM) accelerated reversal of the ATP effect, and PLC activity in myocyte membranes was activated with a similar Ca 2+ dependence. Aluminum reversed the ATP effect by binding with high affinity to PIP 2 . ATP-inhibited potassium channels (K ATP ) were also sensitive to PIP 2 , whereas Na + ,K + pumps and Na + channels were not. Thus, PIP 2 may be an important regulator of both ion transporters and channels.
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Inwardly Rectifying Potassium Channels: Their Structure, Function, and Physiological Roles
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Metadata
- Authors
- Hilgemann, D. W., & Ball, R.
- Venue
- Science
- Published
- 1996-08-16
- Volume
- 273
- Issue
- 5277
- Pages
- 956-959
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2071786252
- Cited by
- 667
- References
- 35
- FWCI
- 9.28
- Type
- journal article
- Language
- en
- Open access
- closed
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- Hilgemann, D. W., & Ball, R. (1996). Regulation of Cardiac Na + ,Ca 2+ Exchange and K ATP Potassium Channels by PIP 2. Science. https://doi.org/10.1126/science.273.5277.956
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
