Arginase modulates myocardial contractility by a nitric oxide synthase 1-dependent mechanism.

@article{Steppan2006ArginaseMM,
  title={Arginase modulates myocardial contractility by a nitric oxide synthase 1-dependent mechanism.},
  author={Jochen Steppan and Sungwoo Ryoo and Karl H. Schuleri and Chris Gregg and Rani K. Hasan and Anthony R. White and Lukasz J. Bugaj and Mehnaz Khan and Lakshmi Santhanam and Daniel P Nyhan and Artin A. Shoukas and Joshua M Hare and Dan E. Berkowitz},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2006},
  volume={103 12},
  pages={4759-64}
}
Cardiac myocytes contain two constitutive NO synthase (NOS) isoforms with distinct spatial locations, which allows for isoform-specific regulation. One regulatory mechanism for NOS is substrate (l-arginine) bioavailability. We tested the hypothesis that arginase (Arg), which metabolizes l-arginine, constrains NOS activity in the cardiac myocyte in an isoform-specific manner. Arg activity was detected in both rat heart homogenates and isolated myocytes. Although both Arg I and II mRNA and… CONTINUE READING

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Hypertension, in press. 4764 www.pnas.org cgi doi

  • A. R. White, S. Ryoo, +7 authors D. E. Berkowitz
  • 2006

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