Nectines et nectines-<i>like</i>

Fournier, Gilles; Garrido‐Urbani, Sarah; Reymond, Nicolas; Lopez, Marc

doi:10.1051/medsci/2010263273

Cited by 11 publications

(3 citation statements)

References 41 publications

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“…Besides their role in physiology, Nectins have been involved in different pathological processes in humans where they serve as virus receptors (poliovirus and herpes simplex virus), they are involved in orofacial malformation (CLPED1) and recently they have been described as markers, actors and potential therapeutic targets in cancer [13]–[14]. Nectin-2 and Nectin-4 are often overexpressed in tumours, and are associated with a poor prognosis [14].…”

Section: Introductionmentioning

confidence: 99%

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The Expression of the Nectin Complex in Human Breast Cancer and the Role of Nectin-3 in the Control of Tight Junctions during Metastasis

et al. 2013

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IntroductionNectins are a family of integral protein molecules involved in the formation of functioning Adherens and Tight Junctions (TJ). Aberrant expression is associated with cancer progression but little is known how this effects changes in cell behaviour. This study aimed to ascertain the distribution of Nectins-1 to -4 in human breast cancer and the effect on junctional integrity of Nectin-3 modulation in human endothelial and breast cancer cells.MethodsA human breast tissue cohort was processed for Q-PCR and immunohistochemistry for analysis of Nectin-1/-2/-3/-4. Nectin-3 over-expression was induced in the human breast cancer cell line MDA-MB-231 and the human endothelial cell line HECV. Functional testing was carried out to ascertain changes in cell behaviour.ResultsQ-PCR revealed a distinct reduction in node positive tumours and in patients with poor outcome. There was increased expression of Nectin-1/-2 in patients with metastatic disease, Nectin-3/-4 was reduced. IHC revealed that Nectin-3 expression showed clear changes in distribution between normal and cancerous cells. Nectin-3 over-expression in MDA-MB-231 cells showed reduced invasion and migration even when treated with HGF. Changes in barrier function resulted in MDAN3 cells showing less change in resistance after 2h treatment with HGF (p<0.001). Nectin-3 transformed endothelial cells were significantly more adhesive, irrespective of treatment with HGF (p<0.05) and had reduced growth. Barrier function revealed that transformed HECV cells had significantly tighter junctions that wildtype cells when treated with HGF (p<0.0001). HGF-induced changes in permeability were also reduced. Overexpression of Nectin-3 produced endothelial cells with significantly reduced ability to form tubules (p<0.0001). Immunoprecipitation studies discovered hitherto novel associations for Nectin-3. Moreover, HGF appeared to exert an effect on Nectin-3 via tyrosine and threonine phosphorylation.ConclusionsNectin-3 may be a key component in the formation of cell junctions and be a putative suppressor molecule to the invasion of breast cancer cells.

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Section: Introductionmentioning

confidence: 99%

“…Nectin-2 and Nectin-4 are often overexpressed in tumours, and are associated with a poor prognosis [14]. Indeed, Nectin-2 has been found to be over-expressed in clinical breast and ovarian cancer tissues by using gene expression profile analysis and immunohistochemistry studies [15].…”

Section: Introductionmentioning

confidence: 99%

The Expression of the Nectin Complex in Human Breast Cancer and the Role of Nectin-3 in the Control of Tight Junctions during Metastasis

et al. 2013

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“…Among these proteins, some have been implicated in the pathogenesis of IA in previous studies, such as the complement components C1, C3 and C5 [ 21 , 22 ] and the ECM remodeling-related proteins ECM1 and TIMP1 [ 23 ]. Furthermore, we also found a number of proteins that have never been reported but are involved in the injury and/or repair of vascular epithelial cells, cell adhesion and migration, and angiogenesis, such as pigment epithelium-derived factor (PEDF) [ 24 ], nectin-like protein 2 (NECL2) [ 25 ], ephrin A1 [ 26 ], neogenin [ 27 ], acheron [ 28 ], lumican [ 29 ] and Axl [ 30 - 33 ].…”

Section: Discussionmentioning

confidence: 99%

Identification of the soluble form of tyrosine kinase receptor Axl as a potential biomarker for intracranial aneurysm rupture

Yan

et al. 2015

BMC Neurol

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BackgroundSubarachnoid hemorrhage caused by a ruptured intracranial aneurysm (RIA) is a devastating condition with significant morbidity and mortality. Despite the fact that RIAs can be prevented by microsurgical clipping or endovascular coiling, there are no reliable means of effectively predicting IA patients at risk for rupture. The purpose of our study was to discover differentially-expressed glycoproteins in IAs with or without rupture as potential biomarkers to predict rupture.MethodsForty age/gender-matched patients with RIA, unruptured IA (UIA), healthy controls (HCs) and disease controls (DCs) (discovery cohort, n = 10 per group) were recruited and a multiplex quantitative proteomic method, iTRAQ (isobaric Tagging for Relative and Absolute protein Quantification), was used to quantify relative changes in the lectin-purified glycoproteins in CSF from RIAs and UIAs compared to HCs and DCs. Then we verified the proteomic results in an independent set of samples (validation cohort, n = 20 per group) by enzyme-linked immunosorbent assay. Finally, we evaluated the specificity and sensitivity of the candidate marker with receiver operating characteristic (ROC) curve methods.ResultsThe proteomic findings identified 294 proteins, 40 of which displayed quantitative changes unique to RIA, 13 to UIA, and 20 to IA. One of these proteins, receptor tyrosine kinase Axl, was significantly increased in RIA, as confirmed in CSF from the discovery cohort as well as in CSF and plasma from the validation cohort (p <0.05). Spearman’s correlation analysis revealed that the CSF and plasma Axl levels were strongly correlated (r = 0.93, p <0.0001). The ROC curve indicated an optimal CSF Axl threshold of 0.12 nM for discriminating RIA from UIA with corresponding sensitivity/specificity of 73.33%/90% and an area under the curve (AUC) of 0.89 (95% CI: 0.80-0.97, p < 0.0001). The optimal threshold for plasma Axl was 1.7 nM with corresponding sensitivity/specificity of 50%/80% and an AUC of 0.71 (95% CI: 0.54-0.87, p = 0.027).ConclusionsBoth CSF and plasma Axl levels are significantly elevated in RIA patients. Axl might serve as a promising biomarker to predict the rupture of IA.Electronic supplementary materialThe online version of this article (doi:10.1186/s12883-015-0282-8) contains supplementary material, which is available to authorized users.

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NECTIN-4 increased the 5-FU resistance in colon cancer cells by inducing the PI3K–AKT cascade

Das

Satapathy

Siddharth

et al. 2015

Cancer Chemother Pharmacol

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Nectines et nectines-like

Cited by 11 publications

References 41 publications

The Expression of the Nectin Complex in Human Breast Cancer and the Role of Nectin-3 in the Control of Tight Junctions during Metastasis

The Expression of the Nectin Complex in Human Breast Cancer and the Role of Nectin-3 in the Control of Tight Junctions during Metastasis

Identification of the soluble form of tyrosine kinase receptor Axl as a potential biomarker for intracranial aneurysm rupture

NECTIN-4 increased the 5-FU resistance in colon cancer cells by inducing the PI3K–AKT cascade

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