Cruzat, AndreaGonzalez-Andrades, MiguelMauris, JérômeAbusamra, DinaChidambaram, PreethiKenyon, Kenneth R.Chodosh, JamesDohlman, ClaesArgueso, Pablo2018-02-262018Cruzat, Andrea, Miguel Gonzalez-Andrades, Jérôme Mauris, Dina B. AbuSamra, Preethi Chidambaram, Kenneth R. Kenyon, James Chodosh, Claes H. Dohlman, and Pablo Argüeso. 2018. “Colocalization of Galectin-3 With CD147 Is Associated With Increased Gelatinolytic Activity in Ulcerating Human Corneas.” Investigative Ophthalmology & Visual Science 59 (1): 223-230. doi:10.1167/iovs.17-23196. http://dx.doi.org/10.1167/iovs.17-23196.http://nrs.harvard.edu/urn-3:HUL.InstRepos:34868881Purpose Galectin-3 is a carbohydrate-binding protein known to promote expression of matrix metalloproteinases, a hallmark of ulceration, through interaction with the extracellular matrix metalloproteinase inducer CD147. The aim of this study was to investigate the distribution of galectin-3 in corneas of patients with ulcerative keratitis and to determine its relationship to CD147 and the presence of gelatinolytic activity. Methods: This was an observational case series involving donor tissue from 13 patients with active corneal ulceration and 6 control corneas. Fixed-frozen sections of the corneas were processed to localize galectin-3 and CD147 by immunofluorescence microscopy. Gelatinolytic activity was detected by in situ zymography. Results: Tissue from patients with active corneal ulceration showed a greater galectin-3 immunoreactivity in basal epithelia and stroma compared with controls. Immunofluorescence grading scores revealed increased colocalization of galectin-3 and CD147 in corneal ulcers at the epithelial–stromal junction and within fibroblasts. Quantitative analysis using the Manders' colocalization coefficient demonstrated significant overlap in corneas from patients with ulcerative keratitis (M1 = 0.29; M2 = 0.22) as opposed to control corneas (M1 = 0.01, P < 0.01; M2 = 0.02, P < 0.05). In these experiments, there was a significant positive correlation between the degree of galectin-3 and CD147 colocalization and the presence of gelatinolytic activity. Conclusions: Our results indicate that concomitant stimulation and colocalization of galectin-3 with CD147 are associated with increased gelatinolytic activity in the actively ulcerating human cornea and suggest a mechanism by which galectin-3 may contribute to the degradation of extracellular matrix proteins during ulceration.en-USCD147corneal ulcerationepithelial–stromal junctiongalectin-3matrix metalloproteinaseJournal Article2018-02-2610.1167/iovs.17-23196