sahar sadat sedighzadeh

Cannabinoid receptor 1 (CB1R) that located throughout the central, peripheral, and enteric nervous system can be found all over the gastrointestinal tract. Cannabinoid receptors (CBRs) play important roles in pathophysiological processes and have been identified as a therapeutic target for developing novel anticancer agents.

The purposes of this study were to evaluate the CB1R expression in human gastric cancer, mRNA and protein expression of CB1R under lipopolysaccharide (LPS)-mediated inflammation condition in human gastric cancer cells (AGS), and the effects of inflammation on cell proliferation in LPS-stimulated AGS cells.

CB1R mRNA expression in human gastric cancer samples and AGS cells were assessed by quantitative real-time polymerase chain reaction (qRT-PCR). The expression level of CB1R, after inflammation induction using LPS, was evaluated by qRT-PCR and western blot techniques. Cell proliferation was evaluated using 5-bromo-2-deoxyuridine (BrdU) labeling assay.

CB1R mRNA was significantly higher in human gastric cancer samples compared to adjacent normal tissues. LPS induced CB1R mRNA and protein expression in stimulated cells and promoted the proliferation of AGS cells.

Our results show the increased expression of CB1R in gastric cancer samples and reveal that LPS induction increases the expression of CB1R and promotes cell proliferation in AGS cells. Accordingly, CB1R may be suggested as a potential molecular target for diagnostic and therapeutic aims in patients with gastric cancer

Infectious bursal disease virus (IBDV) is the causative agent of Gumboro disease, an infectious disease of global economic importance in poultry. Structural protein VP2 of IBDV is the most frequently studied protein due to its significant roles in virus attachment, protective immunity, and serotype specificity. The objective of the present study was to improve the expression of hypervariable region of VP2 protein (hvVP2) in Escherichia coli (E.coli). The results showed that the hvVP2 was expressed in very low amount in E.coli. But, codon optimized hvVP2 protein showed significantly enhanced protein expression level. The coding sequence of hvVP2 was amplified and then identified by polymerase chain reaction (PCR) and sequencing. To achieve high-level expression of hvVP2 protein, we optimized hvVP2 gene base on E. coli preferred codons and synthesized the optimized gene. The synthetical gene was cloned into expression vector pET-26b and expressed in E. coli BL21 (DE3). After induction with Isopropyl-D-1-Thiogalactopyranoside (IPTG) and optimization the conditions of expression, the hvVP2 protein was relatively increased and identified by SDS-PAGE and Western blotting. Productive conformation can now be used for structure-based design purposes as well as structure-function relation of VP1 protein. It is suggested that the codon optimized hvVP2-His protein may be a useful option (but it is not enough) for developing diagnostic tests and immunization proposes.