Jorge Justino has his expertise in the biological evaluation and toxicity studies of natural and synthetic compounds and food chemistry. Full Professor of Escola Superior Agrária de Santarém, MSc. and Ph.D in Chemical Engineering at Instituto Superior Técnico – Universidade Técnica de Lisboa, Habilitation in Food Chemistry at Universidade de Trás-Os-Montes e Alto Douro. He is President of Instituto Politécnico de Santarém and former Director of Escola Superior Agrária de Santarém, He was a member of the networks Euroglycoforum and Prion Chemical Biology Network and is the representative member of the Instituto Politécnico de Santarém at the European Innovation Partnership A3 Group FCUL consortium.
The emergence of antibiotic resistance encouraged chemists to explore new structures as new antibiotics with new modes of action. Dodecyl deoxy glycoside structures have shown a potent activity against Bacillus spp, in particular B. cereus.1-3 A small library of related glycosides, differing in saccharide configuration and deoxygenation pattern, as well as aglycone structure have been synthesized for the recognition of the structural features that determine the selectivity for Bacillus cereus. Their preparation was accomplished by reaction of glycals with alcohols, catalyzed by triphenylphosphane hydrobromide.4 Depending on their structural features, some of these compounds demonstrated a potent activity against B. cereus. In addition, they showed low/very low toxicity and are not genotoxic. This work clearly demonstrates the uniqueness of carbohydrates which stereochemistry and chemical structure can tune the bioactivity exhibited by stereoisomers.
Eduardo Osinaga is Medical Doctor and completed his PhD at the Technological University of Compiègne, France. He is the director of the Laboratory of Glycobiology and Tumor Immunology at Pasteur Institut, Montevideo, and is the Head of the Department of Immunobiology, Faculty of Medicine, Montevideo, Uruguay. His major research interests is the glyco-immunology of cancer. He has published more than 75 papers in reputed journals.
Lung cancer is currently the leading cause of cancer-related death worldwide, accounting for approximately a third of all cancer diagnoses and related-deaths. Non–small cell lung cancer (NSCLC) represents nearly 80% of lung tumors; the two most common NSCLC histological types are squamous cell carcinoma (SCC) and adenocarcinoma (ADCA). Several diagnosis procedures detecting altered glycosylation have been developed and incorporated as assistant procedures in clinical oncology. The synthesis of mucin-type O-glycans is started in a reaction catalyzed by UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts). This is a complex family of enzymes of at least 20 members in humans. We previously found that GALNT13, the gene encoding GalNAc-T13 isoenzyme, is a strong predictor of poor clinical outcome in neuroblastoma patients (Berois et al., Clin Chem. 2006; 52:1701-12). In the present study, we evaluated GalNAc-T13 expression in human NSCLC. We produced a monoclonal antibody (MAb T13.5) that was used to assess the expression profile of the GalNAc-T13 protein in a well-defined population of 443 surgically resected NSCLC patients with 7 years of follow-up. We found that ADCAs expressed higher levels of the enzyme than SCCs. GalNAc-T13 expression correlated significantly with worse overall survival in ADCA patients treated with neoadjuvant chemotherapy. These data suggest that GalNAc-T13 could be a novel marker associated to chemoresistance in lung adenocarcinomas.