Opposing actions of cGMP and calcium on the conductance of the F0 subunit c pore
Opposing actions of cGMP and calcium on the conductance of the F0 subunit c pore
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DOI:
10.1006/bbrc.2000.3231
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发表时间:
2000-08-11
影响因子:
3.1
通讯作者:
Guidotti, G
中科院分区:
文献类型:
--
作者:
McGeoch, JEM;McGeoch, MW;Guidotti, G
Subunit c of ATP synthase can be purified from neuronal plasma membrane and from the inner mitochondrial membrane, In the latter location the hydrophobic 75 amino acid protein is one component of the F-1 F-0 ATP synthase complex but in the former it is alone as a pore that is capable of generating spontaneous electrical oscillations. Pure mammalian subunit c when reconstituted in lipid bilayers and voltage clamped, yields a voltage sensitive pore that conducts a cation current regulated by calcium. The current is here found to be activated by cGMP with a K-M ranging from 14 nM to 19 mu M depending on calcium and temperature. It is sensitively inhibited by a number of ligands, The K-I for calcium ranges from 100 nM to 100 mu M depending on cGMP and temperature. DCCD inhibits with a K-app of 100 nM. The polyamine nicotine inhibits at 84 nM, The pore has properties that would allow it to deliver sodium or calcium through the cell membrane in a controlled manner while maintaining membrane polarization. (C) 2000 Academic Press.