PMID: 9159650Feb 1, 1997Paper

Modulation of inwardly rectifying ATP-regulated K+ channel by phosphorylation process in opossum kidney cells

The Japanese Journal of Physiology
M KubokawaT Kubota

Abstract

The role of phosphorylation in modulating an inwardly rectifying ATP-regulated K+ channel with inward conductance of about 90 pS was examined using the patch-clamp technique on opossum kidney (OK) cells. The activity of the inwardly rectifying K+ channel observed in cell-attached patches rapidly declined (channel "rundown") upon excision of the membrane into inside-out patches in a control bath solution (3 mM Mg2+, ATP-free). The declined channel activity was partially restored by applying ATP to the bath, and the ATP-induced channel restoration reached the near maximal level at an ATP concentration of 3 mM. The channel activity maintained by 3 mM ATP in inside-out patches was inhibited by K-252a (10 microM), a nonspecific protein kinase inhibitor, or KT5720 (200 nm), a specific inhibitor of cyclic AMP (cAMP)-dependent protein kinase (PKA), and was further stimulated by the addition of a catalytic subunit of PKA (20 nM). In cell-attached patches, the channel activity was also inhibited by K-252a (10 microM) or KT5720 (200 nM). The application of dibutyryl-cAMP (100 microM) alone failed to enhance channel activity, but significantly stimulated channel activity after the pretreatment of cells with Ro-20-1724 (100 microM), an inhi...Continue Reading

Citations

Dec 25, 2004·Physiological Reviews·Steven C HebertWenhui Wang
Sep 10, 2002·American Journal of Physiology. Renal Physiology·Kazuyoshi NakamuraManabu Kubokawa
May 14, 2004·American Journal of Physiology. Renal Physiology·Kazuyoshi NakamuraManabu Kubokawa

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