Related Experiment Video
Updated: Aug 14, 2026

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
Abstract:
Chilling induces shape changes in platelets from disks to spheres with abundant filopodia. Such changes were time-dependent and correlated well with the phosphorylation of 20-kDa myosin light chain (LC20). Both the shape changes and the phosphorylation were reversible. After the platelets had been chilled, myosin became incorporated into the Triton X-insoluble fraction. When the chilled platelets were immunocytochemically stained, anti-myosin antibody was localized with filamentous structures inside the filopodia. These results suggest that LC20 phosphorylation and subsequent interactions with actin filaments play a crucial role in the cold-induced changes in platelet shape and in the formation of filopodia.
More Related Videos
Related Concept Videos
Cross-bridge Cycle
The Contractile Ring
A small GTPase, RhoA, controls the function and assembly of the contractile ring. RhoA belongs to the Ras superfamily of proteins. The activation of formins by RhoA promotes...
Intracellular Signaling Affects Focal Adhesions
Some...
Smooth Muscle Contraction
The onset of contraction is triggered by an increase in calcium ions within the sarcoplasm, similar to the process in striated muscle. However, smooth muscles have a relatively smaller reservoir of the sarcoplasmic...

