Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-20531
Nature 1994 Nov 24;3726504:366-9. doi: 10.1038/372366a0.
Show Gene links Show Anatomy links

Potassium channel block by cytoplasmic polyamines as the mechanism of intrinsic rectification.

Lopatin AN , Makhina EN , Nichols CG .


???displayArticle.abstract???
Inwardly rectifying potassium channels conduct ions more readily in the inward than the outward direction, an essential property for normal electrical activity. Although voltage-dependent block by internal magnesium ions may underlie inward rectification in some channels, an intrinsic voltage-dependent closure of the channel plays a contributory, or even exclusive, role in others. Here we report that, rather than being intrinsic to the channel protein, so-called intrinsic rectification of strong inward rectifiers requires soluble factors that are not Mg2+ and can be released from Xenopus oocytes and other cells. Biochemical and biophysical characterization identifies these factors as polyamines (spermine, spermidine, putrescine and cadaverine). The results suggest that intrinsic rectification results from voltage-dependent block of the channel pore by polyamines, not from a voltage sensor intrinsic to the channel protein.

???displayArticle.pubmedLink??? 7969496
???displayArticle.link??? Nature