MAFG is a small basic leucine zipper (bZIP) transcription factor that forms homodimers or heterodimers with other bZIP proteins. These dimers bind to specific DNA sequences, regulating the expression of target genes involved in oxidative stress response, detoxification, and cellular differentiation . MAFG, along with other MAF proteins, is known to interact with the antioxidant response element (ARE) in the promoter regions of genes encoding detoxifying enzymes and antioxidant proteins.
MAFG has been implicated in various diseases, including cancer and neurodegenerative disorders. Its overexpression has been observed in certain types of cancer, where it may contribute to tumor progression by promoting cell survival and proliferation . Additionally, MAFG has been linked to the regulation of genes involved in the oxidative stress response, which is a critical factor in the pathogenesis of neurodegenerative diseases such as Alzheimer’s and Parkinson’s .
Human recombinant MAFG is a synthetically produced version of the protein, often used in research to study its function and potential therapeutic applications. One notable application of human recombinant MAFG is in the reprogramming of human pancreatic duct-derived cells (HDDCs) into insulin-secreting cells. This innovative approach involves the use of synthetic modified mRNA encoding MAFG, which is transfected into HDDCs to induce their differentiation into β-like cells capable of producing insulin .
The ability to reprogram HDDCs into insulin-secreting cells using human recombinant MAFG holds significant promise for the treatment of type 1 diabetes. This approach offers a potential alternative to β-cell replacement therapy, which aims to restore β-cell mass and glucose homeostasis in diabetic patients . The use of non-integrative RNA-based reprogramming techniques ensures that the genetic modifications are transient and do not integrate into the host genome, reducing the risk of adverse effects .