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Waldegger, S; Raber, G; Sussbrich, H; Ruppersberg, J P; Fakler, B; Murer, H; Lang, F; Busch, A E (1996). Coexpression and stimulation of parathyroid hormone receptor positively regulates slowly activating IsK channels expressed in Xenopus oocytes. Kidney International, 49(1):112-116.

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Expression of the IsK protein in Xenopus oocytes induced the characteristically slow, voltage-dependent outward currents. Superfusion with the parathyroid hormone (PTH) peptide 1-34 had no effect on IsK when expressed alone, but increased IsK when IsK was coexpressed with the PTH-receptor. PTH receptor stimulation caused a shift of IsK conductance-voltage relationship to more negative potentials, and a decrease of both the rate of IsK activation and deactivation. IsK regulation by PTH was independent of extracellular Ca2+, and was also present IsK protein mutants lacking the protein kinase C consensus site. However, regulation of IsK by PTH was mimicked by activators of protein kinase A (PKA) and greatly reduced in the presence of the kinase inhibitors staurosporine and H89. These results suggest that PTH regulates IsK by a mechanism involving phosphorylation independent of protein kinase C (PKC). Such regulation may play a role in proximal tubule cells of the kidney, where both PTH receptor and the IsK protein are expressed.


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Additional indexing

Item Type:Journal Article, refereed
Communities & Collections:04 Faculty of Medicine > Institute of Physiology
07 Faculty of Science > Institute of Physiology
Dewey Decimal Classification:570 Life sciences; biology
Date:1 January 1996
Deposited On:11 Feb 2008 12:22
Last Modified:05 Apr 2016 12:18
Publisher:Nature Publishing Group
Publisher DOI:10.1038/ki.1996.15
PubMed ID:8770956

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