Cytochrome b-558 alpha-subunit cloning and expression in rat aortic smooth muscle cells

Biochim Biophys Acta. 1995 Oct 10;1231(3):215-9. doi: 10.1016/0005-2728(95)00098-4.


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 alpha-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.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aorta / chemistry*
  • Aorta / cytology
  • Base Sequence
  • Cells, Cultured
  • Cloning, Molecular
  • Cytochrome b Group / chemistry
  • Cytochrome b Group / genetics*
  • DNA, Complementary
  • Humans
  • Male
  • Mice
  • Molecular Sequence Data
  • Muscle, Smooth, Vascular / chemistry*
  • Muscle, Smooth, Vascular / cytology
  • NADPH Oxidases*
  • Rats
  • Rats, Sprague-Dawley
  • Sequence Homology, Amino Acid


  • Cytochrome b Group
  • DNA, Complementary
  • cytochrome b558
  • NADPH Oxidases

Associated data

  • GENBANK/U18729