IOVS
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1167/iovs.08-2185 on September 20, 2008
 (Investigative Ophthalmology and Visual Science. 2009;50:814-819.)
© 2009 by The Association for Research in Vision and Ophthalmology, Inc.
doi:10.1167/iovs.08-2185
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
iovs.08-2185v1
50/2/814    most recent
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Web of Science (1)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by de Smet, M. D.
Right arrow Articles by Willekens, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by de Smet, M. D.
Right arrow Articles by Willekens, B.

Microplasmin: Ex Vivo Characterization of Its Activity in Porcine Vitreous

Marc D. de Smet,1,2 Christophe Valmaggia,1,3 Javier Zarranz-Ventura,4 and Ben Willekens5

1From the Department of Ophthalmology, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands; 2Division of Vitreo-retinal Surgery and Uveitis, Department of Ophthalmology, Middelheim Hospital, Antwerp, Belgium; 3Department of Ophthalmology, Kantonsspital St. Gallen, St. Gallen, Switzerland; 4Faculty of Medicine, University of Navarra, Pamplona, Spain; and 5Department of Morphology, Netherlands Institute for Neurosciences, Amsterdam, The Netherlands.

PURPOSE. Microplasmin is a recombinant protein limited to the enzymatic moiety of plasmin without any of its cringle domains. Its enzymatic activity is similar to that of plasmin enzyme. The present study characterizes in a porcine eye model the vitreolytic ability of microplasmin.

METHOD. Freshly harvested porcine eyes were used in these trials. Eyes were injected with escalating doses of microplasmin (62.5, 125, 250, 400 µg) for 1 hour or with 125 µg microplasmin with increasing time exposures (15, 30, 60, 120 minutes). Eyes were fixed by a very slow dehydration process to preserve the integrity of the vitreous retinal interface. They were examined by light microscopy to determine the degree of posterior vitreous detachment and by scanning electron microscopy (SEM) to study structural changes.

RESULTS. Effective separation of the posterior hyaloid appeared to be dose dependent. After 1 hour, the posterior pole was detached in 100% of porcine eyes exposed to 125 µg microplasmin and in the midperiphery to 250 µg microplasmin. Vitreous at the ora did not detach. At 120 minutes of exposure, midperipheral detachment was observed with 125 µg microplasmin. A smooth retinal surface was seen where the enzyme caused posterior vitreous detachment. There was also significant change to the integrity of the vitreous without any obvious structural alterations to the retina by histology or scanning electron microscopy.

CONCLUSIONS. Microplasmin caused vitreolysis and posterior vitreous separation in an ex vivo porcine eye model in an apparent dose- and time-dependent fashion. In this model system, the minimal effective dose appeared to be 125 µg.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2009 by the Association for Research in Vision and Ophthalmology