Abstract
The rat thrombin receptor (TR-1) has been expressed in Sf9 cells. Two mutant receptors, one lacking a thrombin cleavage site (RTRM), and the other containing only the extracellular domain of the receptor (ECD), have been expressed. Antibodies to the thrombin receptor activating peptide (TRAP) and to the fibrinogen-binding exosite have been prepared. On Western blots these antibodies bound to TR-1 bands of 65–70 kDa and 44 kDa, similar bands for RTRM, and a doublet of about 10 and 12 kDa for ECD. The free cytosolic Ca++ concentration, measured by Fura-2, increased after thrombin or TRAP stimulation in the cells expressing TR-1. The RTRM cells did not respond to thrombin and had an attenuated response to TRAP. The ECD protein was found in the medium; it was not glycosylated. Both the mutants and the antibodies should be useful for studies of TR-1 structure and function. © 1997 Elsevier Science Ltd
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
