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Am J Physiol Lung Cell Mol Physiol (April 13, 2007). doi:10.1152/ajplung.00458.2006
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Submitted on November 18, 2006
Accepted on April 9, 2007

Respiratory syncytial virus induces insensitivity to beta-adrenergic agonists in mouse lung epithelium in vivo

Ian C Davis1, Anna Xu2, Zhiqian Gao1, Judy M Hickman-Davis1, Phillip Factor2, Wayne M Sullender3, and Sadis Matalon1*

1 Anesthesiology, University of Alabama at Birmingham, Birmingham, Alabama, United States
2 Pulmonary, Allergy and Critical Care Medicine, Columbia University, New York, New York, United States
3 Pediatrics, University of Alabama at Birmingham, Birmingham, Alabama, United States

* To whom correspondence should be addressed. E-mail: sadis{at}uab.edu.

Respiratory syncytial virus (RSV) is the most common cause of bronchiolitis in infants and children worldwide. We wished to determine whether intracheal administration of {beta}-agonists improved alveolar fluid clearance (AFC) across the distal respiratory epithelium of RSV infected mice. Following intranasal infection with RSV strain A2, AFC was measured in anesthetized, ventilated BALB/c mice by instillation of 5% BSA into the dependent lung. We found that direct activation of protein kinase A by forskolin or 8-bromo-cAMP increased AFC at day 2 after infection with RSV. In contrast, short- and long-acting {beta}-agonists had no effect at either day 2 or day 4. Insensitivity to {beta}-agonists was not a result of elevated plasma catecholamines, or lung epithelial cell {beta}-adrenergic receptor degradation. Instead, RSV infected mice had significantly higher levels of phosphorylated PKC{zeta} in the membrane fractions of their lung epithelial cells. In addition, insensitivity to {beta}-agonists was mediated in a paracrine fashion by KC (the murine homolog of CXCL8) and reversed by inhibition of either PKC{zeta} or G protein-coupled receptor kinase 2 (GRK2). These results indicate that insufficient response to {beta}-agonists in RSV may be caused, at least in part, by impaired {beta}-adrenergic receptor signaling, as a consequence of GRK2-mediated uncoupling of {beta}adrenergic receptors from adenylyl cyclase.




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