Molecular cloning and characterization of human endothelial nitric oxide synthase.
The constitutive calcium/calmodulin-dependent nitric oxide (NO) synthase expressed in vascular endothelium shares common biochemical and pharmacologic properties with neuronal NO synthase. However, recent cloning and molecular characterization of NO synthase from bovine endothelial cells indicated the existence of a family of constitutive NO synthases. Accordingly, we undertook molecular cloning and sequence analysis of human endothelial NO synthase. Complementary DNA clones predict a protein of 1,203 amino acids sharing 94% identity with the bovine endothelial protein, but only 60% identity with the rat brain NO synthase isoform. Northern blot analysis with an endothelial-derived cDNA identified a 4.6-4.8 kb mRNA transcript in HUVEC and in situ hybridization localized transcripts to vascular endothelium but not neuronal tissue.
Marsden
P A
PA
Renal Division, St. Michael's Hospital, University of Toronto, Ont., Canada.
Schappert
K T
KT
Chen
H S
HS
Flowers
M
M
Sundell
C L
CL
Wilcox
J N
JN
Lamas
S
S
Michel
T
T
D000594:Amino Acid Oxidoreductases / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D003001:Cloning, Molecular; D004247:DNA; D004730:Endothelium, Vascular / Q000201:enzymology*; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D009474:Neurons / Q000201:enzymology; D019001:Nitric Oxide Synthase; D010215:Papio; D012333:RNA, Messenger / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid
D012333:RNA, Messenger; D004247:DNA; D019001:Nitric Oxide Synthase; D000594:Amino Acid Oxidoreductases