Subject(s)
Arthritis, Psoriatic/enzymology , Arthritis, Rheumatoid/enzymology , Dipeptidyl Peptidase 4/chemistry , Dipeptidyl Peptidase 4/metabolism , Arthritis, Psoriatic/physiopathology , Arthritis, Rheumatoid/physiopathology , Dipeptidyl Peptidase 4/genetics , Humans , Leukocytes, Mononuclear/enzymology , Osteoarthritis/enzymology , Synovial Fluid/enzymologyABSTRACT
Chelerythrine, sanguinarine and an alkaloid extract from Macleaya cordata--sanguiritrin--were found to be inhibitors of aminopeptidase A and dipeptidyl peptidase IV, while fagaronine inhibited dipeptidyl peptidase IV only. At 50 microM, chelerythrine, sanguinarine and sanguiritrin inhibited aminopeptidase N by 82%, 82%, 88%, DPP IV by 38%, 62%, 57%, and fagaronine by 34%, respectively. When bovine serum albumin (500 microg/mL) was added, the inhibition of both proteases by quaternary benzo[c]phenanthridine alkaloids (QBA) (50 microM) was significantly diminished. Strong interaction of chelerythrine and sanguinarine with bovine and human serum albumin was proved by electrophoretic determination of their respective conditional binding constants.
