Endocytosis of CF in marginal cells of stria vascularis regulated by ROCK and MLCK signaling cascade, but not G-proteins.


Journal

Auris, nasus, larynx
ISSN: 1879-1476
Titre abrégé: Auris Nasus Larynx
Pays: Netherlands
ID NLM: 7708170

Informations de publication

Date de publication:
Oct 2019
Historique:
received: 29 10 2018
revised: 14 01 2019
accepted: 17 01 2019
pubmed: 12 2 2019
medline: 29 1 2020
entrez: 12 2 2019
Statut: ppublish

Résumé

Objective The endocytosis of cationized feritin (CF) via a clathrin-mediated pathway is regulated by a signaling network. Marginal cells showed the active endocytosis of CF via a clathrin-mediated pathway. The internalization of receptors through this clathrin-mediated pathway is an important regulatory event in signal transduction. Numerous kinases are involved in endocytosis, and each endocytic route is subjected to high-order regulation by cellular signaling mechanisms. In this study, we investigated whether ROCK and MLCK signaling cascades and G-proteins regulate the endocytosis of CF in marginal cells of the stria vascularis. Methods CF was infused into the cochlear duct with pertussis toxin (PTX),Clostridium botulinum C3 toxin (BTX), guanosine(g-thio)-triphosphate (GTP-γS), ML-7, Y-27632. Endocytic activity was measured at 30 min after the start of infusion under an electron microscope. Results In marginal cells, CF was internalized via a clathrin-mediated pathway that depends on F-actin and microtubules (MT). Its processes were controlled by myosin light chain kinase (MLCK) and Rho-associated kinase (ROCK), but not affected by G-protein-coupled receptor (GPCR) or the RhoA signaling cascade. Conclusion Our previous study showed that the main endocytotic pathway of microperoxidase (MPO) did not depend on the Rho/ROCK molecular switch or actin/myosin motor system, but was mainly regulated by the RhoA signaling cascade. The present study results indicate that these signaling cascades regulating CF internalization completely differ from the cascades for MPO internalization.

Identifiants

pubmed: 30739815
pii: S0385-8146(18)30937-4
doi: 10.1016/j.anl.2019.01.007
pii:
doi:

Substances chimiques

Amides 0
Azepines 0
Enzyme Inhibitors 0
Naphthalenes 0
Pyridines 0
Receptors, G-Protein-Coupled 0
polycationic ferritin 0
ML 7 109376-83-2
Y 27632 138381-45-0
Ferritins 9007-73-2
ADP Ribose Transferases EC 2.4.2.-
exoenzyme C3, Clostridium botulinum EC 2.4.2.-
Pertussis Toxin EC 2.4.2.31
rho-Associated Kinases EC 2.7.11.1
Myosin-Light-Chain Kinase EC 2.7.11.18
Myosin-Light-Chain Phosphatase EC 3.1.3.53
Botulinum Toxins EC 3.4.24.69
GTP-Binding Proteins EC 3.6.1.-
rhoA GTP-Binding Protein EC 3.6.5.2

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

790-796

Informations de copyright

Copyright © 2019. Published by Elsevier B.V.

Auteurs

Akinobu Kakigi (A)

Department of Otolaryngology-Head & Neck Surgery, Kobe University, Graduate School of Medicine, Hyogo, Japan. Electronic address: kakigia@med.kobe-u.ac.jp.

Teruhiko Okada (T)

Department of Anatomy, Kochi Medical School, Nankoku, Kochi, Japan.

Taizo Takeda (T)

Department of Otolaryngology, Kochi Medical School, Nankoku, Kochi, Japan.

Natsumi Uehara (N)

Department of Otolaryngology-Head & Neck Surgery, Kobe University, Graduate School of Medicine, Hyogo, Japan.

Ken-Ichi Nibu (KI)

Department of Otolaryngology-Head & Neck Surgery, Kobe University, Graduate School of Medicine, Hyogo, Japan.

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Classifications MeSH