AJP - Heart Calcium Transients and Cell-Sarcomere
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Am J Physiol Heart Circ Physiol 281: H2304-H2309, 2001;
0363-6135/01 $5.00
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Vol. 281, Issue 6, H2304-H2309, December 2001

SPECIAL TOPIC
Nitric oxide and cGMP protein kinase activity in aged ventricular myocytes

Qihang Zhang, Bruno Molino, Lin Yan, Todd Haim, Yakir Vaks, Peter M. Scholz, and Harvey R. Weiss

Heart and Brain Circulation Laboratory, Departments of Physiology and Biophysics and Surgery, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854

We tested the hypothesis that nitric oxide-induced negative functional effects through cGMP would be reduced in aged cardiac myocytes. Maximum rate of shortening (Rmax) and percent shortening of ventricular myocytes from young (6 mo) and old (3 y) rabbits were studied using a video edge detector. cGMP-dependent phosphorylation was examined by electrophoresis and autoradiography. Myocytes received a nitric oxide donor S-nitroso-N-acetyl-penicillamine (SNAP, 10-7, 10-6, and 10-5 M) followed by KT-5823 (10-6 M), a cGMP protein kinase inhibitor. Baseline function was similar in young and old myocytes (89.1 ± 4.5 young vs. 86.4 ± 8.3 µm/s old Rmax, 5.6 ± 0.3 vs. 5.2 ± 0.7%shortening). SNAP (10-5 M) decreased Rmax in both young (25%, n = 6) and old myocytes (24%, n = 7). SNAP also reduced percent shortening by 28% in young and 23% in old myocytes. The negative effects of SNAP were partially reversed by KT-5823 only in young myocytes. Multiple proteins were phosphorylated by cGMP, and KT-5823 could reduce this effect. The degree of phosphorylation was significantly less in old myocytes. These results suggest that the functional response of ventricular myocytes to nitric oxide was preserved during aging. However, the importance of cGMP-dependent protein phosphorylation was decreased, indicating a shift to other pathways.

cardiac myocytes; aging; rabbit; myocyte function


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