Elucidating Citrullination by Mass Spectrometry and Its Role in Disease Pathogenesis

This
review focuses on discussing key mechanisms in disease pathogenesis
mediated by the protein post-translational modification citrullination.
These processes are discussed in depth in the context of complex diseases
such as rheumatoid arthritis, cancer, central nervous system disorders,
and cardiovascular disease. Additionally, a critical evaluation of
challenges in laboratory detection of citrullination sites is also
outlined. In this context, the role of mass spectrometry is discussed
with a focus on contemporary techniques that offer promising options
to detect the exact site of protein citrullination. Novel methods
described in the paper have the potential to detect and quantify the
occurrence of post-translational modification sites for diagnosis
and therapeutic purposes with a high degree of specificity and sensitivity.
Furthermore, they offer a much faster performance than traditional
techniques making them ideal for large-scale experimentation.