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Thrombin, a survival factor for cultured myoblasts.

C Chinni¹, M R de Niese, D J Tew

¹Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3168, Australia.

The Journal of Biological Chemistry

|March 27, 1999

Summary

Thrombin inhibits myoblast fusion but protects myoblasts from apoptosis, acting as a survival factor. This protective effect is mediated by an unknown thrombin receptor, suggesting a role in muscle development and repair.

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Area of Science:

Muscle Biology
Cell Signaling
Protease-Activated Receptors (PARs)

Background:

Protease-activated receptors (PARs) are key mediators of cellular responses to proteases.
PAR-1, -3, and -4 are identified as thrombin receptors.
PAR-1 expression decreases as myoblasts differentiate and fuse into myotubes.

Purpose of the Study:

To investigate the hypothesis that thrombin inhibits myoblast fusion.
To explore thrombin's effects on myoblast apoptosis and survival.

Main Methods:

Primary rodent myoblast cultures were serum-deprived to induce fusion.
Cultures were treated with or without thrombin.
Apoptosis and fusion rates were assessed.
PAR-activating peptides were used to probe receptor involvement.

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Main Results:

Thrombin significantly inhibited myoblast fusion.
Thrombin markedly reduced apoptosis in serum-deprived myoblasts.
Proteolysis was essential for thrombin's effects.
Neither PAR-1 nor PAR-4 activating peptides mimicked thrombin's protective effects.
An unidentified thrombin receptor mediated the protective action via a secreted factor.

Conclusions:

Thrombin acts as a survival factor for myoblasts, protecting them from apoptosis.
The protective mechanism involves an unknown thrombin receptor and a secreted inhibitor.
Thrombin likely plays a crucial role in muscle development and repair processes.