Measurement of activities in two different angiotensin II generating systems, chymase and angiotensin-converting enzyme, in the vitreous fluid of vitreoretinal diseases: a possible involvement of chymase in the pathogenesis of macular hole patients

Curr Eye Res. 2004 Oct-Nov;29(4-5):321-5. doi: 10.1080/02713680490516161.

Abstract

Purpose: To investigate possible involvement of chymase and angiotensin-converting enzyme (ACE) in the pathogenesis of vitreoretinal diseases, both of which are related to the production of angiotensin II.

Methods: We measured chymase and ACE activities in the vitreous in the 54 affected eyes of 54 patients who had undergone vitreous surgery for idiopathic macular holes (MH, n = 14), proliferative diabetic retinopathy (PDR, n = 14), idiopathic epiretinal membranes (ERM, n = 13), and rhegmatogenous retinal detachment (RRD, n = 13).

Results: Chymase activities in the vitreous from patients with MH, PDR, ERM, and RRD were 1.87 +/- 0.53, 0.06 +/- 0.04, 0.40 +/- 0.12, and 0.08 +/- 0.03 (mean +/- SE) mU/mg protein, respectively, and ACE activities in the vitreous humor were 0.18 +/- 0.09, 0.30 +/- 0.07, 0.01 +/- 0.01, and 0.03 +/- 0.02 (mean +/- SE) mU/mg protein, respectively. Chymase activity was significantly elevated in MH among these diseases (p < 0.01, Scheffe), and ACE was significantly activated in PDR compared to ERM and RRD (p < 0.05, Scheffe).

Conclusions: Our results suggest that two different angiotensin II generating systems are activated in human vitreous humor; an increased activity of chymase may play a possible role in the formation of macular holes.

MeSH terms

  • Aged
  • Angiotensin II / metabolism*
  • Chymases
  • Diabetic Retinopathy / enzymology
  • Enzyme Activation
  • Epiretinal Membrane / enzymology
  • Female
  • Humans
  • Male
  • Middle Aged
  • Peptidyl-Dipeptidase A / metabolism*
  • Retinal Detachment / enzymology
  • Retinal Perforations / enzymology*
  • Retinal Perforations / etiology
  • Serine Endopeptidases / metabolism*
  • Vitrectomy
  • Vitreous Body / enzymology*

Substances

  • Angiotensin II
  • Peptidyl-Dipeptidase A
  • Serine Endopeptidases
  • Chymases