Matrix metalloproteinase 2 and 9 (MMP-2 and 9, also known as gelatinase A a
nd B) have been implicated in a number of eye diseases, bur their possible
involvement in lens pathology is yet to be determined. In the present study
, we therefore investigated a possible role of matrix metalloproteinases in
cataract and posterior capsule opacification, Whole porcine lenses were re
moved from the eye and cultured in either Eagles Minimum Essential Medium (
EMEM) or EMEM supplemented with 1 mM hydrogen peroxide, The medium was samp
led and changed every 2 days. On some occasions a sham cataract operation w
as performed on cultured lenses. The resulting capsular bag was secured to
a Petri dish and cultured in EMEM. Culture media from all preparations were
analysed for MMP-2 and 9 activity by gelatin zymography Media samples from
lenses which maintained clarity over the 6 day culture period did not disp
lay any detectable gelatinolytic activity. However, media from cataractous
lenses demonstrated a gelatinolytic band, which had similar molecular weigh
ts to the pro-form of MMP-2. In addition to this band, bands with a similar
molecular weight to pro-MMP-9 and its dimeric form were also detected in s
amples obtained from capsular bag preparations within 24 hr. The data prese
nted indicate that normal lenses have undetectable gelatinase activity. How
ever, there is an associated expression of gelatinases with pathological st
ates of the lens, and therefore gelatinase expression could play an importa
nt role in cataractogenesis and posterior capsule opacification. (C) 2000 A
cademic Press.