Expression and Tyrosine Phosphorylation of E-Cadherin, β- and γ-Catenin, and Epidermal Growth Factor Receptor in Cervical Cancer Cells

Moon, Hye Sung; Choi, Eun A; Park, Hae Young; Choi, Jungkweon; Chung, Hye Won; Kim, Jong‐Il; Park, Won I.

doi:10.1006/gyno.2001.6163

Cited by 23 publications

(16 citation statements)

References 19 publications

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“…EGF receptor activity has been reported to modulate certain junctional proteins, leading to downregulation and protein degradation [9, 45–47]. The catenins are well studied, but less is known regarding the fate of cadherins in response to EGF receptor activation.…”

Section: Resultsmentioning

confidence: 99%

Differential Downregulation of E-Cadherin and Desmoglein by Epidermal Growth Factor

Chavez

Buhr

Petrie

et al. 2012

Dermatology Research and Practice

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Modulation of cell : cell junctions is a key event in cutaneous wound repair. In this study we report that activation of the epidermal growth factor (EGF) receptor disrupts cell : cell adhesion, but with different kinetics and fates for the desmosomal cadherin desmoglein and for E-cadherin. Downregulation of desmoglein preceded that of E-cadherin in vivo and in an EGF-stimulated in vitro wound reepithelialization model. Dual immunofluorescence staining revealed that neither E-cadherin nor desmoglein-2 internalized with the EGF receptor, or with one another. In response to EGF, desmoglein-2 entered a recycling compartment based on predominant colocalization with the recycling marker Rab11. In contrast, E-cadherin downregulation was accompanied by cleavage of the extracellular domain. A broad-spectrum matrix metalloproteinase inhibitor protected E-cadherin but not the desmosomal cadherin, desmoglein-2, from EGF-stimulated disruption. These findings demonstrate that although activation of the EGF receptor regulates adherens junction and desmosomal components, this stimulus downregulates associated cadherins through different mechanisms.

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Section: Resultsmentioning

confidence: 99%

Differential Downregulation of E-Cadherin and Desmoglein by Epidermal Growth Factor

Chavez

Buhr

Petrie

et al. 2012

Dermatology Research and Practice

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“…Angiogenic stimuli such as vascular endothelial growth factor (VEGF) [15], epidermal growth factor (EGF) [14], fibroblast growth factor (FGF) [12], and angiopoietin-1 [16] have produced inconsistent effects on induction of tyrosine phosphorylation of VE-cadherin. The literature suggests that VEGF and EGF may trigger tyrosine phosphorylation of VE-cadherin, disassembling the adherens junction complex through Src and Rac pathways [14,15]; angiopoietin-1 and FGF may dephosphorylate VE-cadherin to stabilize the endothelial barrier apparatus associated with β-integrin [12,16]. Observations from the present study displayed that ANG, an early identified angiogenic factor, was remarkably increased in endothelial layers in the microvasculature in multiple organs post-infection with R. conorii , and co-localized with SFG rickettsiae in the lesion.…”

Section: Discussionmentioning

confidence: 99%

Compartmentalized, functional role of angiogenin during spotted fever group rickettsia-induced endothelial barrier dysfunction: evidence of possible mediation by host tRNA-derived small noncoding RNAs

