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[Cellular receptor of thrombin]

D Lasne¹, F Rendu, M Aiach

¹Laboratoire d'hémostase, hôpital Broussais, Paris, France.

Annales De Biologie Clinique

|January 1, 1994

Summary

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Researchers identified a new G protein-coupled receptor for thrombin (a key enzyme in blood clotting). This thrombin receptor activation mechanism involves protease cleavage and unmasking of a tethered ligand, mimicking thrombin

Area of Science:

Biochemistry
Cell Biology
G protein-coupled receptors

Context:

Thrombin, a serine protease, triggers diverse cellular responses via specific receptors.
Recent cloning and expression of the human thrombin receptor in Xenopus laevis oocytes have revealed its structure.
The receptor belongs to the seven transmembrane domain receptor superfamily, known for G protein interactions.

Purpose:

To characterize the structure and function of the newly identified thrombin receptor.
To elucidate the mechanism of thrombin-mediated cellular activation.
To investigate the role of agonist peptides in mimicking thrombin's cellular effects.

Summary:

The cloned thrombin receptor features a large extracellular N-terminal domain with a thrombin cleavage site (Leu-Asp-Pro-Arg).

Related Experiment Videos

Cleavage by thrombin unmasks a new N-terminus that acts as a tethered ligand, initiating receptor activation.

Synthetic peptides mimicking this unmasked N-terminus can activate the receptor and elicit cellular responses, confirming its role in thrombin signaling.

Impact:

Provides a molecular understanding of thrombin signaling pathways.
Identifies a novel G protein-coupled receptor involved in cellular responses to thrombin.
Offers potential therapeutic targets for diseases involving thrombin activity, such as thrombosis and inflammation.