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Article: Phosphorylation of the type I regulatory subunit of cAMP-dependent protein kinase in rat tissues. (Collegiate Communications--Undergraduate).(Brief Article)
- Article from:
- Proceedings of the North Dakota Academy of Science
- Article date:
- April 1, 2000
- Author:
CopyrightCOPYRIGHT 2000 North Dakota Academy of Science. This material is published under license from the publisher through the Gale Group, Farmington Hills, Michigan. All inquiries regarding rights should be directed to the Gale Group. (Hide copyright information)
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INTRODUCTION
cAMP-dependent protein kinase (PKA) is a multi functional enzyme regulating processes such as signaling, gene expression, anti cellular proliferation. A single phosphorylation site was identified in vivo at Ser-81 of the type I regulatory subunit (RI[alpha]) of PKA by electrospray ionization mass spectrometry (1). The role of phosphorylation is unknown. However, modulation of the phosphorylation state of Riot in response to CAMP modulating agents suggests that the phosphorylation may serve some physiological purpose (2,3,4). Hearts of spontaneously hypertensive rats (STIR) have been shown to have reduced levels of PKAI relative to normotensive rats ...
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