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Am J Physiol Cell Physiol 283: C1399-C1413, 2002. First published July 3, 2002; doi:10.1152/ajpcell.00020.2002
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Vol. 283, Issue 5, C1399-C1413, November 2002

Differential autophosphorylation of CaM kinase II from phasic and tonic smooth muscle tissues

Jillinda M. Lorenz*, Marilyn H. Riddervold*, Elizabeth A. H. Beckett, Salah A. Baker, and Brian A. Perrino

Department of Physiology and Cell Biology, University of Nevada School of Medicine, Reno, Nevada 89557

Ca+/calmodulin-dependent protein kinase II (CaM kinase II) is regulated by calcium oscillations, autophosphorylation, and its subunit composition. All four subunit isoforms were detected in gastric fundus and proximal colon smooth muscles by RT-PCR, but only the gamma  and delta  isoforms are expressed in myocytes. Relative gamma  and delta  message levels were quantitated by real-time PCR. CaM kinase II protein and Ca2+/calmodulin-stimulated (total) activity levels are higher in proximal colon smooth muscle lysates than in fundus lysates, but Ca2+/calmodulin-independent (autonomous) activity is higher in fundus lysates. CaM kinase II in fundus lysates is relatively unresponsive to Ca2+/calmodulin. Alkaline phosphatase decreased CaM kinase II autonomous activity in fundus lysates and restored its responsiveness to Ca2+/calmodulin. Acetylcholine (ACh) increased autonomous CaM kinase II activity in fundus and proximal colon smooth muscles in a time- and dose-dependent manner. KN-93 enhanced ACh-induced fundus contractions but inhibited proximal colon contractions. The different properties of CaM kinase II from fundus and proximal colon smooth muscles suggest differential regulation of its autophosphorylation and activity in tonic and phasic gastrointestinal smooth muscles.

calmodulin; protein kinase; phosphorylation; tonic smooth muscle; phasic smooth muscle

* J. M. Lorenz and M. H. Riddervold contributed equally to this work.




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