Dual Effects of Endothelin-1 (1-31): Induction of Mesangial Cell Migration and Facilitation of Monocyte Recruitment through Monocyte Chemoattractant Protein-1 Production by Mesangial Cells

Ishizawa, Keisuke; Yoshizumi, Masanori; Tsuchiya, Koichiro; Hishida, Hitoshi; Minakuchi, Kazuo; Izawa, Yuki; Kanematsu, Yasuhisa; Kubo, Shoji; Hirose, Masao; Takahashi, Toshiaki

doi:10.1291/hypres.27.433

Cited by 25 publications

(26 citation statements)

References 43 publications

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“…Finally, some groups have suggested that ET-1 (1-31) acts as a selective ET A agonist, albeit in in vitro models (Ishizawa et al, 2004;Zhou et al, 2006). In vivo, in the mouse model, however, ET A or ET B receptor blockade reduce or amplify, respectively, the pressor responses to Big ET-1, ET-1 (1-31), and ET-1.…”

Section: Discussionmentioning

confidence: 99%

Chymase-Dependent Conversion of Big Endothelin-1 in the Mouse in Vivo

Simard

Jin²,

Miyazaki³

et al. 2008

J Pharmacol Exp Ther

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The aim of this study was to identify the role of chymase in the conversion of exogenously administered Big endothelin-1 in the mouse in vivo. Real-time polymerase chain reaction analysis detected mRNA of mucosal mast cell chymases 4 and 5, endothelin-converting enzyme 1a, and neutral endopeptidase 24.11 in pulmonary, cardiac, and aorta homogenates derived from C57BL/6J mice, with the latter tissue expressing the highest levels of both chymase isoforms. Furthermore, hydrolysis of a fluorogenic peptide substrate, Suc-Leu-Leu-Val-Tyr-7-amino-4-methylcoumarin, was sensitive to the chymase inhibitors Suc-ValPro-PheS)-Gly-X-Phe-al, where X can be the amino acid Leu, Val, or Ile) (100 M) in supernatants extracted from the same tissue homogenates. In anesthetized mice, Big endothelin-1, endothelin-1 (1-31), and endothelin-1 triggered pressor responses (ED 50 s, 0.67, 0.89, and 0.16 nmol/kg) that were all reduced or potentiated by selective endothelin ET A or ET B receptor antagonists,, each at 1 mg/kg. The pressor responses to big endothelin-1 were significantly reduced by the neutral endopeptidase inhibitor thiorphan (DL-3-mercapto-2-benzylpropanoylglycine) (1 mg/kg) or the endothelin-converting enzyme inhibitorIn contrast, the responses to endothelin-1 (1-31) were abolished by thiorphan but unaffected by CGS 35066. In addition, Suc-Val-Pro-Phe P (OPh) 2 (20 -40 mg/kg) reduced, by more than 60%, the hemodynamic response to big endothelin-1 but not to endothelin-1 (1-31) and endothelin-1. Finally, intravenous administration of big endothelin-1 induced Suc-Val-Pro-Phe P -(OPh) 2 -sensitive increases in plasma-immunoreactive levels of endothelin-1 (1-31) and endothelin-1. The present study suggests that chymase plays a pivotal role in the conversion and cardiovascular properties of big endothelin-1 in vivo. , 2003). It is noteworthy that tissues derived from mice knockdown for both ECE-1 and ECE-2, which are nonviable past late gestational stages, still contain two thirds of mature endothelin peptides found in wild-type congeners, thus suggesting an important role for other pro- The authors of the present manuscript declare that there are no financial links, including consultancies with manufacturers of material or devices described in the article, and no links to the pharmaceutical industry or regulatory agencies or any other potential conflicts of interest.Article, publication date, and citation information can be found at http://jpet.aspetjournals.org. doi:10.1124/jpet.108.142992. -788, N-[N-[N-[(2,6-dimethyl-1-piperidinyl) ABBREVIATIONS: ECE, endothelin-converting enzyme; ET, endothelin; phosphoramidon, N-(␣-rhamno-pyranosyl-oxy-hydroxy-phosphinyl)-Leu-

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Section: Discussionmentioning

confidence: 99%

Chymase-Dependent Conversion of Big Endothelin-1 in the Mouse in Vivo

Simard

Jin²,

Miyazaki³

et al. 2008

J Pharmacol Exp Ther

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“…RMCs were isolated from intact glomeruli of 4-to 6-week-old male Sprague-Dawley rats and maintained in 18% fetal bovine serum (FBS) and RPMI 1640 as described previously (Ishizawa et al 2004). For the experiments, cells from passages 5 to 9 were used after 24-48 h of serum depletion.…”

