Lysosomal enzyme levels in corneal storage media. K-Sol versus McCarey-Kaufman

• Published in: Ophthalmology (Rochester, Minn.) Vol. 95; no. 11; p. 1498
• Main Authors: Morgan, K M, Bruner, W E, Wyszynski, R E, DiMarco, M S
• Format: Journal Article
• Language: English
• Published: United States 01.11.1988
• Subjects: Chondroitin - analogs & derivatives; Chondroitin Sulfates; Cornea - enzymology; Culture Media; HEPES; Humans; Hydrolases - metabolism; Lysosomes - enzymology; Organic Chemicals; Piperazines; Tissue Preservation
• ISSN: 0161-6420
• DOI: 10.1016/S0161-6420(88)32984-2

Evidence indicates that lysosomal enzymes can carry out corneal autolysis during corneal storage and that they are damaging to the corneal endothelium. The authors investigated the release of lysosomal enzymes into two corneal storage media (K-Sol and McCarey-Kaufman [M-K]) by paired human donor corneas during 4 degrees C storage. The authors also studied the interaction of these media with lysosomal enzymes from human cornea. K-Sol and M-K stimulated (P less than 0.01) both beta-glucuronidase and alpha-galactosidase about equally. beta-N-Acetyl-glucosaminidase, a major catabolic enzyme of the cornea, was inhibited by the chondroitin sulfate in K-Sol by over 90% (P less than 0.01). Corneas stored in M-K released more lysosomal enzymes than corneas stored in K-Sol. At 4 days, the values approached significance (P less than 0.06) and by day 10 significantly higher values were found in the M-K media (P less than 0.01). Both storage methods showed a linear release. Individual corneas were found to vary in their release rates. Whether corneas that release more enzyme will show higher endothelial cell loss or produce less successful penetrating keratoplasty grafts deserves further study.