Localization of Tricellular Tight Junction Molecule LSR at Midbody and Centrosome During Cytokinesis in Human Epithelial Cells.


Journal

The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society
ISSN: 1551-5044
Titre abrégé: J Histochem Cytochem
Pays: United States
ID NLM: 9815334

Informations de publication

Date de publication:
01 2020
Historique:
pubmed: 31 10 2019
medline: 15 8 2020
entrez: 31 10 2019
Statut: ppublish

Résumé

Epithelial integrity and barrier function are maintained during cytokinesis in vertebrate epithelial tissues. The changes in localization and the roles of tricellular tight junction molecule lipolysis-stimulated lipoprotein receptor (LSR) during cytokinesis are not well known, although new tricellular tight junctions form at the flank of the midbody during cytokinesis. In this study, we investigated the changes in localization and the role of LSR at the midbody and centrosome during cytokinesis using human endometrial carcinoma cell line Sawano, comparing the tricellular tight junction molecule tricellulin; bicellular tight junction molecules occludin, claudin-7, zonula occludens-1, and cingulin; and the epithelial polarized related molecules apoptosis-stimulating of p53 protein 2, PAR3, and yes-associated protein. During cytokinesis induced by treatment with taxol, the epithelial barrier was maintained and the tricellular tight junction molecules LSR and tricellulin were concentrated at the flank of the acetylated tubulin-positive midbody and in γ-tubulin-positive centrosomes with the dynein adaptor Hook2, whereas the other molecules were localized there as well. All the molecules disappeared by knockdown using small interfering RNAs. Furthermore, by the knockdown of Hook2, the epithelial barrier was maintained and most of the molecules disappeared from the centrosome. These findings suggest that LSR may play crucial roles not only in barrier function but also in cytokinesis.

Identifiants

pubmed: 31662022
doi: 10.1369/0022155419886263
pmc: PMC6931164
doi:

Substances chimiques

Apoptosis Regulatory Proteins 0
Cell Cycle Proteins 0
Hook2 protein, human 0
LSR protein, human 0
Microtubule-Associated Proteins 0
Phosphoproteins 0
Receptors, Lipoprotein 0
TP53BP2 protein, human 0
Transcription Factors 0
YY1AP1 protein, human 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

59-72

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Auteurs

Takumi Konno (T)

Department of Cell Science, Research Institute for Frontier Medicine, Sapporo Medical University School of Medicine, Sapporo, Japan.

Takayuki Kohno (T)

Department of Cell Science, Research Institute for Frontier Medicine, Sapporo Medical University School of Medicine, Sapporo, Japan.

Shin Kikuchi (S)

Department of Anatomy, Sapporo Medical University School of Medicine, Sapporo, Japan.

Hiroshi Shimada (H)

Department of Cell Science, Research Institute for Frontier Medicine, Sapporo Medical University School of Medicine, Sapporo, Japan.
Department of Obstetrics and Gynecology, Sapporo Medical University School of Medicine, Sapporo, Japan.

Seiro Satohisa (S)

Department of Obstetrics and Gynecology, Sapporo Medical University School of Medicine, Sapporo, Japan.

Kenichi Takano (K)

Department of Otolaryngology, Sapporo Medical University School of Medicine, Sapporo, Japan.

Tsuyoshi Saito (T)

Department of Obstetrics and Gynecology, Sapporo Medical University School of Medicine, Sapporo, Japan.

Takashi Kojima (T)

Department of Cell Science, Research Institute for Frontier Medicine, Sapporo Medical University School of Medicine, Sapporo, Japan.

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Classifications MeSH