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Molecular Basis of Chemotherapy and Radiotherapy Treatments Resistance in Cancer Management Michael Sunday Abu; Ojochenemi Ejeh Yakubu; Mgbede Timothy; Isaac John Umaru
African Multidisciplinary Journal of Sciences and Artificial Intelligence Vol 1 No 1 (2024): African Multidisciplinary Journal of Sciences and Artificial Intelligence
Publisher : Darul Yasin Al Sys

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.58578/amjsai.v1i1.3739

Abstract

Cancer is a leading cause of death worldwide. Surgery is the primary treatment approach for cancer, but the survival rate is very low due to the rapid progression of the disease and presence of local and distant metastasis at diagnosis. Adjuvant chemotherapy and radiotherapy are important components of the multidisciplinary approaches for cancer treatment. However, resistance to radiotherapy and chemotherapy may result in treatment failure or even cancer recurrence. Radioresistance in cancer is often caused by the repair response to radiation-induced DNA damage, cell cycle dysregulation, cancer stem cells (CSCs) resilience, and epithelial-mesenchymal transition (EMT). Understanding the molecular alterations that lead to radioresistance may provide new diagnostic markers and therapeutic targets to improve radiotherapy efficacy. Patients who develop resistance to chemotherapy drugs cannot benefit from the cytotoxicity induced by the prescribed drug and will likely have a poor outcome with these treatments. Chemotherapy often shows a low response rate due to various drug resistance mechanisms. This review focuses on the molecular mechanisms of radioresistance and chemoresistance in cancer and discusses recent developments in therapeutic strategies targeting chemoradiotherapy resistance to improve treatment outcomes.
Production and Characterisation of Peroxidase from Aspergillus terrens Isolated from Water Sample in Wukari, Taraba State, Nigeria Mgbede Timothy; Moses Adondua Abah; Victoria Ifeoluwa Ayo; Maryam Usman Ahmed; Okpanachi Nuhu Oyibo; Nkechi Gift Ijeomah; Adetoyi Moses Gbadebo; Ajala-Lawal R. A; Aliyu Olamilekan Najeeb; Olabanji Martina Morolake; Kingsley Iyoko Iseko; Dafup Katdel Istifanus; Isaac John Umaru
African Journal of Biochemistry and Molecular Biology Research Vol 1 No 1 (2024): African Journal of Biochemistry and Molecular Biology Research
Publisher : Darul Yasin Al Sys

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.58578/ajbmbr.v1i1.3667

Abstract

The use of biocatalysts like enzymes in the development of environmentally sustainable processes has been reported as an ecofriendly approach for the current bioeconomy. This research aimed at producing and characterizing peroxidase from Aspergillus terrens isolated from water sample in Wukari, Taraba State, Nigeria. Fungi species from surface water sample obtained in Federal University Wukari, Taraba Nigeria were isolated through serial dilution of peptone water and was cultured in a room temperature in different petri dishes using Potato Dextrose Agar (PDA). A portion of the fungi growth chosen from the best growth of cultured water sample were cut and transferred into the 250 Erlenmeyer flask each containing an acceptable proportion of phosphate buffer, pH 6.0. The screening for peroxidase production was aseptically performed on a plate by inoculating the fermented medium with azur B dye. The appearance of a clear zone indicated a positive result for peroxidase activity. The incubation of the peroxidase enzyme was conducted over eleven days, with the highest enzyme yield observed on the eighth day. The results obtained in this study showed that the effect of pH on peroxidase activity was studied, revealing that the optimum pH for enzyme activity was 7.5. Peroxidase activity was lowest at pH 1. Temperature variation studies showed that the optimum temperature for peroxidase activity was 30°C. Peroxidase activity changed as substrate concentration was varied. Peroxidase activity was revealed to be highest at substrate concentration 1.9 mM. The kinetic parameters for peroxidase were investigated to be: Vmax = 10.57082; Km = 0.244186. The evidence presented in this research has shown that peroxidase can be produced in mass by using of white rot fungi from/around our surroundings and can be explored as a cheap source of peroxidase for industrial and biotechnological purposes. In conclusion, producing peroxidase from local isolates presents an eco-friendly and affordable alternative for industrial applications, contributing to environmental sustainability and public health.