Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.jtos.2013.10.001
Title: S100A proteins as molecular targets in the ocular surface inflammatory diseases
Authors: Tong, L. 
Lan, W.
Lim, R.R.
Chaurasia, S.S.
Keywords: Corneal angiogenesis
Dry eye
Meibomian gland disease
Meibomian gland dysfunction
Ocular surface
Pterygium
S100A proteins
Issue Date: Jan-2014
Citation: Tong, L., Lan, W., Lim, R.R., Chaurasia, S.S. (2014-01). S100A proteins as molecular targets in the ocular surface inflammatory diseases. Ocular Surface 12 (1) : 23-31. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jtos.2013.10.001
Abstract: The S100 proteins are calcium-binding proteins that are exclusively expressed in vertebrates, where they interact with enzymes, cytoskeletal proteins, receptors, transcription factors, and nucleic acids to regulate proliferation, differentiation, apoptosis, inflammation, cell migration, energy metabolism, and Ca2 homeostasis. In this review, we focus on the S100A8 and S100A9 members of the family that are involved in the regulation of neutrophil chemotaxis and inflammation related to ocular surface diseases such as dry eye, meibomian gland dysfunction, pterygium, and corneal neovascularization. In our previous studies, we have found that the levels of S100A8 and S100A9 were elevated in these inflammatory ocular diseases. For instance, S100A8 and A9 were found to be upregulated in pterygium tissues at both transcript and protein levels. These findings are consistent with the role of S100A8 and S100A9 proteins in activating the innate immune system in the eye via Toll-like receptors (TLRs) and altering the immune tolerance of the eye-associated lymphoid system. Recently, use of S100A8-targeting antibody has shown promising results in targeting corneal neovascularization. Injection of S100A8 has been shown to inhibit eosinophilic infiltration and thus may have potential therapeutic implications in allergic diseases. © 2014 Elsevier Inc. All rights reserved.
Source Title: Ocular Surface
URI: http://scholarbank.nus.edu.sg/handle/10635/110629
ISSN: 15420124
DOI: 10.1016/j.jtos.2013.10.001
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