Endothelin converting enzyme is located on α-actin filaments in smooth muscle cells

Barnes, Kay; Turner, Anthony J.

doi:10.1016/s0008-6363(99)00009-7

Cited by 23 publications

(17 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the rat prostate gland, big-ET, the inactive precursor of ET, was observed in the stroma and co-localised with a-actin of smooth muscle fibroblasts (Ventura and Salamoussa, 2002). Endothelinconverting enzyme-1 has also been shown to co-localise with a-actin in human vascular smooth muscle cells (Barnes and Turner, 1999). This implies that ET-1 is synthesised on demand from bigET in the stroma of the prostate.…”

Section: Discussionmentioning

confidence: 98%

Stromal–epithelial interactions influence prostate cancer cell invasion by altering the balance of metallopeptidase expression

et al. 2004

View full text Add to dashboard Cite

Perturbations of stromal -epithelial interactions in the developing tumour can contribute to cancer invasion and metastasis. The structurally related metallopeptidases endothelin-converting enzyme (ECE) and neutral endopeptidase (NEP) contribute sequentially to the synthesis and inactivation of ET-1, a mitogenic peptide that has been shown to affect tumour behaviour. This study has investigated the interaction between metastatic tumour epithelial cells, which lack NEP, and stromal cells, which we have shown to express ECE-1 (stromal -epithelial interactions), using Matrigel invasion chambers. The epithelial cell lines utilised in this study include androgen-sensitive LNCaP, androgen-independent PC-3, Du145 and recently established PNT-1a, PNT2-C2 and P4E6 prostate cell lines. Specific inhibition of endogenous ECE-1 activity in stromal cells reduced PC-3 and Du145 invasion by 70 and 50%, respectively. Addition of recombinant NEP to inactivate endogenous mitogenic peptides resulted in 50 and 20% reductions in invasion in PC-3 and Du145 cells, respectively. Neutral endopeptidase effects were reversed in the presence of thiorphan, a specific NEP inhibitor. Supplementation of defined media with bradykinin and ET-1 significantly increased PC-3 invasion by 40 and 50%, respectively. Du145 cell invasion increased by approximately 100% on adding ET-1. These studies implicate the metallopeptidases NEP and ECE-1 as mediators of prostate cancer invasion via a stromal/epithelial interaction.

show abstract

Section: Discussionmentioning

confidence: 98%

Stromal–epithelial interactions influence prostate cancer cell invasion by altering the balance of metallopeptidase expression

et al. 2004

View full text Add to dashboard Cite

show abstract

“…ECE-1 is expressed by endothelial, epithelial, smooth muscle, and neuronal cells, which are regulated by neuropeptides that are potential ECE-1 substrates (Barnes and Turner, 1997, 1999; Korth et al, 1999). Endosomal ECE-1 may regulate receptors in these cells provided the peptide and its receptor traffic to ECE-1– containing endosomes, and the peptide is an ECE-1 substrate at endosomal pH.…”

Section: Discussionmentioning

confidence: 99%

Endothelin-converting enzyme-1 regulates endosomal sorting of calcitonin receptor-like receptor and β-arrestins

