Startseite Synthetic cell-permeable caveolin-1 scaffolding domain peptide activates phagocytosis of Escherichia coli by regulating Rab5 activity
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Synthetic cell-permeable caveolin-1 scaffolding domain peptide activates phagocytosis of Escherichia coli by regulating Rab5 activity

  • Makoto Hagiwara und Kenji Matsushita EMAIL logo
Veröffentlicht/Copyright: 26. Mai 2020
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Abstract

Caveolae are defined as 50–100 nm wide pits in the plasma membrane containing oligomeric caveolin proteins. They have been implicated in endocytosis (including phagocytosis), transcytosis, calcium signalling, and numerous other signal transduction events. Caveolin-1, a major structural component of caveolae, enhances Rab5 activity. In this study, we examined the effect of a synthetic cell-permeable peptide of the caveolin-1 scaffolding domain (CSD) on phagocytosis. Treatment with the CSD peptide increased Rab5 activity, Rab5-early endosome antigen 1 (EEA1) interaction, and phagocytosis of Escherichia coli. The results suggest that the synthetic cell-permeable CSD peptide is an activator of phagocytosis.


Corresponding author: Kenji Matsushita, Department of Oral Disease Research, National Center for Geriatrics and Gerontology, 7-430 Morioka, 474-8522, Obu, Aichi, Japan, E-mail:

Acknowledgements

The authors thank Dr. G. Li (University of Oklahoma Health Science Center) for providing the GST-R5BD vector and Dr. Y. Yamamoto (Tokyo University of Agriculture) for providing the GFP-Rab5 vector.

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Received: 2020-02-04
Accepted: 2020-04-15
Published Online: 2020-05-26
Published in Print: 2020-09-25

© 2020 Walter de Gruyter GmbH, Berlin/Boston

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