Abstract:
:The present investigation was designed to examine whether calmodulin is involved in the inhibition of the ATP-sensitive K+ (K(ATP)) channel by glucagon-like peptide 1(7-36) amide (GLP-1) in mouse pancreatic beta-cells. Membrane potential, single channel and whole-cell currents through the K(ATP) channels, and intracellular free Ca2+ concentration ([Ca2+]i) were measured in single mouse pancreatic beta-cells. Whole-cell patch-clamp experiments with amphotericin-perforated patches revealed that membrane conductance at around the resting potential is predominantly supplied by the K(ATP) channels in mouse pancreatic beta-cells. The addition of 20 nM GLP-1 in the presence of 5 mM glucose significantly reduced the membrane K(ATP) conductance, accompanied by membrane depolarization and the generation of electrical activity. A calmodulin inhibitor N-(6-aminohexyl)-5-chloro-1-naphthalenesulphonamide (W-7, 20 microM) completely reversed the inhibitory actions of GLP-1 on the membrane K(ATP) conductance and resultant membrane depolarization. Cell-attached patch recordings confirmed the inhibition of the K(ATP) channel activity by 20 nM GLP-1 and its restoration by 20 microM W-7 or 10 microM calmidazolium at the single channel level. Bath application of 20 microM W-7 also consistently abolished the GLP-1-evoked increase in [Ca2+]i in the presence of 5 mM glucose. These results strongly suggest that the mechanisms by which GLP-1 inhibits the K(ATP) channel activity accompanied by the initiation of electrical activity in mouse pancreatic beta-cells include a calmodulin-dependent mechanism in addition to the well-documented activation of the cyclic AMP-protein kinase A system.
journal_name
Exp Physioljournal_title
Experimental physiologyauthors
Ding WG,Kitasato H,Matsuura Hdoi
10.1113/eph8602173subject
Has Abstractpub_date
2001-05-01 00:00:00pages
331-9issue
3eissn
0958-0670issn
1469-445Xpii
EPH_2173journal_volume
86pub_type
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