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Nitric Oxide-dependent Cilia Regulatory Enzyme Localization in Bovine Bronchial Epithelial Cells

Sarah L. Stout, Todd A. Wyatt, Jennifer J. Adams and Joseph H. Sisson

Pulmonary, Critical Care, Sleep & Allergy Section, Department of Internal Medicine, University of Nebraska Medical Center, Omaha, Nebraska (SLS,TAW,JHS); Department of Veterans Affairs, Research Service, Omaha, Nebraska (TAW); and Department of Anesthesiology and Critical Care Medicine, Johns Hopkins Hospital, Baltimore, Maryland (JJA)

Correspondence to: Joseph H. Sisson, MD, Pulmonary, Critical Care, Sleep & Allergy Medicine, Dept. of Internal Medicine, University of Nebraska Medical Center 985300, Omaha, NE 68198-5300. E-mail: jsisson{at}unmc.edu

Airway epithelial-derived nitric oxide (NO), through the activation of nucleotide cyclases and downstream kinases, stimulates ciliary beating, yet the precise locations of these enzymes are unknown. We hypothesized that these NO-activated enzymes are located within, or adjacent to, the ciliary axoneme. Immunohistochemistry of intact ciliated cells revealed that endothelial-type nitric oxide synthase (eNOS), the RII isoform of the cAMP-dependent protein kinase (PKA-RII), the type I isoform of the cGMP-dependent protein kinase (PKG-I), and guanylate cyclase ß (GC-ß) all colocalized with pericentrin to the basal body. In contrast, the PKA-RI isoform and the PKG-II isoform localized to ciliary axonemes. Western blot analysis of isolated demembranated ciliary preparations detected eNOS, GC-ß, and both isoforms of PKA and PKG. An A-kinase-anchoring protein was also detected. Our findings suggest that these enzymes are sequestered close to their points of action into a discrete ciliary metabolon, enabling targeted phosphorylation and efficient upregulation of ciliary beating. (J Histochem Cytochem 55:433–442, 2007)

Key Words: cilia • cAMP-dependent protein kinase • cGMP-dependent protein kinase • nitric oxide • alcohol

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