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Glycobiology Advance Access published online on September 7, 2009

Glycobiology, doi:10.1093/glycob/cwp133
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© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Analysis of Differential Expression of Glycosyltransferases in Healing Corneas by Glycogene Microarrays

Chandrassegar Saravanan1,2, Zhiyi Cao2, Steven R. Head3 and Noorjahan Panjwani1,2*

1 Program in Cell, Molecular and Developmental Biology, Sackler School of Graduate Biomedical Sciences
2 Department of Ophthalmology and The New England Eye Center, Tufts University School of Medicine, Boston, MA
3 The Scripps Research Institute, La Jolla, CA


* Corresponding Author: Noorjahan Panjwani, Ph.D., Department of Ophthalmology, Tufts University School of Medicine, 136 Harrison Avenue, Boston, MA 02111. Telephone: 617-636-6776, Fax: 617-636-0348. Email: noorjahan.panjwani{at}tufts.edu

Received on December 18, 2008; accepted on August 28, 2009

It is generally accepted that the glycans on the cell surface and extracellular matrix proteins play a pivotal role in the events that mediate re-epithelialization of wounds. Yet, the global alteration in the structure and composition of glycans, specifically occuring during corneal wound closure remains unknown. In this study, GLYCOv2 glycogene microarray technology was used for the first time to identify the differentially expressed glycosylation-related genes in healing mouse corneas. Of ~ 2000 glycogenes on the array, the expression of 11 glycosytransferase and glycosidase enzymes was upregulated and that of 19 was downregulated more than 1.5-fold in healing corneas compared with the normal, uninjured corneas. Among them, notably, glycosyltransferases, β3GalT5, T-synthase, and GnTIVb, were all found to be induced in the corneas in response to injury, whereas, GnTIII and many sialyltransferases were downregulated. Interestingly, it appears that the glycan structures on glycoproteins and glycolipids, expressed in healing corneas as a result of differential regulation of these glycosyltransferases, may serve as specific counterreceptors for galectin-3, a carbohydrate-binding protein, known to play a key role in re-epithelialization of corneal wounds. Additionally, many glycogenes including a proteoglycan, glypican-3, and cell adhesion proteins dectin-1 and -2, and mincle, and mucin 1 were identified for the first time to be differentially regulated during corneal wound healing. Results of glycogene microarray data were confirmed by qRT-PCR and lectin blot analyses. The differentially expressed glycogenes identified in the present study have not previously been investigated in the context of wound healing and represent novel factors for investigating the role of carbohydrate-mediated recognition in corneal wound healing.

Key words: cornea / galectin-3 / glycosyltransferases / microarray / wound healing


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