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Am J Physiol Lung Cell Mol Physiol 279: L209-L215, 2000;
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Vol. 279, Issue 2, L209-L215, August 2000

Gs protein dysfunction in allergen-challenged human isolated passively sensitized bronchi

Pingfang Song, Manlio Milanese, Emanuele Crimi, Santina Bruzzone, Elena Zocchi, Kai Rehder, and Vito Brusasco

Cattedra di Fisiopatologia Respiratoria, Dipartimento di Scienze Motorie e Riabilitative, and Cattedra di Biochimica, Dipartimento di Medicina Sperimentale, Università di Genova, 16132 Genoa, Italy

We studied the intracellular mechanisms of allergen-induced beta 2-adrenoceptor dysfunction in human isolated passively sensitized bronchi. Sensitization was obtained by overnight incubation of bronchial rings with serum containing a high specific IgE level to Dermatophagoides but a low total IgE level. Allergen challenge was done by incubation with a Dermatophagoides mix. The Gs protein stimulant cholera toxin (2 µg/ml) displaced the carbachol (CCh) concentration-response curves of control and sensitized but not of challenged rings to the right. Cholera toxin (10 µg/ml) displaced the concentration-response curves to CCh of control, sensitized, and challenged rings to the right, but this effect was less in challenged rings. The effects of the Gi protein inhibitor pertussis toxin (250 ng/ml or 1 µg/ml) on salbutamol concentration-relaxation curves did not differ significantly between challenged and sensitized rings. The adenylyl cyclase activator forskolin and the Ca2+-activated K+-channel opener NS-1619 relaxed CCh-contracted bronchial rings without significant differences between control, sensitized, and challenged rings. Neither Gi nor Gs alpha -subunit expression differed between control, sensitized, and challenged tissues. We conclude that Gs protein dysfunction may be a mechanism of allergen-induced beta 2-adrenoceptor dysfunction in human isolated passively sensitized bronchi.

airway smooth muscle; calcium-activated potassium channels; adenylyl cyclase; Gi protein; beta -adrenergic receptors


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