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Liver cell myosin: isolation and properties.

T Ueno¹, T Sekine

¹Department of Biochemistry, School of Medicine, Juntendo University, Tokyo, Japan.

Biochemistry International

|December 1, 1987

Summary

Rabbit liver cells contain unique myosin, differing from blood vessel myosin. Phosphorylation of liver myosin light chains significantly activates its Mg2+-ATPase activity with F-actin.

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Area of Science:

Biochemistry
Cell Biology
Muscle Physiology

Background:

Myosin is a crucial motor protein involved in various cellular functions.
Understanding tissue-specific myosin isoforms is essential for comprehending diverse physiological processes.

Purpose of the Study:

To purify and characterize myosin from isolated rabbit liver cells.
To investigate the biochemical properties and functional differences of liver cell myosin compared to myosin from other sources.

Main Methods:

Purification of myosin from isolated rabbit liver cells.
Analysis of myosin heavy and light chain composition using SDS-PAGE.
Investigation of myosin light chain phosphorylation by chicken gizzard myosin light-chain kinase.
Assay of Mg2+-ATPase activity in the presence of F-actin.

Main Results:

Purified liver cell myosin consists of a 200-kDa heavy chain and 24-kDa, 22-kDa, and 17-kDa light chains.
Liver cell myosin exhibits distinct light chain composition and PPi-PAGE mobility compared to liver blood vessel myosin.
Phosphorylation of liver myosin light chains by myosin light-chain kinase resulted in a 10-fold activation of Mg2+-ATPase activity by F-actin.

Conclusions:

Rabbit liver cells possess a distinct myosin isoform with unique light chain composition.
The phosphorylation of liver myosin light chains plays a significant role in regulating its actin-activated Mg2+-ATPase activity.
These findings contribute to the understanding of tissue-specific myosin function and regulation.

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