April 2011
Volume 52, Issue 14
Free
ARVO Annual Meeting Abstract  |   April 2011
Determination Of The Inactivation Of Ocriplasmin In The Vitreous
Author Affiliations & Notes
  • Bart Jonckx
    Research and Development, ThromboGenics NV, Heverlee, Belgium
  • Peter Stalmans
    Department of Ophthalmology, University Hospitals Leuven, Leuven, Belgium
  • Joachim Van Calster
    Department of Ophthalmology, University Hospitals Leuven, Leuven, Belgium
  • Marc Vanhove
    Research and Development, ThromboGenics NV, Heverlee, Belgium
  • Bernard Noppen
    Research and Development, ThromboGenics NV, Heverlee, Belgium
  • Frans Aerts
    Research and Development, ThromboGenics NV, Heverlee, Belgium
  • Jean Marie Stassen
    Research and Development, ThromboGenics NV, Heverlee, Belgium
  • Marc D. de Smet
    AMC, University of Amsterdam, Amsterdam, The Netherlands
    Retina and Inflammation Service, Clinique de Montchoisi, Lausanne, Switzerland
  • Footnotes
    Commercial Relationships  Bart Jonckx, ThromboGenics (E); Peter Stalmans, Bausch & Lomb (F), ThromboGenics (R); Joachim Van Calster, None; Marc Vanhove, ThromboGenics (E); Bernard Noppen, ThromboGenics (E); Frans Aerts, ThromboGenics (E); Jean Marie Stassen, ThromboGenics (E); Marc D. de Smet, ThromboGenics (F, I, C, P, R)
  • Footnotes
    Support  Study funded by ThromboGenics
Investigative Ophthalmology & Visual Science April 2011, Vol.52, 6684. doi:
  • Views
  • Share
  • Tools
    • Alerts
      ×
      This feature is available to authenticated users only.
      Sign In or Create an Account ×
    • Get Citation

      Bart Jonckx, Peter Stalmans, Joachim Van Calster, Marc Vanhove, Bernard Noppen, Frans Aerts, Jean Marie Stassen, Marc D. de Smet; Determination Of The Inactivation Of Ocriplasmin In The Vitreous. Invest. Ophthalmol. Vis. Sci. 2011;52(14):6684.

      Download citation file:


      © ARVO (1962-2015); The Authors (2016-present)

      ×
  • Supplements
Abstract

Purpose: : To determine the pharmacokinetics of ocriplasmin enzyme in ex vivo vitreous, vitreous humor or buffer.

Methods: : Residual ocriplasmin activity was determined in vitreous samples taken from porcine eyes 0, 5, 15, 30, 60, 120 and 180 minutes following intravitreal injection of ocriplasmin; and in ocriplasmin mixed with phosphate buffered saline (PBS), porcine or human vitreous humor, at specific time points (up to 24 hours) after mixing. Ocriplasmin (50, 125, 175 and 250 µg) in a citrate buffer was added to each sample, and residual enzymatic activity was determined based on the release of p-nitroaniline (pNA) from the substrate Glu-Phe-Lys-pNA, measured on a spectrophotometer at 405 nm.

Results: : Degradation in ex vivo porcine eyes closely resembles degradation in in vitro vitreous humor or buffer. Ocriplasmin degradation most closely matches a reaction of second order kinetics. A rapid decline in activity was noted during the first 5 hours of incubation at 37°C in porcine vitreous or PBS, with 35.4 ± 3.5% and 17.3 ± 2.3% of the initial concentration remaining, respectively. Subsequent inactivation occurred at a slower rate. After 72 hours, only 0.6% of the initial dose was present in human vitreous. These second order processes were characterized by rate constants of 81 ± 15 M-1.s-1, 195 ± 21 M-1.s-1 and 207 ± 15 M-1.s-1, for porcine and human vitreous humor, and PBS, respectively.

Conclusions: : Ocriplasmin undergoes rapid, concentration-dependent, auto-proteolytic degradation, as previously described for plasmin, which is most closely described by second order kinetics. Previous investigation has shown that, despite this rapid degradation, residual activity at 72 hours is sufficient for biologic activity. These data demonstrate that ocriplasmin exerts activity in the vitreous for several hours, and are consistent with previous findings for plasmin.Acknowledgements: Ashraf Gad El Kareem for technical support/training

Keywords: vitreous • retinal adhesion 
×
×

This PDF is available to Subscribers Only

Sign in or purchase a subscription to access this content. ×

You must be signed into an individual account to use this feature.

×