The status of EGFR CA SSR1 is a potential prognostic factor for patients with oral squamous cell carcinoma
ORAL ONCOLOGY
Authors: Lin, Yan-Liang; Wang, Wen-Yi; Lin, Jin-Ching; Wong, Yong-Kie; Chien, Yi-Chih
Abstract
The EGFR is an oncogene known to be involved in the development and progression of many cancers. It has been reported that the expression of EGFR and EGFR CA simple sequence repeat 1 (CA SSR1) repeat numbers in tumors can be useful prognostic factors in several cancer types. The objective of the present study was to analyze whether the EGFR polymorphism can be a useful prognostic factor in OSCC in the Taiwanese population. OSCC tissues were collected from 47 patients by surgical excision. The genotyping of EGFR were performed with the ABI Prism 3100 Genetic Analyzer. OSCC patients had a tendency toward an allelic imbalance of CA SSR1. The results also suggested that OSCC patients who were homozygous for CA SSR1 had a poorer prognosis than those who were heterozygous (P < 0.001). Besides, patients with an allelic imbalance of CA SSR1 had significantly lower overall and disease free survival rates than those without, using the Kaplan-Meier method (P < 0.001). This suggests that the status of CA SSR1 has the potential to be a useful prognosis factor in OSCC. (C) 2011 Elsevier Ltd. All rights reserved.
Molecular Cloning, Carbohydrate Specificity and the Crystal Structure of Two Sclerotium rolfsii Lectin Variants
MOLECULES
Authors: Peppa, Vassiliki I.; Venkat, Hemalatha; Kantsadi, Anastassia L.; Inamdar, Shashikala R.; Bhat, Ganapati G.; Eligar, Sachin; Shivanand, Anupama; Chachadi, Vishwanath B.; Satisha, Gonchigar J.; Swamy, Bale M.; Skamnaki, Vassiliki T.; Zographos, Spyridon E.; Leonidas, Demetres D.
Abstract
SRL is a cell wall associated developmental-stage specific lectin secreted by Sclerotium rolfsii, a soil-born pathogenic fungus. SRL displays specificity for TF antigen (Gal13GalNAc--Ser//Thr) expressed in all cancer types and has tumour suppressing effects in vivo. Considering the immense potential of SRL in cancer research, we have generated two variant gene constructs of SRL and expressed in E. coli to refine the sugar specificity and solubility by altering the surface charge. SSR1 and SSR2 are two different recombinant variants of SRL, both of which recognize TF antigen but only SSR1 binds to Tn antigen (GalNAc-Ser/Thr). The glycan array analysis of the variants demonstrated that SSR1 recognizes TF antigen and their derivative with high affinity similar to SRL but showed highest affinity towards the sialylated Tn antigen, unlike SRL. The carbohydrate binding property of SSR2 remains unaltered compared to SRL. The crystal structures of the two variants were determined in free form and in complex with N-acetylglucosamine at 1.7 angstrom and 1.6 angstrom resolution, respectively. Structural analysis highlighted the structural basis of the fine carbohydrate specificity of the two SRL variants and results are in agreement with glycan array analysis.
COA
Publication 
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