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Published on: January 7, 2019
Moesin becomes linked to the plasma membrane in attached neutrophil granulocytes
M Keresztes1, Z Lajtos, J Fischer
1Department of Biochemistry, Albert Szent-Györgyi Medical University, 6701 Szeged, Hungary. margo@biochem.szote.u-szeged.hu
Abstract:
Following 35 min of adhesion to a plastic surface, an 80-kDa F-actin-binding protein was shown to be enriched in the plasma membrane fractions of porcine neutrophils by protein blotting with labeled F-actin. This protein was almost undetectable in membrane fractions of free floating neutrophils, while it was present in total cell samples. The 80-kDa protein appeared to be a major high molecular mass component of the isolated actin-cytoskeleton of both control and attached cells. The studied F-actin-binding protein was recognized by anti-moesin antibodies. Our results suggest that moesin is translocated to the plasma membrane upon adhesion of neutrophils to the extracellular surface.
Insights
Neutrophil adhesion to surfaces triggers the movement of an 80-kDa F-actin-binding protein to the plasma membrane. This protein, identified as moesin, is crucial for neutrophil cell structure and function.
Area of Science:
- Cell Biology
- Immunology
- Biochemistry
Background:
- Neutrophils play a critical role in the immune response.
- Cell adhesion is a fundamental process in cell biology and immunology.
- The actin cytoskeleton is essential for maintaining cell shape and function.
Purpose of the Study:
- To investigate the changes in protein localization within neutrophils upon adhesion.
- To identify F-actin-binding proteins that are recruited to the plasma membrane during neutrophil adhesion.
- To determine the role of moesin in neutrophil adhesion.
Main Methods:
- Porcine neutrophils were allowed to adhere to a plastic surface for 35 minutes.
- Protein blotting with labeled F-actin was used to detect F-actin-binding proteins.
- Plasma membrane and total cell fractions were analyzed.
- Immunoblotting with anti-moesin antibodies was performed.
Main Results:
- An 80-kDa F-actin-binding protein was significantly enriched in the plasma membrane fractions of adhered neutrophils.
- This 80-kDa protein was largely absent in the membrane fractions of non-adhered neutrophils.
- The 80-kDa protein was identified as moesin.
- Moesin was a major component of the isolated actin cytoskeleton in both adhered and non-adhered cells.
Conclusions:
- Neutrophil adhesion to a surface induces the translocation of moesin to the plasma membrane.
- Moesin is involved in the structural changes of neutrophils upon adhesion.
- These findings contribute to understanding neutrophil behavior during inflammatory responses.
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