Localization and activity of lysyl oxidase within nuclei of fibrogenic cells.
Lysyl oxidase (EC 1.4.3.13) oxidizes peptidyl lysine to peptidyl aldehyde residues within collagen and elastin, thus initiating formation of the covalent cross-linkages that insolubilize these extracellular proteins. Recent findings raise the possibility that this enzyme may also function intracellularly. The present study provides evidence by immunocytochemical confocal microscopy, Western blot analysis, enzyme assays, and chemical analyses for lysyl oxidase reaction products that this enzyme is present and active within rat vascular smooth muscle cell nuclei. Confocal microscopy indicates its presence within nuclei of 3T3 fibroblasts, as well.
Li
W
W
Department of Biochemistry, Boston University School of Medicine, MA 02118, USA.
Nellaiappan
K
K
Strassmaier
T
T
Graham
L
L
Thomas
K M
KM
Kagan
H M
HM
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D002384:Catalysis; D002467:Cell Nucleus / Q000201:enzymology*; D002478:Cells, Cultured; D007150:Immunohistochemistry; D018613:Microscopy, Confocal; D008969:Molecular Sequence Data; D009131:Muscle, Smooth, Vascular / Q000201:enzymology*; D009687:Nuclear Proteins / Q000378:metabolism; D008249:Protein-Lysine 6-Oxidase / Q000378:metabolism*; D051381:Rats
D009687:Nuclear Proteins; D008249:Protein-Lysine 6-Oxidase