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

FEBS Lett. 1993 Jan 25;316(2):175-80. doi: 10.1016/0014-5793(93)81210-q.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adolescent
  • Adult
  • Amino Acid Oxidoreductases / biosynthesis
  • Amino Acid Oxidoreductases / genetics*
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cell Line
  • Cerebellum / enzymology*
  • Cloning, Molecular
  • DNA
  • Female
  • Humans
  • Male
  • Molecular Sequence Data
  • Muscles / enzymology*
  • Nitric Oxide Synthase
  • RNA, Messenger / genetics
  • Rats
  • Sequence Homology, Amino Acid


  • RNA, Messenger
  • DNA
  • Nitric Oxide Synthase
  • Amino Acid Oxidoreductases

Associated data

  • GENBANK/L02881
  • GENBANK/L22015
  • GENBANK/X68456
  • GENBANK/X68457
  • GENBANK/X68458
  • GENBANK/X68459
  • GENBANK/X68460
  • GENBANK/X68461
  • GENBANK/X68462
  • GENBANK/X68463