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Hejazi, Seyed Hesam,Ahangari, Ghasem,Pornour, Majid,Deezagi, Abdolkhaleagh,Aminzadeh, Saeed,Ahmadkhaniha, Hamid Reza,Akbari, Mohamad Esmail Asian Pacific Journal of Cancer Prevention 2014 Asian Pacific journal of cancer prevention Vol.15 No.11
Breast cancer is a serious and potentially lethal multi-factor disease among 40-50 aged women in both developed and developing countries. Also, various studies have pointed to roles of neurotransmitters like serotonin in development of cancers, through action on various types of receptors. This study was conducted to evaluate serotonin receptor (5HT2AR and 5HT3AR) genes expression in peripheral blood mononuclear cells (PBMCs) of breast cancer patients in comparison with the healthy people and in the MCF7 cell line. Peripheral blood samples were obtained from 30 patients and 30 healthy individuals. Total RNA was extracted from PBMCs and MCF-7 cells. and 5HT2AR and 5HT3AR were detected by RT-PCR techniques. Finally, serotonin receptor gene expression variation in breast cancer patients and MCF-7 cells were determined by real time-PCR. This latter indicated significant promotion in expression of 5HT3AR and 5HT2AR in PBMCs in breast cancer patients but expression of 5HT2AR in the MCF-7 cell line was significantly decreased. In conclusion, after performing complimentary tests, determine of gene expression changes in serotonin receptors (5HT2AR and 5HT3AR) may be useful as a new approach in treatment of breast cancer based on use of antagonists.
Reyhane Zamani,Sayyed Shahryar Rahpeyma,Moein Aliakbari,Mousa Naderi,Mohsen Yazdanei,Saeed Aminzadeh,Jafar Khezri,Kamahldin Haghbeen,Ali Asghar Karkhane 한국생물공학회 2023 Biotechnology and Bioprocess Engineering Vol.28 No.4
Improving the thermal stability of enzymes is an essential factor in the industrial applications of enzymes. Many methods related to increased thermal stability were explained, and increasing salt bridges is one of the strategies for improving the thermal stability of enzymes. In this study, mutations T59E, I145R, N149R, V219D, and A262R are introduced into the native cellulase gene to produce the mutant 5M-cel5E cellulase. In silico results showed that the mutation increased the salt bridges from 15 to 28. Root mean square fluctuation (RMSF) calculations confirmed that the mutation increased protein stability. Furthermore, the docking results showed that the affinity of cellobiose for the 5M-cel5E active site (-122.759) was slightly decreased compared to native cellulase (-130.93). No enzymatic activity was found in 5M-cel5E cellulase after cloning, expression and purification. Activated the enzyme with a back mutation of R149N, the result of which was named 4M-cel5E. The last mutation increases the salt bridges from 15 to 22, creating 4 salt bridge networks. The 4M-cel5E enzyme exhibited a maximum activity of 463 U/mg at pH 6.0 and 45°C. The mutations also increased the enzyme thermal stability up to 1.5 and 3.4-fold at temperatures of 65 and 67oC, respectively. These mutations made the Clostridium thermocellum cellulase suitable for various industries such the biofuel and paper.