Heat shock treatment suppresses angiotensin II-induced activation of NF-κB pathway and heart inflammation:: a role for IKK depletion by heat shock?
Heat shock treatment suppresses angiotensin II-induced activation of NF-κB pathway and heart inflammation:: a role for IKK depletion by heat shock?
复制标题
DOI:
10.1152/ajpheart.00102.2004
复制
发表时间:
2004-09-01
影响因子:
4.8
通讯作者:
Currie, RW
中科院分区:
文献类型:
--
作者:
Chen, Y;Arrigo, AP;Currie, RW
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)-kappaB 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 degreesC 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-kappa B nuclear translocation and activity, examined by Western blot analysis and electrophoretic mobility shift assay, was suppressed by HS treatment. HS treatment depleted I kappa B kinase-alpha (IKK-alpha) and phosphorylated IKK-alpha and suppressed the depletion of I kappa B-alpha and the accumulation of phosphorylated I kappa B-alpha. 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.