Cytochrome b-558 α-subunit cloning and expression in rat aortic smooth muscle cells
T Fukui, B Lassègue, H Kai, RW Alexander… - … et Biophysica Acta (BBA …, 1995 - Elsevier
T Fukui, B Lassègue, H Kai, RW Alexander, KK Griendling
Biochimica et Biophysica Acta (BBA)-Bioenergetics, 1995•ElsevierRecent studies have shown that the NADPH oxidase participates in the generation of
superoxide anion in non-phagocytic cells. Here we report the isolation and nucleotide
sequence of a cDNA for the cytochrome b-558 α-subunit of the NADPH oxidase in rat
vascular smooth muscle cells (VSMCs). The coding region of the cDNA was 93%
homologous to mouse and 81% to human in nucleotide sequence and 96% homologous to
mouse and 89% to human in the deduced amino acid sequence. Our results provide a tool …
superoxide anion in non-phagocytic cells. Here we report the isolation and nucleotide
sequence of a cDNA for the cytochrome b-558 α-subunit of the NADPH oxidase in rat
vascular smooth muscle cells (VSMCs). The coding region of the cDNA was 93%
homologous to mouse and 81% to human in nucleotide sequence and 96% homologous to
mouse and 89% to human in the deduced amino acid sequence. Our results provide a tool …
Recent studies have shown that the NADPH oxidase participates in the generation of superoxide anion in non-phagocytic cells. Here we report the isolation and nucleotide sequence of a cDNA for the cytochrome b-558 α-subunit of the NADPH oxidase in rat vascular smooth muscle cells (VSMCs). The coding region of the cDNA was 93% homologous to mouse and 81% to human in nucleotide sequence and 96% homologous to mouse and 89% to human in the deduced amino acid sequence. Our results provide a tool with which to explore the mechanism of superoxide anion generation in rat VSMCs and other non-phagocytic cells.
Elsevier