Abstract:
:The effects of cytosolic ATP on Ca2+-dependent K+ (K(Ca)) channel activation in cultured bovine adrenal chromaffin cells were investigated by using single-channel recording patch-clamp techniques. Application of ATP to the intracellular surface of excised inside-out patches activated K(Ca) channels in a dose-dependent manner at 30 microM to 10 mM. The K(Ca) channels also were activated by 3 mM of adenosine 5'-O-(3'-thiotriphosphate) (ATPgammaS), a non-hydrolyzable analogue of ATP, but not by 5'-adenylylimidodiphosphate (AMP-PNP) (from 300 microM to 3 mM). Furthermore, other nucleotides also activated K(Ca) channels in inside-out patches. This modulation took place without addition of exogenous protein kinase and was dependent on the presence of Mg2+ in the bathing solution. Staurosporine, a non-specific kinase inhibitor, or H-89 (N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinoline-sulfonamide), a cAMP-dependent protein kinase inhibitor, was unable to alter ATP-mediated K(Ca) channel activation. Following complete removal of Mg2+, a higher concentration of ATP (10 mM) and other nucleotides was required to activate K(Ca) channels; however, Mg2+ was ineffective in altering the activation of K(Ca) channels by itself. It is concluded that intracellular ATP and other nucleotides activate K(Ca) channels directly. These nucleotides may regulate catecholamine release by changing the cell membrane potential in adrenal chromaffin cells.
journal_name
Eur J Pharmacoljournal_title
European journal of pharmacologyauthors
Chen C,Houchi H,Tamaki T,Nakaya Ydoi
10.1016/s0014-2999(98)00239-8subject
Has Abstractpub_date
1998-06-05 00:00:00pages
293-9issue
2-3eissn
0014-2999issn
1879-0712pii
S0014-2999(98)00239-8journal_volume
350pub_type
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