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10.1007/s004240050251

http://scihub22266oqcxt.onion/10.1007/s004240050251
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9019734!?!9019734

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suck abstract from ncbi

pmid9019734      Pflugers+Arch 1996 ; 433 (1-2): 77-83
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  • Heterooligomeric assembly of inward-rectifier K+ channels from subunits of different subfamilies: Kir2 1 (IRK1) and Kir4 1 (BIR10) #MMPMID9019734
  • Fakler B; Bond CT; Adelman JP; Ruppersberg JP
  • Pflugers Arch 1996[Nov]; 433 (1-2): 77-83 PMID9019734show ga
  • Activities of strong inward-rectifier K+ channels composed of Kir2. 1(84 M), Kir2.1(84T) and Kir4.1 subunits and weak inward-rectifier K+ channels composed of Kir4.1(E158N) subunits were measured from giant inside-out patches of Xenopus laevis oocytes. The conductance/voltage (g/V) relationship for block by intracellular spermine (SPM) was biphasic for both Kir2.1 channel types while it was monophasic for both Kir4.1 channel types. The release of blocking Mg2+ ions was slow for Kir2.1(84T) but virtually instantaneous for Kir2.1(84M) and both Kir4.1 channel types. Coexpression of Kir2.1(84T) and Kir4.1(E158N) resulted in heterooligomeric channels which were strongly rectifying, with a g/V relationship for SPM-evoked block that was significantly different from that of either parental homooligomeric channel type. Block by intracellular Mg2+ was markedly stronger than that for Kir4.1(E158N) channels, while release of the block was almost instantaneous, similar to that for Kir4.1(E158N) channels. This suggests preferential formation of a particular heterooligomer such as was recently proposed for subunits within the Kir3.0 family.
  • |Animals[MESH]
  • |Electrophysiology[MESH]
  • |Female[MESH]
  • |Magnesium/pharmacology[MESH]
  • |Oocytes/metabolism[MESH]
  • |Potassium Channel Blockers[MESH]
  • |Potassium Channels/*chemistry/*physiology[MESH]
  • |Spermine/pharmacology[MESH]


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