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Alpha-mangostin dephosphorylates ERM to induce adhesion and decrease surface stiffness in KG-1 cells.

Thi Kieu Trang Phan^1,2, Thi Ly Do¹, Kouichi Tachibana^3,4

¹Department of Life and Environment Engineering, Faculty of Environmental Engineering, The University of Kitakyushu, 1-1 Hibikino, Wakamatsu, Kitakyushu, Fukuoka, 808-0135, Japan.

|November 24, 2021

Summary

This summary is machine-generated.

Alpha-mangostin, a natural compound, softens leukocyte cells by impacting their actin cytoskeleton. This study reveals it reduces cell stiffness and promotes adhesion through protein kinase C activation and ezrin/radixin/moesin dephosphorylation.

Keywords:

Alpha-mangostin ERM Leukocytes Mechanical stiffness PKC

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Area of Science:

Biophysics
Cell Biology
Biochemistry

Background:

Cell surface stiffness is crucial for cellular functions and states.
Alpha-mangostin is a natural compound known for bioactivities, including reducing cell mechanical stiffness.
The precise mechanism of alpha-mangostin's effect on the actin cytoskeleton and cell stiffness is not fully understood.

Purpose of the Study:

To elucidate the mechanism by which alpha-mangostin affects the surface stiffness of leukocytes.
To investigate the role of protein dephosphorylation and kinase activity in alpha-mangostin's effects on KG-1 cells.

Main Methods:

Treatment of KG-1 cells with alpha-mangostin.
Assessment of surface stiffness and microvilli disruption.
Inhibition studies using calyculin A (protein phosphatase inhibitor) and GF109203X (PKC inhibitor).
Analysis of ezrin/radixin/moesin (ERM) protein phosphorylation levels and protein kinase C (PKC) activity.

Main Results:

Alpha-mangostin significantly reduced the surface stiffness and disrupted microvilli of KG-1 cells.
The reduction in stiffness was partially reversed by calyculin A, suggesting phosphatase involvement.
Alpha-mangostin promoted KG-1 cell adhesion and decreased phosphorylated ERM levels, indicating ERM dephosphorylation.
PKC activity was increased by alpha-mangostin, and inhibiting PKC blocked the observed effects on stiffness and adhesion.

Conclusions:

Alpha-mangostin decreases leukocyte (KG-1 cell) surface stiffness and induces cell adhesion.
These effects are mediated by the activation of protein kinase C (PKC) and subsequent dephosphorylation of ezrin/radixin/moesin (ERM) proteins.
The findings provide mechanistic insight into how alpha-mangostin modulates cell mechanics and adhesion.