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Volume 316, Issue 2 p. 175-180
Research letters
Free Access

Cloned human brain nitric oxide synthase is highly expressed in skeletal muscle

Masaki Nakane

Masaki Nakane

Vascular Biology, Abbott Laboratories, Abbott Park, Illinois 60064, USA

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Harald H.H.W. Schmidt

Harald H.H.W. Schmidt

Department of Pharmacology, Northwestern University Medical School, Chicago, Illinois 60611, USA

Present address: Medizinische Universitätsklinik, Klinische Forschergruppe, Josef-Schneider-Str. 2, W-8700 Würzburg, Germany. Search for more papers by this author
Jennifer S. Pollock

Jennifer S. Pollock

Vascular Biology, Abbott Laboratories, Abbott Park, Illinois 60064, USA

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Ulrich Förstermann

Ulrich Förstermann

Vascular Biology, Abbott Laboratories, Abbott Park, Illinois 60064, USA

Department of Pharmacology, Northwestern University Medical School, Chicago, Illinois 60611, USA

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Ferid Murad

Ferid Murad

Vascular Biology, Abbott Laboratories, Abbott Park, Illinois 60064, USA

Department of Pharmacology, Northwestern University Medical School, Chicago, Illinois 60611, USA

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First published: January 25, 1993
Citations: 395
Correspondence address: M. Nakane, D46B, AP10, Abbott Laboratories, Abbott Park, IL 60064, USA. Fax: (1) (708) 938-6107.

Abstract

Complementary DNA clones corresponding to human brain nitric oxide (NO) synthase have been isolated. The deduced amino acid sequence revealed an overall identity with rat brain NO synthase of about 93% and contained all suggested consensus sites for binding of the co-factors. The cDNA transfected COS-1 cells showed significant NO synthase activity with the typical co-factor requirements. Unexpectedly, messenger RNA levels of this isoform of NO synthase was more abundant in human skeletal muscle than human brain. Moreover, we detected high NO synthase activity and the expressed protein in human skeletal muscle by Western blot analysis, indicating a possible novel function of NO in skeletal muscle.