Effect of lysyl hydroxylase inhibitor, minoxidil, on ultrastructure and behavior of cultured rabbit subconjunctival fibroblasts

Graefes Arch Clin Exp Ophthalmol. 1995 Jun;233(6):347-53. doi: 10.1007/BF00200483.


Background: Minoxidil is an inhibitor of lysyl hydroxylase, an enzyme involved in collagen production, and decreases collagen production in vitro. We investigated the in vitro effects of minoxidil on behavior such as proliferation and migration of rabbit subconjunctival fibroblasts (SCFs). The ultrastructural effect of the drug on SCFs was also examined.

Methods: Proliferation of SCFs and closure of the defect produced in monolayer cultures in the presence or absence of minoxidil was studied. The ultrastructure of SCFs treated with minoxidil was also examined.

Results: Minoxidil inhibited SCF proliferation and the closure of the defect produced in monolayer cell sheets. Ultrastructural observations revealed extensive areas of irregularly dilated endoplasmic reticulum in cells treated with minoxidil, indicating the accumulation of protein, probably underhydroxylated collagen precursors, in the cisternae of endoplasmic reticulum.

Conclusions: The results indicated that minoxidil attenuated cellular activities of SCFs such as proliferation and migration in vitro. The exact mechanism of the inhibitory effects of minoxidil on these cellular activities is unknown. The findings suggest that the drug might help to prevent bleb scarring after glaucoma filtering surgery.

MeSH terms

  • Animals
  • Cell Division / drug effects
  • Cell Movement / drug effects
  • Cells, Cultured
  • Conjunctiva / cytology
  • Conjunctiva / drug effects*
  • Conjunctiva / ultrastructure
  • Enzyme Inhibitors
  • Female
  • Fibroblasts / drug effects
  • Fibroblasts / ultrastructure
  • Male
  • Microscopy, Electron
  • Minoxidil / pharmacology*
  • Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase / antagonists & inhibitors*
  • Rabbits
  • Wound Healing / drug effects


  • Enzyme Inhibitors
  • Minoxidil
  • Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase