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Heat shock treatment suppresses angiotensin II-induced activation of NF-B pathway and heart inflammation: a role for IKK depletion by heat shock?

¹Department of Anatomy and Neurobiology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 1X5, and ²Laboratoire Stress Oxidant, Chaperons et Apoptose, Centre de Génétique Moleculaire et Cellulaire, Centre National de la Recherche Scientifique UMR-5534, Université Claude Bernard Lyon-1, 69622 Villeurbanne, France

Submitted 3 February 2004 ; accepted in final form 7 April 2004

Heat shock (HS) proteins (Hsps) function in tissue protection through their chaperone activity and by interacting with cell signaling pathways to suppress apoptosis. Here, we investigated the effect of HS treatment on the nuclear factor (NF)-B signaling pathway in the angiotensin II (ANG II) model of inflammation. Male Sprague-Dawley rats were divided into sham and HS-, ANG II-, and HS + ANG II-treated groups. HS treatment was administered 24 h before the initiation of ANG II infusion. HS treatment (42°C for 15 min) decreased 7-day ANG II-induced hypertension from 191 ± 4 to 147 ± 3 mmHg (P < 0.01). Histological staining of hearts showed that HS treatment reduced ANG II-induced leukocyte infiltration, perivascular and interstitial inflammation, and fibrosis. Heart NF-B nuclear translocation and activity, examined by Western blot analysis and electrophoretic mobility shift assay, was suppressed by HS treatment. HS treatment depleted IB kinase- (IKK-) and phosphorylated IKK- and suppressed the depletion of IB- and the accumulation of phosphorylated IB-. HS treatment blocked ANG II induced expression of IL-6 and ICAM-1 in the heart. ANG II and HS treatment induced high-level expression of Hsp27 and Hsp70 and their phosphorylation. Phosphorylated isoforms of Hsp27 and Hsp70 may play an important role in protecting the heart against ANG II-induced inflammation.

heat shock proteins; IB-; IB kinase-; nuclear factor-B; protein phosphorylation; hypertension

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