Angiotensin AT
            <sub>1</sub>
            Receptor Stimulates Heat Shock Protein 27 Phosphorylation In Vitro and In Vivo

Meier, Matthias; King, George L.; Clermont, Allen C.; Perez, Alexandra; Hayashi, Michio; Feener, Edward P.

doi:10.1161/hy1201.096573

Cited by 28 publications

(18 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We recently reported that overexpression of Hsp27 in LNCaP cells suppressed castration-induced apoptosis and confers androgen resistance (23), whereas Hsp27 knockdown using ASO potently decreases Hsp27 levels, increases caspase-3 cleavage and apoptosis, enhances paclitaxel chemosensitivity, and delays tumor progression in vivo (22,23 . p38 kinase and Akt were reported to be the Hsp27 kinases (32,33), although protein kinase C (PKC) a and y and cyclic AMP-dependent kinase can also phosphorylate Hsp27 (43). Hsp27 becomes phosphorylated when exposed to angiotensin (43), interleukin-6 (IL-6), IL-1, heat shock and tumor necrosis factor-a (44).…”

Section: Discussionmentioning

confidence: 99%

Cooperative Interactions between Androgen Receptor (AR) and Heat-Shock Protein 27 Facilitate AR Transcriptional Activity

et al. 2007

View full text Add to dashboard Cite

Androgen receptor (AR) transactivation is known to enhance prostate cancer cell survival. However, the precise effectors by which the prosurvival effects of androgen and AR drive prostate cancer progression are poorly defined. Here, we identify a novel feed-forward loop involving cooperative interactions between ligand-activated AR and heat-shock protein 27 (Hsp27) phospho-activation that enhance AR stability, shuttling, and transcriptional activity, thereby increasing prostate cancer cell survival. Androgen-bound AR induces rapid Hsp27 phosphorylation on Ser 78 and Ser 82

show abstract

Section: Discussionmentioning

confidence: 99%

Cooperative Interactions between Androgen Receptor (AR) and Heat-Shock Protein 27 Facilitate AR Transcriptional Activity

et al. 2007

View full text Add to dashboard Cite

show abstract

“…Angiotensin II is shown to induce HSP27 phosphorylation through AT1-receptor activation (43). Phosphorylated HSP27 stabilizes actin filaments and plays a central role in SMC contraction.…”

Section: Biological Functions Of the Identified Proteins And Their Pomentioning

confidence: 99%

Proteome Analysis of Cultivated Vascular Smooth Muscle Cells from a CADASIL Patient

Ihalainen

Soliymani

Iivanainen

et al. 2007

Mol Med

View full text Add to dashboard Cite

Cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy (CADASIL) is a vascular dementing disease caused by mutations in the NOTCH3 gene, most which are missense mutations leading to an uneven number of cysteine residues in epidermal growth factor-like repeats in the extracellular domain of Notch3 receptor (N3ECD). CADASIL is characterized by degeneration of vascular smooth muscle cells (VSMC) and accumulation of N3ECD on the VSMCs of small and middle-sized arteries. Recent studies have demonstrated that impairment of Notch3 signaling is not the primary cause of the disease. In the present study we used proteomic analysis to characterize the protein expression pattern of a unique material of genetically genuine cultured human CADASIL VSMCs. We identified 11 differentially expressed proteins, which are involved in protein degradation and folding, contraction of VSMCs, and cellular stress. Our findings indicate that misfolding of Notch3 may cause endoplasmic reticulum stress and activation of unfolded protein response, leading to increased reactive oxygen species and inhibition of cell proliferation. In addition, upregulation of contractile proteins suggests an alteration in the signaling system of VSMC contraction. The accumulation of N3ECD on the cell surface possibly upregulates the angiotensin II regulatory feedback loop and thereby enhances the readiness of the cells to respond to angiotensin II stimulation.

show abstract

“…Angiotensin II (Ang II), the effector peptide of the rennin-angiotensin system formed as a result of sequential proteolysis of the angiotensinogen precursor, plays an important role in the development of hypertension and regulation of body fluid homeostasis. Interestingly, Ang II induces expression of Hsps in smooth muscle cell culture, aorta, and kidney (Xu et al 1995;Aizawa et al 2000;Meier et al 2001;Ishizaka et al 2002), and all suggest a protective role of Hsps against Ang II-induced end-organ injury. However, there is no direct evidence for HS treatment having an effect on Ang II-induced hypertension and inflammation.…”

Section: Introductionmentioning

confidence: 97%

Heat shock treatment protects against angiotensin II–induced hypertension and inflammation in aorta

Chen

Ross²,

Currie³

2004

Cell Stress Chaperones

View full text Add to dashboard Cite

Angiotensin II (Ang II) is a potent vasoconstrictor and induces inflammation and end-organ injury through its activation of the proinflammatory transcription factor, nuclear factor-B (NF-B). Heat shock (HS) treatment with subsequent expression of heat shock proteins (Hsps) is an effective strategy for tissue protection against oxidative injuries. Recently, HS and Hsps have been shown to interact with NF-B in tissue injury. In this study, we investigated whether HS could protect against Ang II-induced hypertension and inflammation by inhibiting NF-B. Sprague-Dawley rats were divided into control and HS groups. Control and 24-hour post-heat shocked rats were treated with Ang II. At days 1, 3, 5, 7, 11, and 14 after Ang II administration, systolic blood pressures were measured by tail-cuff plethysmography, and aorta tissues were collected. Aorta NF-B deoxyribonucleic acid-binding activity was measured by electrophoretic mobility shift assay, and NF-B p65 subunit, Hsp70, Hsp27, and interleukin-6 (IL-6) expressions were measured by Western analysis. HS treatment significantly decreased Ang II-induced hypertension. The activation of NF-B in aorta by Ang II was suppressed by HS treatment. The elevated expression of IL-6 induced by Ang II treatment was also decreased by HS treatment. Although Ang II treatment induced an increase in Hsp70 and Hsp27, HS treatment induced a greater elevation of Hsp70 and Hsp27 expression. HS treatment protects against Ang II-induced hypertension and inflammation. This protection may relate to the interaction of Hsps and the NF-B pathway.

show abstract

Angiotensin AT ₁ Receptor Stimulates Heat Shock Protein 27 Phosphorylation In Vitro and In Vivo

Cited by 28 publications

References 31 publications

Cooperative Interactions between Androgen Receptor (AR) and Heat-Shock Protein 27 Facilitate AR Transcriptional Activity

Cooperative Interactions between Androgen Receptor (AR) and Heat-Shock Protein 27 Facilitate AR Transcriptional Activity

Proteome Analysis of Cultivated Vascular Smooth Muscle Cells from a CADASIL Patient

Heat shock treatment protects against angiotensin II–induced hypertension and inflammation in aorta

Contact Info

Product

Resources

About

Angiotensin AT 1 Receptor Stimulates Heat Shock Protein 27 Phosphorylation In Vitro and In Vivo

Cited by 28 publications

References 31 publications

Cooperative Interactions between Androgen Receptor (AR) and Heat-Shock Protein 27 Facilitate AR Transcriptional Activity

Cooperative Interactions between Androgen Receptor (AR) and Heat-Shock Protein 27 Facilitate AR Transcriptional Activity

Proteome Analysis of Cultivated Vascular Smooth Muscle Cells from a CADASIL Patient

Heat shock treatment protects against angiotensin II–induced hypertension and inflammation in aorta

Contact Info

Product

Resources

About

Angiotensin AT ₁ Receptor Stimulates Heat Shock Protein 27 Phosphorylation In Vitro and In Vivo