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Research Abstracts Online
January 2008 - March 2009

University of Minnesota Twin Cities
College of Biological Sciences and Medical School
Department of Biochemistry, Molecular Biology, and Biophysics

PI: Lincoln R. Potter

Identification of the Natriuretic Peptide Receptor A (NPR-A) Kinase

This research is designed to identify the cognate kinase of natriuretic peptide receptor A (NPR-A). NPR-A aids in the regulation of cardiovascular homeostasis by functioning in vivo to lower blood pressure and decrease intravascular volume. NPR-A requires phosphorylation to be activated, and desensitization of the receptor is accomplished by dephosphorylation. Thus regulation of phosphorylation of NPR-A is a critical control mechanism for this receptor.

The researchers are using several different techniques to identify the NPR-A kinase. These techniques include affinity purification of the kinase, in-gel kinase assays, and highly specific chemical crosslinking to NPR-A. The identification of interacting proteins from these methods will be assessed by mass spectrometric analysis, such as peptide mass fingerprinting by MALDI-TOF-MS. Alternatively, the researchers may use a human kinase siRNA screen to determine the NPR-A kinase.

Once the kinase is identified, the researchers will further confirm its relevance in cell culture systems utilizing both knockdown and overexpression techniques to determine its effect on NPR-A activity and phosphorylation status. In doing so, they hope to yield a pharmacologic target that can bolster NPR-A activity, which is often diminished in disease states such as congestive heart failure. Completion of this goal will advance knowledge of a critical regulator of the cardiovascular system.

Group Member

Andrea Yoder, Graduate Student