Occludin induces microvillus formation via phosphorylation of ezrin in a mouse hepatic cell line

Murata, Masaki; Osanai, Makoto; Takasawa, Akira; Takasawa, Kumi; Aoyama, Tomoyuki; Kawada, Yuka; Yamamoto, Akihiro; Ono, Yoshio; Hiratsuka, Yutaro; Kojima, Takashi; Sawada, Norimasa

doi:10.1016/j.yexcr.2018.03.018

Cited by 3 publications

(3 citation statements)

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“…By phosphorylating ezrin, occludin promotes the production of microvilli, while occludin-knockout cells formed fewer microvilli. 46 The cytotoxicity induced by patulin was manifested by the destruction of TJ protein partly, 47 and the active-site inactivation of protein tyrosine phosphatases, which regulate how TJ proteins work. 48 According to the TEM images obtained in this work (Fig.…”

Section: Discussionmentioning

confidence: 99%

Saccharomyces cerevisiae: a patulin degradation candidate both in vitro and in vivo

et al. 2023

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Section: Discussionmentioning

confidence: 99%

Saccharomyces cerevisiae: a patulin degradation candidate both in vitro and in vivo

et al. 2023

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“…The increased OCLN accumulation beneath the virions was associated with very efficient particle internalization (Figure 4I), indicating that a certain threshold of OCLN may be required for HCV internalization. Previous links have been established between OCLN and Ezrin phosphorylation, [48,49] but further studies will be required to fully elucidate the complex series of events leading to efficient HCV internalization.…”

Section: Discussionmentioning

confidence: 99%

Occludin stalls HCV particle dynamics apart from hepatocyte tight junctions, promoting virion internalization

Deffieu¹,

Clément²,

Dorobantu³

et al. 2022

Hepatology

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HAL is a multi-disciplinary open access archive for the deposit and dissemination of scientific research documents, whether they are published or not. The documents may come from teaching and research institutions in France or abroad, or from public or private research centers. L'archive ouverte pluridisciplinaire HAL, est destinée au dépôt et à la diffusion de documents scientifiques de niveau recherche, publiés ou non, émanant des établissements d'enseignement et de recherche français ou étrangers, des laboratoires publics ou privés.

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“…Occludin is a protein of the claudin group and the key component of tight junction [18], playing a pivotal role in maintaining their barrier properties. Therefore, absence or mutation of occludin could increase epithelial leakiness, which is a critical barrier to cancer prevention [19], and it can also cause reduced adhesion and tight junction function and increased invasion in breast cancer tissues [20]. In addition, occludin participates in the regulation of apoptosis, disruption of which is an important aspect of a number of diseases [21].…”

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confidence: 99%

miR-132 mediates cell permeability and migration by targeting occludin in high-glucose -induced ARPE-19 cells

et al. 2021

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This study investigated the effects and mechanisms of miR-132 related to the permeability and mobility of human retinal pigment epithelium ARPE-19 cells in high-glucose (HG) condition. ARPE-19 cells were cultured in normal and HG condition and identified by immunofluorescence staining. Cell viability was assessed by the MTT assay, cell permeability was assessed by the FITC-dextran assay and cell mobility was assessed by the wound healing assay. Different miRNA and mRNA expression levels were determined by quantitative real-time polymerase chain reaction (RT-qPCR). The expression of tight junction-related proteins was determined by Western blot assay and immunofluorescence. The interaction between occludin and miR-132 was confirmed by a dual-luciferase reporter assay. We revealed that HG-treated ARPE-19 cells exhibited significantly increased miR-132 expression, decreased expression of the tight-junction markers including occludin and Ecadherin, and increased cell mobility and permeability. Occludin is a direct target of miR-132, which could regulate cell viability, mobility and permeability under HG condition through the JAK/STAT3 signaling pathway. These are the first data to suggest that miR-132 may contribute to the progression of diabetic retinopathy (DR) and that targeting the effect of miR-132 on occudin and the JAK/STAT3 pathway could represent a novel effective DR-treatment strategy.

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Occludin induces microvillus formation via phosphorylation of ezrin in a mouse hepatic cell line

Cited by 3 publications

References 58 publications

Saccharomyces cerevisiae: a patulin degradation candidate both in vitro and in vivo

Saccharomyces cerevisiae: a patulin degradation candidate both in vitro and in vivo

Occludin stalls HCV particle dynamics apart from hepatocyte tight junctions, promoting virion internalization

miR-132 mediates cell permeability and migration by targeting occludin in high-glucose -induced ARPE-19 cells

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