Cited by 546Nitric Oxide and Endothelin EffectsMuscle Physiology and DisordersHemoglobin structure and function

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

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Nakane, Masaki, Schmidt, Harald H.H.W., Pollock, Jennifer S., Förstermann, Ulrich, Murad, Ferid·1993·FEBS Letters

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.

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  • Skeletal muscle contains significant levels of active neuronal NOS (nNOS or NOS1).

    “However, Murad et al. found in 1993 that neuronal NOS (nNOS or NOS1) is expressed in skeletal muscle tissue in significant quantities [21].”

    From Skeletal muscle as an endogenous nitrate reservoir (2015) · cites this paper as [21]

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Research works printed but not linked: 5

  1. Murad, F., Ishii, K., Gorsky, L., Fiistennann, U., Kerwin, J.F. and Heller, M. (1990) Nitric Oxide from L-Arginine: A Bioregula- tory System (S. Moncada and E.A. Higgs, eds.) pp. 301-315, Elsevier, Amsterdam.
  2. Knowles, R.G., Palacios, M., Palmer, R.M.J. and Moncada, S. (1989) Proc. Nat]. Acad. Sci. USA 86, 5159-5162.
  3. Bredt, D.S. and Snyder, S.H. (1990) Proc. Nat]. Acad. Sci. USA 87, 682685.
  4. O'Dell, T.J., Hawkins, R.D., Kandel, E.R. and Arancio, 0. (1991) Proc. Nat]. Acad. Sci. USA 88, 11285-l 1289.
  5. Lamas, S., Marsden, P.A.. Li. G.K., Tempst, P. and Michel, T. (1992) Proc. Nat]. Acad. Sci. USA 89, 6348-6352.

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Authors
Nakane, M., Schmidt, H. H. H. W., Pollock, J. S., Förstermann, U., & Murad, F.
Affiliations
  • Abbott (United States) (US)
  • Northwestern University (US)
Venue
FEBS Letters
Publisher
Wiley
Published
1993-01-25
Volume
316
Issue
2
Pages
175-180
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W2086823174
Cited by
546
References
28
Citations by year
2026: 1 · 2025: 3 · 2024: 2 · 2023: 2 · 2021: 2 · 2020: 5 · 2019: 4 · 2018: 5 · 2017: 4 · 2016: 7 · 2015: 12 · 2014: 10 · 2013: 4 · 2012: 8
FWCI
29.94
Type
journal article
Language
en
Open access
Locations
  • FEBS Letters (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Abbott Laboratories
  • National Institutes of Health (7r01dk030787-09, 7r01hl028474-08)
  • National Heart, Lung, and Blood Institute (HL-28474)
  • National Institute of Diabetes and Digestive and Kidney Diseases (DK 30787)
Topics
  • Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
Keywords
nitric oxide synthase, skeletal muscle, cDNA cloning, amino acid sequence, mRNA expression, nitric oxide
MeSH terms
Adolescent, Adult, Amino Acid Oxidoreductases, Amino Acid Sequence, Animals, Binding Sites, Cell Line, Cerebellum, Cloning, Molecular, DNA, Female, Humans, Male, Molecular Sequence Data, Muscles, RNA, Messenger, Sequence Homology, Amino Acid, Nitric Oxide Synthase, Rats

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