Ivanisevic Malcic A.,University of Zagreb |
Breen L.,Proteomics Core |
Josic D.,Proteomics Core |
Josic D.,Brown University |
And 8 more authors.
Journal of Oral Pathology and Medicine | Year: 2015
Background: Keratocystic odontogenic tumour (KCOT) is a benign, yet aggressive odontogenic tumour. Herein, proteome analysis of KCOT lesions in comparison with control patient-matched tissue unaffected by the disease and with inflammatory odontogenic cysts, namely radicular cysts is presented. Methods: For the proteomics profiling, two complementary proteomics techniques MALDI-MS/MS and LC-ESI-MS/MS were employed. Potential candidate biomarkers were validated by immunohistochemistry. Results: More than 43 proteins were found to be differentially expressed or up-regulated in KCOT lesions in comparison with patient-matched unaffected oral mucosa. These proteins bear important biological functions and are involved in cell proliferation, cytoskeletal re-organization, transcription, cellular motility and apoptosis. In particular, a number of differentially expressed proteins participate in autocrine regulation and signalization within JNK and p38 MAPK signalling pathways. Conclusions: Immunohistochemical validation of chosen putative biomarkers revealed axin interaction partner and dorsalization-antagonist (AIDA), known as a protein that blocks activation of JNK signalling pathway, as a differential biomarker for KCOT lesions on an independent cohort of KCOT tissue samples in comparison with most prevalent intra-oseal lesions inflammatory odontogenic cysts. © 2014 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd.
Srajer Gajdosik M.,Josip Juraj Strossmayer University of Osijek |
Gaso-Sokac D.,Josip Juraj Strossmayer University of Osijek |
Pavlovic H.,Josip Juraj Strossmayer University of Osijek |
Clifton J.,Brown University |
And 6 more authors.
Food Research International | Year: 2013
The antimicrobial activity of quaternary ammonium salts of pyridinium oxime against four food pathogenic bacteria, the Gram positive Bacillus subtilis and Listeria monocytogenes, as well as the Gram negative Escherichia coli and Yersinia enterocolitica, were evaluated. Changes of proteome in these bacteria grown under stress conditions were identified. By the application of a new method for sample preparation, followed by both in-gel and in-solution digestion and LC-MS/MS, both characterization and comparison of proteomes of these food pathogens were achieved. It was shown in all investigated bacteria that some of the proteins of key importance for protein turnover and bacterial metabolism are down regulated. Some stress proteins involved in protein folding and degradation were up regulated. Most of both up- and down-regulated proteins belong to the group of proteins with high abundance. Flagellin is the only protein of lower abundance that was found to be down regulated in two strains, B. subtilis and E. coli. The presented results give the better view into the proteome of food pathogens, and pave the way for further investigation of their virulence, pathogenicity and detection of biomarkers for tracing the ways and sources of food contamination. © 2012 Elsevier Ltd.