Therefore, in group 1 it seems that dexamethasone delayed the re-epithelialization of the epithelium, induced keratocyte apoptosis and the upregulation of extracellular materials in the corneal stroma adjacent to the epithelial defect, and increased stromal changes and corneal haze. On the contrary, in group 3 corneal haze decreased compared with controls. Conclusion The findings of the present study shows that Inhibitors,research,lifescience,medical the association of 3% concentration of NAC and 0.1% concentration of dexamethasone immediately after corneal ulceration can delay corneal wound healing, and consequently produce more corneal
haze. Thus, the use of 0.1% concentration of dexamethasone should be delayed at least until the completion of the epithelial Cabozantinib FDA defects. Further studies with larger sample size are needed to confirm the findings of this study. Inhibitors,research,lifescience,medical Acknowledgment This study was supported by a research grant (84-VE-1781-C308) from the Research Council of Shiraz University. The authors would like to thank Dr Maryam Ansari for her assistance with the statistical analysis of the findings. Conflict of Interest: None declared
The amino groups of proteins, particularly the side chain of lysine, arginine, and histidine react non-enzymatically with reducing sugars. This post-translational modification called “glycation” or “maillard reaction”, leads via reversible Schiff-base adducts to protein bound amadori Inhibitors,research,lifescience,medical products.1-3 By subsequent oxidation
and dehydration, a broad range of brown heterogeneous Inhibitors,research,lifescience,medical products, mostly fluorescent with nitrogen- and oxygen- containing heterocyclic compounds, called advanced glycation end products
(AGEs) are formed. The formation of AEGs is irreversible, and causes a resistant protein deposition to protease.4,5 The Maillard reaction was first described by L.C. Maillard a chemist, who reported the formation of brown products upon heating a solution of amino acid (AA) and sugar.6 Schematic representation of the Maillard reaction (A) and structures of AGEs (B, C and Inhibitors,research,lifescience,medical D),7 are shown in figure 1. Pathological Consequences of AGEs In vivo Glycation modifies the structural properties of proteins such as albumin and haemoglobin leading to inflammation and oxidative stress. The pathological role of AGEs in diseases such as diabetes mellitus (DM) Dacomitinib is not fully understood. In addition to change of the protein structure, the receptor mediated mechanism of AGEs is of special interest.8 Figure 1 Schematic representation of the Maillard reaction (A) and structure of advanced glycation end products AGEs (B, C and D). The pathological features of AGEs, which are not receptor mediated, can be observed in the progression of cataracts. Evidence suggests that the glycation of lens protein is one of the causes of cataract,9 and is observed in long-lived proteins such as collagen and eye crystalline.10 However, the pivotal role of AGEs and the interaction with the receptor is not fully understood.