Induction of Matrix Metalloproteinases 2 and 9 following Stress to the Lens

• Published in: Experimental eye research 2000-12, Vol.71 (6), p.591-597
• Main Authors: Tamiya, Shigeo, Wormstone, I.Michael, Marcantonio, Julia M, Gavrilovic, Jelena, Duncan, George
• Format: Article
• Language: English
• Subjects: Animals; Biological and medical sciences; Cataract - enzymology; cataractogenesis; Culture Media - analysis; Electrophoresis, Polyacrylamide Gel; Eye and associated structures. Visual pathways and centers. Vision; Fundamental and applied biological sciences. Psychology; gelatin zymography; Lens, Crystalline - enzymology; matrix metalloproteinase; Matrix Metalloproteinase 2 - physiology; Matrix Metalloproteinase 9 - physiology; Molecular Weight; Organ Culture Techniques; posterior capsule opacification; Swine; Vertebrates: nervous system and sense organs; wound healing
• ISSN: 0014-4835; 1096-0007
• DOI: 10.1006/exer.2000.0916

Matrix metalloproteinase 2 and 9 (MMP-2 and 9, also known as gelatinase A and B) have been implicated in a number of eye diseases, but 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 removed from the eye and cultured in either Eagles Minimum Essential Medium (EMEM) or EMEM supplemented with 1m M hydrogen peroxide. The medium was sampled and changed every 2 days. On some occasions a sham cataract operation was 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 display any detectable gelatinolytic activity. However, media from cataractous lenses demonstrated a gelatinolytic band, which had similar molecular weights 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 samples obtained from capsular bag preparations within 24hr. The data presented indicate that normal lenses have undetectable gelatinase activity. However, there is an associated expression of gelatinases with pathological states of the lens, and therefore gelatinase expression could play an important role in cataractogenesis and posterior capsule opacification.