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Master of Pharmaceutical Chemistry, Zagros Institute of Higher Education, Kermanshah, Iran. , modafe.1400mmmm@gmail.com
Abstract:   (165 Views)
Hepatitis B virus (HBV)-related HCC (hepatocellular carcinoma) is one of the most important malignancies with high mortality worldwide. HCC accounts for the vast majority of liver cancers (approximately 90%). Hepatitis B virus X (HBx) protein is an important etiological agent of HBV-related HCC. Most of the available evidence shows the relationship between the presence of HBx and the development of HCC. About 1 million people die annually due to cirrhosis and HCC secondary to HBV infection. Hepatitis B vaccination of newborns took place in Iran since 1372, and before that the prevalence of hepatitis B in Iran was 2-5%. And after vaccination, this number has been reduced to 2%. In 2017, 1,400,000 people in the country were infected with hepatitis B. In Iran, 80% of liver cancer cases have a history of hepatitis B. Less than 1/3 of patients diagnosed with HCC are treated with existing methods. Therefore, the diagnosis of HCC in the early stages is vital for the patient's survival and the identification of biomarkers for the early diagnosis of HCC is a necessity. For this purpose, in this research, common proteins effective in HCC and proteins that interact with hepatitis B virus X protein were identified using articles and databases, and the protein-protein interaction (PPI) network between them was determined using Cytoscape 3.7.1 software. was drawn Then, using the Centiscape plugin, the hub proteins in this network were identified. TP53, HSP90AB1, HSPB1, PIN1, HIF1A and HSPA4 are the important proteins of the network. 4 biological pathways of these hub proteins were determined using Funrich 3.1.3 software. 100% of these proteins were involved in VEGF and VEGFR signaling network and 80% of proteins were involved in ErbB receptor signaling network, Insulin Pathway, Class I PI3K signaling events. Considering the role of hepatitis B virus X protein in the progression of HCC disease, primer design was done for the X gene and the desired fragment was obtained through PCR. In the next step, the attachment of the desired fragment to the pET-M33 expression plasmid was confirmed by using PCR colony to connect the desired fragment to the plasmid. The protein fragment was heterologously expressed in E. coli BL21(DE3) and the presence of the target protein was confirmed by SDS-PAGE. After confirming the expression of the protein, its purification by Ni2 column + - NTA done
 
     
Type of Study: Research | Subject: Pharmacy

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