Accessibility navigation

Phorbol ester, but not ischemic preconditioning, activates protein kinase D in the rat heart

Brooks, G., Goss, M.W., Rozengurt, E. and Galinanes, M. (1997) Phorbol ester, but not ischemic preconditioning, activates protein kinase D in the rat heart. Journal of Molecular and Cellular Cardiology, 29 (8). pp. 2273-2284. ISSN 0022-2828

Full text not archived in this repository.

To link to this item DOI: 10.1006/jmcc.1997.0466


The signal transduction pathways that mediate the cardioprotective effects of ischemic preconditioning remain unclear. Here we have determined the role of a novel kinase, protein kinase D (PKD), in mediating preconditioning in the rat heart. Isolated rat hearts (n=6/group) were subjected to either: (i) 36 min aerobic perfusion (control); (ii) 20 min aerobic perfusion plus 3 min no-flow ischemia, 3 min reperfusion, 5 min no-flow ischemia, 5 min reperfusion (ischemic preconditioning); (iii) 20 min aerobic perfusion plus 200 nmol/l phorbol 12-myristate 13-acetate (PMA) given as a substitute for ischemic preconditioning. The left ventricle then was excised, homogenized and PKD immunoprecipitated from the homogenate. Activity of the purified kinase was determined following bincubation with [γ32P]-ATP±syntide-2, a substrate for PKD. Significant PKD autophosphorylation and syntide-2 phosphorylation occurred in PMA-treated hearts, but not in control or preconditioned hearts. Additional studies confirmed that recovery of LVDP was greater and initiation of ischemic contracture and time-to-peak contracture were less, in ischemic preconditioned hearts compared with controls (P<0.05). Our results suggest that the early events that mediate ischemic preconditioning in the rat heart occur via a PKD-independent mechanism.

Item Type:Article
Divisions:Faculty of Life Sciences > School of Biological Sciences > Biomedical Sciences
Interdisciplinary centres and themes > Institute for Cardiovascular and Metabolic Research (ICMR)
ID Code:16084
Uncontrolled Keywords:Cardioprotection; Ischemia; Phosphorylation; Signal transduction

University Staff: Request a correction | Centaur Editors: Update this record

Page navigation