Citrullination of adenosine deaminase impairs its binding to dipeptidyl peptidase IV.

The presence of citrullinated adenosine deaminase (ADA) was reported in the synovial fluids of rheumatoid arthritis individuals. This work reports the effects of ADA citrullination on the formation/stabilization of ADA complex with dipeptidyl peptidase IV (DPPIV). The electrophoretic mobility of in vivo citrullinated ADA was diminished compared to the native one.

Adenosine deaminase - A target for new piperazine derivatives.

The level of adenosine deaminase (ADA) activity increases in pathological effusions. Therefore, the concentration of its substrate, anti-inflammatory adenosine, decreases, thereby aggravating inflammation. Hence, the quest for ADA inhibiting compounds is an actual problem in medicine and pharmacology.