Thioredoxin reduces complement factor H and alters its complement regulatory function

Complement factor H (CFH) is an enzyme responsible for inactivating components of the complement cascade, thus limiting the downstream effector mechanisms which would otherwise occur were the process to continue unregulated. In view of the close structural and functional homology between β2GPI and CFH we sought in this study to determine whether CFH is a substrate for oxidoreductases, and whether distinct redox forms can be found in the plasma or serum of individuals and if so to determine the functional implications of such redox transformations to CFH complement regulatory function. This dataset relates to the detection of reduced disulfide bonds in CFH by TRX-1/TRX-R/NADPH.