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Synthetic Cell-Permeable caveolin-1 Scaffolding Domain Peptide Activates Phagocytosis of Escherichia Coli by Regulating Rab5 Activity

Makoto Hagiwara, Kenji Matsushita

Z Naturforsch C J Biosci. 2020 May 26;/j/znc.ahead-of-print/znc-2020-0023/znc-2020-0023.xml.

PMID: 32452824

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.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
IAR4241337 Caveolin-1 Scaffolding Domain Peptide, Cell-permeable Caveolin-1 Scaffolding Domain Peptide, Cell-permeable Price
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