Gong

Lee

Lee³

et al. 2013

BMC Infect Dis

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BackgroundMicrovascular endothelial barrier dysfunction is the central enigma in spotted fever group (SFG) rickettsioses. Angiogenin (ANG) is one of the earliest identified angiogenic factors, of which some are relevant to the phosphorylation of VE-cadherins that serve as endothelial adherens proteins. Although exogenous ANG is known to translocate into the nucleus of growing endothelial cells (ECs) where it plays a functional role, nuclear ANG is not detected in quiescent ECs. Besides its nuclear role, ANG is thought to play a cytoplasmic role, owing to its RNase activity that cleaves tRNA to produce small RNAs. Recently, such tRNA-derived RNA fragments (tRFs) have been shown to be induced under stress conditions. All these observations raise an intriguing hypothesis about a novel cytoplasmic role of ANG, which is induced upon infection with Rickettsia and generates tRFs that may play roles in SFG rickettsioses.MethodsC3H/HeN mice were infected intravenously with a sublethal dose of R. conorii. At days 1, 3, and 5 post infection (p.i.), liver, lung and brain were collected for immunofluorescence (IF) studies of R. conorii and angiogenin (ANG). Human umbilical vein endothelial cells (HUVECs) were infected with R. conorii for 24, 48, and 72 hrs before incubation with 1μg/ml recombinant human ANG (rANG) in normal medium for 2 hrs. HUVEC samples were subjected to IF, exogenous ANG translocation, endothelial permeability, and immunoprecipitation phosphorylation assays. To identify small non-coding RNAs (sncRNAs) upon rickettsial infection, RNAs from pulverized mouse lung tissues and HUVECs were subjected to library preparation and deep sequencing analysis using an Illumina 2000 instrument. Identified sncRNAs were confirmed by Northern hybridization, and their target mRNAs were predicted in silico using BLAST and RNA hybrid programs.ResultsIn the present study, we have demonstrated endothelial up-regulation of ANG, co-localized with SFG rickettsial infection in vivo. We also have provided direct evidence that rickettsial infection sensitizes human ECs to the translocation of exogenous ANG in a compartmentalized pattern at different times post-infection. Typically, exogenous ANG translocates into the nucleus at 24 hrs and to the cytoplasm at 72 hrs post-infection. The ANG cytoplasmic translocation enhances phosphorylation and destabilization of VE-cadherin and attenuates endothelial barrier function. Of note, deep sequencing analysis detected tRFs, mostly derived from the 5'-halves of host tRNAs, that are induced by ANG. Northern hybridization validates the two most abundantly cloned tRFs derived from tRNA-ValGTG and tRNA-GlyGCC, in both mouse tissues and human cells. Bioinformatics analysis predicted that these tRFs may interact with transcripts associated with the endothelial barrier, the host cell inflammatory response, and autophagy.ConclusionsOur data provide new insight into the role of compartmentalized ANG during SFG rickettsioses, and highlight its possible mediation through tRFs.

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“…The HT-3 line was selected based on its ability to form cadherin-based cell-cell junctions at a level comparable to that of ME-180 (31). As with the ME-180 cells, Ab to ICAM-1 significantly blocked transmission of cell-associated HIV-1 across HT-3 cell monolayers when compared with untreated or isotype-control treated monolayers (Fig.…”

Section: Anti-icam-1 Abs Block Monocyte-associated Hiv-1 Transmissionmentioning

confidence: 99%

Lactobacilli-Expressed Single-Chain Variable Fragment (scFv) Specific for Intercellular Adhesion Molecule 1 (ICAM-1) Blocks Cell-Associated HIV-1 Transmission across a Cervical Epithelial Monolayer

Chancey

Khanna

Seegers

et al. 2006

The Journal of Immunology

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The vaginal and cervical epithelia provide an initial barrier to sexually acquired HIV-1 infection in women. To study the interactions between HIV-1-infected cells or cell-free HIV-1 and the reproductive epithelium, the transmission of HIV-1 by infected cells or cell-free virus across human cervical epithelial cells was examined using a Transwell culture system. Cell-associated HIV-1 was transmitted more efficiently than cell-free virus, and monocyte-associated virus was transmitted most efficiently. Abs to ICAM-1 added to the apical side of the epithelium blocked cell-mediated transepithelial HIV-1 transmission in vitro. When used in a previously described model of vaginal HIV-1 transmission in human PBL-SCID mice, anti-murine ICAM-1 Abs (0.4 μg/10 μl) also blocked vaginal transmission of cell-associated HIV-1 in vivo. To evaluate a candidate delivery system for the use of this Ab as an anti-HIV-1 microbicide, anti-ICAM single-chain variable fragment Abs secreted by transformed lactobacilli were evaluated for their protective efficacy in the Transwell model. Like the intact Ab and Fab derived from it, the single-chain variable fragment at a concentration of 6.7 μg/100 μl was able to reduce HIV-1 transmission by 70 ± 5%. These data support the potential efficacy of an anti-ICAM Ab delivered by lactobacilli for use as an anti-HIV-1 microbicide.

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Expression and Tyrosine Phosphorylation of E-Cadherin, β- and γ-Catenin, and Epidermal Growth Factor Receptor in Cervical Cancer Cells

Cited by 23 publications

References 19 publications

Differential Downregulation of E-Cadherin and Desmoglein by Epidermal Growth Factor

Differential Downregulation of E-Cadherin and Desmoglein by Epidermal Growth Factor

Compartmentalized, functional role of angiogenin during spotted fever group rickettsia-induced endothelial barrier dysfunction: evidence of possible mediation by host tRNA-derived small noncoding RNAs

Lactobacilli-Expressed Single-Chain Variable Fragment (scFv) Specific for Intercellular Adhesion Molecule 1 (ICAM-1) Blocks Cell-Associated HIV-1 Transmission across a Cervical Epithelial Monolayer

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