Section: Cell Culture and Transfectionmentioning

confidence: 99%

“…To assess cell migration, a modified Boyden chamber assay was performed with minor modification to the method described previously (Ishizawa et al 2004). The assay was performed using Transwell chambers (6 .…”

Section: Rmc Migration Assaysmentioning

confidence: 99%

“…Increased glomerular MC turnover is a hallmark of CKD (Striker et al 1989). MC migration caused by various vasoactive substances is known to be critical for the development of glomerular sclerosis and also for the ECM organization process (Kagami et al 1999, Kohno et al 1999, Ishizawa et al 2004, Takeuchi et al 2006. In addition, the initial phase of the anti-Thy 1 nephritis model in animals characterized by mesangiolysis is followed by migration and proliferation of MCs (Bagchus et al 1990).…”

Section: Introductionmentioning

confidence: 99%

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Inhibitory effects of adiponectin on platelet-derived growth factor-induced mesangial cell migration

Ishizawa

Dorjsuren²,

Izawa‐Ishizawa³

et al. 2009

Journal of Endocrinology

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Adiponectin, an adipocyte-derived hormone, has been involved in metabolic syndrome, a known risk factor for the development of chronic kidney disease (CKD). Recent studies have demonstrated that plasma adiponectin levels are elevated when kidney function declines in patients with CKD. Excessive mesangial cell (MC) turnover is one of the important features of CKD. The aim of the present study is to elucidate the effects of adiponectin on platelet-derived growth factor (PDGF)-induced cell migration and intracellular signaling pathways, in cultured rat MCs (RMCs). PDGF-induced RMC migration was significantly inhibited by the pretreatment of adiponectin. Adiponectin alone had no effect on RMC migration. Big mitogen-activated protein (MAP) kinase 1 (BMK1), p38 MAP kinase, and Akt were activated by PDGF stimulation in a time-and concentration-dependent manner in RMC. Adiponectin alone did not affect BMK1, p38 MAP kinase, and Akt phosphorylations in RMC. PDGF-induced BMK1 and p38 MAP kinase phosphorylations were significantly attenuated by the pretreatment of adiponectin in RMCs. On the other hand, the phosphorylation of Akt by PDGF was not diminished by the pretreatment of adiponectin. Adiponectin had no effects on PDGF-receptor autophosphorylation by PDGF. We also confirmed that PDGF-induced RMC migration was significantly suppressed by siBMK1 transfection or SB203580, a p38 MAP kinase inhibitor. From these findings, it is implied that the elevated plasma adiponectin levels in patients with CKD might play a compensatory role aimed at counteracting renal dysfunction related to MC disorders.

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“…To assess cell migration, especially invasive displacement, a modified Boyden chamber assay was performed by minor modification to the method described previously (31). The assay was performed using Transwell chambers (6.5 mm, model 3422; Costar, Cambridge, USA) with an 8-μm pore polycarbonate membrane.…”

Section: Modified Boyden Chamber Assaymentioning

confidence: 99%

Big Mitogen-Activated Protein Kinase 1 (BMK1)/Extracellular Signal Regulated Kinase 5 (ERK5) Is Involved in Platelet-Derived Growth Factor (PDGF)-Induced Vascular Smooth Muscle Cell Migration

et al. 2007

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Dual Effects of Endothelin-1 (1-31): Induction of Mesangial Cell Migration and Facilitation of Monocyte Recruitment through Monocyte Chemoattractant Protein-1 Production by Mesangial Cells

Abstract: We previously found that human chymase selectively cleaves big endothelin-1 (ET-1) at the Tyr

Cited by 25 publications

References 43 publications

Chymase-Dependent Conversion of Big Endothelin-1 in the Mouse in Vivo

Chymase-Dependent Conversion of Big Endothelin-1 in the Mouse in Vivo

Inhibitory effects of adiponectin on platelet-derived growth factor-induced mesangial cell migration

Big Mitogen-Activated Protein Kinase 1 (BMK1)/Extracellular Signal Regulated Kinase 5 (ERK5) Is Involved in Platelet-Derived Growth Factor (PDGF)-Induced Vascular Smooth Muscle Cell Migration

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