Rosmarinic acid, Polyphenol

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

DNA Polymerase beta often referred to as Pol β is an important enzyme in the cell's DNA repair machinery. It has a molecular mass approximately 39 kDa. This enzyme is a member of the DNA polymerase family but is distinct in its activities. Pol β primarily facilitates base excision repair a critical process for maintaining genomic stability. It is expressed widely in various tissues and plays an important role in repairing small lesions and resolving mismatches in DNA. Fyn a member of the Src family of tyrosine kinases interacts with structures in the cytoplasm and affects cellular signaling. Fyn’s activity is important in the regulation of cell signaling and behavior.

Biological function summary

This enzyme not only contributes to the general maintenance of the genome but also interacts with other components of the DNA repair machinery. Pol β is not part of a large complex but works in tandem with scaffold proteins such as XRCC1 which serve as a platform to recruit various repair factors to DNA lesions. This recruitment and subsequent action allow the cell to swiftly repair DNA preventing potential mutations. Fyn modulates intracellular signaling which has implications on cell growth differentiation and other vital cellular responses.

Pathways

Pol β plays a central role in the base excision repair pathway. This pathway is essential for correcting single-strand breaks and non-bulky lesions caused by oxidative stress alkylation and ionizing radiation. It partners with other proteins such as PARP1 in the early stages of this pathway to initiate repair. Similarly Fyn operates in the T-cell receptor signaling pathway influencing immune responses. It can interact with proteins including Lck which is involved in the cascade of signals transmitted through this pathway.

Defects in Pol β function have been associated with increased susceptibility to cancer. Inefficient or faulty repair of DNA lesions leads to mutagenesis and genome instability factors that drive tumorigenesis. Moreover mutations within its structure link it to certain types of oral cancers. Fyn on the other hand has a connection to neurodegenerative disorders such as Alzheimer's disease where it interacts with tau protein contributing to tau phosphorylation and neurofibrillary tangle formation. Together these interactions underline the significance of Pol β and Fyn in health and disease contexts.