Immunohistochemical Detection of Latent membrane Protein 1 and Human Twist Protein in Patients with Thyroid Cancer

Epstein Barr virus is tumour virus that expresses cancer genes and immortalizes infected lymphocytes. This study is designed to determine the presence of the LMP-1 and human Twist protein and study the association between them in a patient with thyroid cancer and benign lesion. The retrospective study consists of 40 formalin-fixed, paraffin-embedded thyroid tissue blocks were obtained, from 20 patients with thyroid papillary carcinoma and 20 patients with thyroid follicular carcinoma, and compared with 10 tissues from follicular hyperplasia without atypia were collected from Teaching Laboratories in Medical city, Baghdad, during the period from July 2019 till February 2020. Tissue blocks were used for the detection of LMP1 and human twist protein by immunohistochemistry technique. The results of LMP-1 was (45%, 40% and 30%) respectively and high proportion was noticed in females than males, (77.78%), (78%), (100%) respectively, and the results reveal high percentage 66.67% in age (20-40 years). Human twist protein shows that the most favourable cases 9 (45%), 8 (40%), in patients with PTC and FTC while no instances in the control group. In conclusion, LMP1 and human Twist protein may have an essential role in the progression of thyroid cancer.

TFF3 modulates NF-κB and a novel negative regulatory molecule of NF-κB in intestinal epithelial cells via a mechanism distinct from TNF-α

Trefoil factor 3 (intestinal trefoil factor) is a cytoprotective factor in the gut. Herein we compared the effect of trefoil factor 3 with tumor necrosis factor-α on 1) activation of NF-κB in intestinal epithelial cells; 2) expression of Twist protein (a molecule essential for downregulation of nuclear factor-κB activity in vivo); and 3) production of interleukin-8. We showed that Twist protein is constitutively expressed in intestinal epithelial cells. Tumor necrosis factor-α induced persistent degradation of Twist protein in intestinal epithelial cells via a signaling pathway linked to proteasome, which was associated with prolonged activation of NF-κB. In contrast to tumor necrosis factor, trefoil factor 3 triggered transient activation of NF-κB and prolonged upregulation of Twist protein in intestinal epithelial cells via an ERK kinase-mediated pathway. Unlike tumor necrosis factor-α, transient activation of NF-κB by trefoil factor 3 is not associated with induction of IL-8 in cells. To examine the role of Twist protein in intestinal epithelial cells, we silenced the Twist expression by siRNA. Our data showed that trefoil factor 3 induced interleukin-8 production after silencing Twist in intestinal epithelial cells. Together, these observations indicated that 1) trefoil factor 3 triggers a diverse signal from tumor necrosis factor-α on the activation of NF-κB and its associated molecules in intestinal epithelial cells; and 2) trefoil factor 3-induced Twist protein plays an important role in the modulation of inflammatory cytokine production in intestinal epithelial cells.