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CLONED HUMAN BRAIN NITRIC-OXIDE SYNTHASE IS HIGHLY EXPRESSED IN SKELETAL-MUSCLE
Author(s): NAKANE M, SCHMIDT HHHW, POLLOCK JS, FORSTERMANN U, MURAD F
Source: FEBS LETTERS    Volume: 316    Issue: 2    Pages: 175-180    Published: JAN 25 1993  
Times Cited: 448     References: 30     
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.
Document Type: Article
Language: English
Reprint Address: NAKANE, M (reprint author), ABBOTT LABS, VASC BIOL, D46B, AP10, ABBOTT PK, IL 60064 USA
Addresses:
1. NORTHWESTERN UNIV, SCH MED, DEPT PHARMACOL, CHICAGO, IL 60611 USA
Publisher: ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology
IDS Number: KH969
ISSN: 0014-5793
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