The AT1 receptor is important for blood pressure. The signaling mechanisms of the receptor is of particular interest in order to understand the overall effect of angiotensin 11 binding to the receptor. The proposal herein addresses:
Specific Aim 1 : To investigate the importance of the five tyrosines located on the carboxyl tail of the AT receptor for G-protein coupling and/or activation. Hypothesis - The tyrosines on the carboxyl tail of the AT1 receptor are necessary for -protein coupling and/or activation.
Specific Aim 2 : To investigate the significance of the five tyrosines located on the carboxyl tail of the AT1 receptor for tyrosine kinase activity. Hypothesis - The mutation of the five tyrosines on the carboxyl tail of the AT receptor does not disrupt the coupling of the receptor to intracellular tyrosine kinase proteins.

Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
1F32HL010269-01
Application #
6013696
Study Section
Pathology A Study Section (PTHA)
Program Officer
Bishop, Terry Rogers
Project Start
1999-12-31
Project End
Budget Start
1999-07-01
Budget End
2000-06-30
Support Year
1
Fiscal Year
1999
Total Cost
Indirect Cost
Name
Emory University
Department
Pathology
Type
Schools of Medicine
DUNS #
042250712
City
Atlanta
State
GA
Country
United States
Zip Code
30322
Bernstein, K E; Sayeski, P P; Doan, T et al. (2001) Signal transduction pathways of angiotensin II in the kidney. Contrib Nephrol :16-33
Doan, T N; Ali, M S; Bernstein, K E (2001) Tyrosine kinase activation by the angiotensin II receptor in the absence of calcium signaling. J Biol Chem 276:20954-8