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

FEBS Letters

Förstermann, Ulrich¹  Pollock, Jennifer S.¹  Schmidt, Harald H.H.W.²  Nakane, Masaki¹  Murad, Ferid¹ 

[1]Vascular Biology, Abbott Laboratories, Abbott Park, Illinois 60064, USA

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

关键词: Brain;    Molecular cloning;    Human;    Nitric oxide synthase;    Skeletal muscle;    BH4;    5;    6;    7;    8-tetrahydrobiopterin;    CaM;    calmodulin;    cDNA;    complimentary DNA;    EGTA;    [ethylenebis (oxyethylenenitrilo)]tetraacetic acid;    HEPES;    4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid;    NMA;    N G-methyl-l-arginine;    NNA;    N G-nitio-l-arginine;    NO;    nitric oxide;    PCR;    polymerase chain reaction;    PMSF;    phenylmethylsulfonyl fluoride;    SDS;    sodium dodecyl sulfate;    TFP;    trifluoperazine;   

DOI  :  10.1016/0014-5793(93)81210-Q

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown