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Updated: Aug 14, 2026
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Platelet-based Detection of Nitric Oxide in Blood by Measuring VASP Phosphorylation
Published on: January 7, 2019
Myosin light chain phosphorylation is correlated with cold-induced changes in platelet shape
H Kawakami1, M Higashihara, M Ohsaka
1Department of Anatomy, Kyorin University School of Medicine, Mitaka, Tokyo, Japan. kaha@kyorin-u.ac.jp
Summary
Cold temperatures cause platelet shape changes, including filopodia formation. This is linked to reversible myosin light chain (LC20) phosphorylation and actin interactions, crucial for these cold-induced transformations.
Area of Science:
- Hematology
- Cell Biology
- Biochemistry
Background:
- Platelets undergo morphological changes in response to various stimuli.
- Understanding cold-induced platelet alterations is important for transfusion medicine and cryopreservation.
Purpose of the Study:
- To investigate the molecular mechanisms underlying cold-induced platelet shape changes.
- To determine the role of myosin light chain phosphorylation in these transformations.
Main Methods:
- Observing platelet shape changes upon chilling.
- Measuring 20-kDa myosin light chain (LC20) phosphorylation.
- Analyzing myosin localization using Triton X-insoluble fraction and immunocytochemistry.
Main Results:
- Chilling induced time-dependent platelet shape changes from disks to spheres with filopodia.
- These shape changes correlated with LC20 phosphorylation, which was reversible.
- Myosin localized to filamentous structures within filopodia in chilled platelets.
Conclusions:
- LC20 phosphorylation is critical for cold-induced platelet shape changes.
- Actin filament interactions with phosphorylated myosin drive filopodia formation in chilled platelets.
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