© 1996 American Heart Association, Inc.
Articles |
Depletion of Mitogen-Activated Protein Kinase Using an Antisense Oligodeoxynucleotide Approach Downregulates the Phenylephrine-Induced Hypertrophic Response in Rat Cardiac Myocytes
From the National Heart and Lung Institute (Cardiac Medicine) (P.E.G., S.K., S.J.F., P.H.S.), Imperial College of Science, Technology and Medicine, London, UK, and the Department of Biochemistry (E.M.S., G.J.S.), University of Southampton (UK).
Correspondence to Dr Peter E. Glennon, Unit of Cardiovascular Medicine, University of Cambridge School of Clinical Medicine, Department of Medicine, Level 5, Box 157, Addenbrookes Hospital, Hills Road, Cambridge CB2 2QQ, UK.
Abstract An antisense oligodeoxynucleotide (ODN) approach was used to investigate whether mitogen-activated protein kinase (MAPK) is necessary for the hypertrophic response in cardiac myocytes. A phosphorothioate-protected 17-mer directed against the initiation of translation sites of the p42 and p44 MAPK isoform mRNAs was introduced into cultured cardiac myocytes by liposomal transfection. At an antisense ODN concentration of 0.2 µmol/L, p42 MAPK protein was reduced by 82% (immunoblot) after 48 hours, and p42 and p44 MAPK activities were reduced by 44% and 60%, respectively. The same concentration of anti-MAPK ODN inhibited development of the morphological features of hypertrophy (sarcomerogenesis, increased cell size) in myocytes exposed to phenylephrine. Phenylephrine-induced activation of the atrial natriuretic factor (ANF) promoter (measured by the activity of a transfected ANF promoter/luciferase reporter gene) and induction of ANF mRNA (measured by RNase protection assay) were also attenuated. We conclude that MAPK is important for the development of the hypertrophic phenotype in this model of hypertrophy.
Key Words: antisense oligodeoxynucleotides • p42 and p44 mitogen-activated protein kinases • immunoblotting • atrial natriuretic factor expression • cardiac hypertrophy
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D. C. H. Ng, C. S. Long, and M. A. Bogoyevitch A Role for the Extracellular Signal-regulated Kinase and p38 Mitogen-activated Protein Kinases in Interleukin-1beta -stimulated Delayed Signal Tranducer and Activator of Transcription 3 Activation, Atrial Natriuretic Factor Expression, and Cardiac Myocyte Morphology J. Biol. Chem., July 27, 2001; 276(31): 29490 - 29498. [Abstract] [Full Text] [PDF]
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L. Wang, I. Gout, and C. G. Proud Cross-talk between the ERK and p70 S6 Kinase (S6K) Signaling Pathways. MEK-DEPENDENT ACTIVATION OF S6K2 IN CARDIOMYOCYTES J. Biol. Chem., August 24, 2001; 276(35): 32670 - 32677. [Abstract] [Full Text] [PDF]
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R. Gusterson, B. Brar, D. Faulkes, A. Giordano, J. Chrivia, and D. Latchman The Transcriptional Co-activators CBP and p300 Are Activated via Phenylephrine through the p42/p44 MAPK Cascade J. Biol. Chem., January 18, 2002; 277(4): 2517 - 2524. [Abstract] [Full Text] [PDF]
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F. Lin, W. A. Owens, S. Chen, M. E. Stevens, S. Kesteven, J. F. Arthur, E. A. Woodcock, M. P. Feneley, and R. M. Graham Targeted {alpha}1A-Adrenergic Receptor Overexpression Induces Enhanced Cardiac Contractility but not Hypertrophy Circ. Res., August 17, 2001; 89(4): 343 - 350. [Abstract] [Full Text] [PDF]
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