Thrombin Receptor Structure and Function

  1. S.R. Coughlin*,,
  2. R.M. Scarborough§,
  3. T.-K.H. Vu*, and
  4. D.T. Hung*,
  1. *Cardiovascular Research Institute, and Departments of Medicine and Laboratory Medicine, University of California, San Francisco, California 94143-0524; §COR Therapeutics, Inc., South San Francisco, California 94080

This extract was created in the absence of an abstract.

Excerpt

How do proteases that interact with the cell surface cause intracellular signaling events? One answer to this question was provided by the recent cloning and characterization of a functional thrombin receptor reviewed herein (Liu et al. 1991; Rasmussen et al. 1991; Vu et al. 1991a,b; Coughlin et al. 1992; Hung et al. 1992a,b,c,d; Scarborough et al. 1992).

Thrombin is a multifunctional serine protease generated at sites of vascular injury. Its varied actions on both soluble protein substrates and cells may be viewed as orchestrating not only hemostatic responses, but also perhaps inflammatory and proliferative responses to wounding. In addition to cleaving fibrinogen to the fibrin monomer to form the fibrous meshwork of blood clots, thrombin is a potent activator of a number of cell types. First and foremost, thrombin is the most potent stimulator of platelet aggregation (Davey and Luscher 1967; Shuman 1986), a thrombin activity probably critical in arterial...

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