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RACK1, a PKC Targeting Protein, Is Exclusively Localized to Basal Airway Epithelial Cells

Rebecca E. Slager, Jane M. DeVasure, Jaqueline A. Pavlik, Joseph H. Sisson and Todd A. Wyatt

Pulmonary, Critical Care and Sleep Medicine Section, Department of Internal Medicine, University of Nebraska Medical Center, Omaha, Nebraska (RES,JMD,JAP,JHS,TAW), and Research Service, Department of Veterans Affairs Medical Center, Omaha, Nebraska (TAW)

Correspondence to: Todd A. Wyatt, PhD, Department of Internal Medicine, Pulmonary and Critical Care Medicine Section, University of Nebraska Medical Center, 985300 Nebraska Medical Center, Omaha, NE 68198-5300. E-mail: twyatt{at}unmc.edu

The novel isoform of protein kinase C (PKC), PKC, is an important regulator of ciliated cell function in airway epithelial cells, including cilia motility and detachment of ciliated cells after environmental insult. However, the mechanism of PKC signaling in the airways and the potential role of the PKC-interacting protein, receptor for activated C kinase 1 (RACK1), has not been widely explored. We used immunohistochemistry and Western blot analysis to show that RACK1 is localized exclusively to basal, non-ciliated (and non-goblet) bovine and human bronchial epithelial cells. Our immunohistochemistry experiments used the basal body marker pericentrin, a marker for cilia, β-tubulin, and an airway goblet cell marker, MUC5AC, to confirm that RACK1 was excluded from differentiated airway cell subtypes and is only expressed in the basal cells. These results suggest that PKC signaling in the basal airway cell may involve RACK1; however, PKC regulation in ciliated cells uses RACK1-independent pathways. (J Histochem Cytochem 56:7–14, 2008)

Key Words: receptor for activated C kinase 1 • protein kinase C • airway • cilia

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