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(Hypertension. 2003;41:751.)
© 2003 American Heart Association, Inc.

Scientific Contributions

Transduction of a Functional Domain of the AT₁ Receptor in Neurons by HIV-Tat PTD

Jorge Vázquez; Chengwen Sun; Jianqing Du; Lucía Fuentes; Colin Sumners; Mohan K. Raizada

From the Department of Physiology and Functional Genomics and the University of Florida, McKnight Brain Institute, Gainesville.

Correspondence to Mohan K. Raizada, PhD, Professor, Department of Physiology and Functional Genomics, PO Box 100274, University of Florida, College of Medicine, Gainesville, FL 32610. E-mail mraizada{at}phys.med.ufl.edu

Despite advances in transgenic and gene transfer technologies, in vivo structure–function studies of the angiotensin II type I receptor (AT₁R) have revealed limited information on the diverse actions of angiotensin II. Our objective in the present study was to determine if protein transduction technology with the use of the HIV-Tat protein transduction domain could fill this gap. Recombinant HIV-Tat protein transduction domain fused to EGFP and to the third intracellular loop of the AT₁R was expressed. Incubation of hypothalamus and brainstem neurons with this peptide indicated an efficient transport of the protein to most of the cells. This transduction was accompanied by an increase in neuronal firing rate, an effect similar to that observed with angiotensin II stimulation of the neuronal AT₁R. The characteristics of the chronotropic effects of recombinant third intracellular loop and its synthetic counterpart were similar and comparable to the effects of angiotensin II on these neurons. In addition, in the presence of the protein kinase C inhibitor calphostin C, the peptide failed to increase firing rate. These observations demonstrated that transduction of neurons with the third intracellular loop of the AT₁R produces chronotropic effects similar to those induced by angiotensin II. The data suggests that protein transduction technology could be useful for in vivo AT₁R domain transduction.

Key Words: receptors, angiotensin II • protein kinases • transduction technology

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