Wd. Li et al., LOCALIZATION AND ACTIVITY OF LYSYL OXIDASE WITHIN NUCLEI OF FIBROGENIC CELLS, Proceedings of the National Academy of Sciences of the United Statesof America, 94(24), 1997, pp. 12817-12822
Lysyl oxidase (EC 1.4.3.13) oxidizes peptidyl lysine to peptidyl aldeh
yde residues within collagen and elastin, thus initiating formation of
the covalent cross-linkages that insolubilize these extracellular pro
teins. Recent findings raise the possibility that this enzyme may also
function intracellularly. The present study provides evidence by immu
nocytochemical confocal microscopy, Western blot analysis, enzyme assa
ys, and chemical analyses for lysyl oxidase reaction products that thi
s enzyme is present and active within rat vascular smooth muscle cell
nuclei. Confocal microscopy indicates its presence within nuclei of 3T
3 fibroblasts, as well.