ReferenceID 270

Emodin inhibits tonic tension through suppressing PKCδ-mediated inhibition of myosin phosphatase in rat isolated thoracic aorta

Br J Pharmacol

BACKGROUND AND PURPOSE: Dysregulated tonic tension and calcium sensitization in blood vessels has frequently been observed in many cardiovascular diseases. Despite a huge therapeutic potential, little is known about natu

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Reference Id
270
Evidence Id
16860
Core Evidence Id
16860
Source Reference Id
506
Herb2 Reference Id
HBREF000852
Subject Paper Key
HBIN025042_24909118
Pubmed Id
24909118
Doi
10.1111/bph.12804
Paper Title
Emodin inhibits tonic tension through suppressing PKCδ-mediated inhibition of myosin phosphatase in rat isolated thoracic aorta
Paper Abstract
BACKGROUND AND PURPOSE: Dysregulated tonic tension and calcium sensitization in blood vessels has frequently been observed in many cardiovascular diseases. Despite a huge therapeutic potential, little is known about natural products targeting tonic tension and calcium sensitization. EXPERIMENTAL APPROACH: We screened natural products for inhibitory effects on vasoconstriction using the rat isolated thoracic aorta and found that an anthraquinone derivative, emodin, attenuated tonic tension. Organ bath system, primary vascular smooth muscle cells, confocal microscopy and Western blot analysis were employed to demonstrate the suppressive effects of emodin on PKCδ-mediated myosin phosphatase inhibition. KEY RESULTS: Emodin, an active ingredient of Polygonum multiflorum extract, inhibited phenylephrine-induced vasoconstriction in rat isolated thoracic aorta, and inhibited vasoconstriction induced by 5-HT and endothelin-1. It also generally suppressed vasoconstrictions mediated by voltage-operated, store-operated calcium channels and intracellular calcium store. However, emodin did not affect agonist-induced calcium increases in primary smooth muscle cells. In contrast, post-treatment with emodin following phenylephrine stimulation potently suppressed tonic tension in rat aortic rings. Western blot analysis revealed that emodin inhibited phenylephrine-induced phospho-myosin light chain (pMLC) and the phosphorylation of myosin-targeting subunit and C-kinase-activated protein phosphatase-1 inhibitor (CPI-17). This was mediated by selective inhibition of PKCδ, whereas PKCα was not involved. CONCLUSION AND IMPLICATIONS: Emodin attenuates tonic tension through the blockade of PKCδ and CPI-17-mediated MLC-phosphatase inhibition. This new mode of action for the suppression of tonic tension and structural insights into PKCδ inhibition revealed by emodin may provide new information for the development of modulators of tonic tension and for the treatment of hypertension.
Journal
Br J Pharmacol
Publish Year
2014
Experiment Subject
rat, fadu-pflag-twist1 cancer cell
Experiment Type
Animal & Cell Experiment
Phenotype Related
Hypertension
Paper Title Cn
Paper Title En
Emodin inhibits tonic tension through suppressing PKCδ-mediated inhibition of myosin phosphatase in rat isolated thoracic aorta
Bilingual Status
semi_complete