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Am J Physiol Cell Physiol (July 3, 2002). doi:10.1152/ajpcell.00035.2002
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Articles in PresS, published online ahead of print July 3, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00035.2002
Submitted on January 22, 2002
Accepted on June 24, 2002

MODULATION OF BKCa CHANNEL ACTIVITY BY FATTY ACIDS AND OTHER CHARGED LIPIDS: STRUCTURAL REQUIREMENTS AND MECHANISM OF ACTION

Alison L Clarke1*, Steven Petrou1, John V Walsh, Jr2, and Joshua J Singer2

1 Physiology, The University of Melbourne, Parkville, VIC, Australia
2 Physiology, The University of Massachusetts Medical School, Worcester, MA, USA

* To whom correspondence should be addressed. E-mail: alisonlc{at}unimelb.edu.au.

To determine the mechanism of fatty acid modulation of rabbit pulmonary artery Ca2+-activated K+ (BKCa) channel activity, we studied effects of fatty acids and other lipids on channel activity in excised patches using patch clamp techniques. The structural features of the fatty acid required to increase BKCa channel activity (or average number of open channels, NPo) were identified to be the negatively charged head group and a sufficiently long (>8C) carbon chain. Positively charged lipids like sphingosine, which have a sufficiently long alkyl chain (>=8C) produced a decrease in NPo. Neutral and short chain lipids did not alter NPo. Screening of membrane surface charge with high ionic strength bathing solutions (330 mM K or 130 mM K, 300 mM Na) did not alter the modulation of the BKCa channel NPo by fatty acids and other charged lipids indicating that channel modulation is unlikely to be due to an alteration of the membrane electric field or the attraction of local counterions to the channel. Fatty acids and other negatively charged lipids were able to modulate BKCa channel activity in bathing solutions containing 0 mM Ca2+, 20 mM EGTA, suggesting that calcium is not required for this modulation. Taken together, these results indicate that modulation of BKCa channels by fatty acids and other charged lipids most likely occurs by their direct interaction with the channel protein itself or with some other channel associated component.




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