Padilla

Cottrell

Roosterman

et al. 2007

The Journal of Cell Biology

121

View full text Add to dashboard Cite

Although cell surface metalloendopeptidases degrade neuropeptides in the extracellular fluid to terminate signaling, the function of peptidases in endosomes is unclear. We report that isoforms of endothelin-converting enzyme-1 (ECE-1a–d) are present in early endosomes, where they degrade neuropeptides and regulate post-endocytic sorting of receptors. Calcitonin gene-related peptide (CGRP) co-internalizes with calcitonin receptor-like receptor (CLR), receptor activity-modifying protein 1 (RAMP1), β-arrestin2, and ECE-1 to early endosomes, where ECE-1 degrades CGRP. CGRP degradation promotes CLR/RAMP1 recycling and β-arrestin2 redistribution to the cytosol. ECE-1 inhibition or knockdown traps CLR/RAMP1 and β-arrestin2 in endosomes and inhibits CLR/RAMP1 recycling and resensitization, whereas ECE-1 overexpression has the opposite effect. ECE-1 does not regulate either the resensitization of receptors for peptides that are not ECE-1 substrates (e.g., angiotensin II), or the recycling of the bradykinin B2 receptor, which transiently interacts with β-arrestins. We propose a mechanism by which endosomal ECE-1 degrades neuropeptides in endosomes to disrupt the peptide/receptor/β-arrestin complex, freeing internalized receptors from β-arrestins and promoting recycling and resensitization.

show abstract

“…However, other mechanisms may also be involved. Interestingly, ETconverting enzyme has recently been localized to the F-actin microfilament in smooth muscle cells (Barnes and Turner, 1999).…”

Section: Chen Et Almentioning

confidence: 99%

Interaction of Endothelin-1 with Vasoactive Factors in Mediating Glucose-Induced Increased Permeability in Endothelial Cells

Chen

Apostolova

Cherian

et al. 2000

Laboratory Investigation

View full text Add to dashboard Cite

SUMMARY: Alteration of endothelins (ET) and/or their receptors may be important in mediating vascular dysfunction in diabetes.We investigated mechanisms regulating ET-1 expression in human umbilical vein endothelial cells (HUVEC) in response to glucose and the functional significance of these mechanisms. Permeability across HUVEC, grown in medium containing either low (5 mmol/l) or high (25 mmol/l) D-glucose were investigated. L-glucose was used as a control. ET-1, ET A , and ET B mRNA were assessed by semiquantitative RT-PCR. ET-1 immunoreactivity and F-actin microfilament assembly were investigated using confocal microscopy. Increased transendothelial permeability was noted in cells cultured in high glucose or when the cells grown in low (physiologic) glucose were incubated with ET-1, vascular endothelial growth factor (VEGF), or N (G) -nitro-L-arginine methyl ester but not when they were incubated with ET-3, N(G)-nitro-D-arginine methyl ester, or L-glucose. Increased permeability was associated with increased ET-1, ET A , and ET B mRNA expression and augmented ET-1 immunoreactivity. High glucose induced increased permeability, increased ET-1, ET A , and ET B mRNA expression. ET-1 immunoreactivity was blocked by the protein kinase C (PKC) inhibitor chelerythrine, the specific PKC isoform inhibitor 379196, VEGF-neutralizing antibody, or the ET A blocker TBC11251, but was not blocked by the specific ET B blocker BQ788 or by a VEGF-non-neutralizing antibody. Increased permeability was also associated with deranged F-actin assembly in the endothelial cells and by derangement of endothelial cell junctions as assessed by electron microscopy. Data from this study suggest that high glucose-induced increased permeability may be induced through increased ET-1 expression and disorganization of F-actin assembly. ET-1 expression and increased permeability may occur secondary to PKC isoform activation and may be modulated by VEGF and nitric oxide. (Lab Invest 2000, 80:1311-1321.

show abstract

Endothelin converting enzyme is located on α-actin filaments in smooth muscle cells

Abstract: The 120 kDa endothelin converting enzyme co-localizes with alpha-actin in smooth muscle cells and resembles that found in endothelial cells in that it is present on both the plasma membrane and intracellularly.

Cited by 23 publications

References 43 publications

Stromal–epithelial interactions influence prostate cancer cell invasion by altering the balance of metallopeptidase expression

Stromal–epithelial interactions influence prostate cancer cell invasion by altering the balance of metallopeptidase expression

Endothelin-converting enzyme-1 regulates endosomal sorting of calcitonin receptor-like receptor and β-arrestins

Interaction of Endothelin-1 with Vasoactive Factors in Mediating Glucose-Induced Increased Permeability in Endothelial Cells

Contact Info

Product

Resources

About