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Mass spectrometric characterization of circulating covalent protein adducts derived from a drug acyl glucuronide metabolite: multiple albumin adductions in diclofenac patients.
J Pharmacol Exp Ther
August 2014
Medical Research Council Centre for Drug Safety Science, Institute of Translational Medicine, (T.G.H., X.M., R.E.J., J.L.M., A.S.C., S.L.R., C.J.E., B.K.P., D.P.W.) and Department of Chemistry (A.V.S.), University of Liverpool, Liverpool, United Kingdom; Nottingham Digestive Diseases Centre, NIHR Nottingham Digestive Diseases-Biomedical Research Unit, Nottingham University Hospitals NHS Trust and University of Nottingham (G.P.A.) and Department of Rheumatology, Nottingham University Hospitals NHS Trust (I.P.), Nottingham, United Kingdom; and AstraZeneca U.K. Ltd (S.N.L.B.) and Safety Assessment, AstraZeneca U.K. Ltd (J.G.K.), Alderley Park, Macclesfield, Cheshire, United Kingdom
Covalent protein modifications by electrophilic acyl glucuronide (AG) metabolites are hypothetical causes of hypersensitivity reactions associated with certain carboxylate drugs. The complex rearrangements and reactivities of drug AG have been defined in great detail, and protein adducts of carboxylate drugs, such as diclofenac, have been found in liver and plasma of experimental animals and humans. However, in the absence of definitive molecular characterization, and specifically, identification of signature glycation conjugates retaining the glucuronyl and carboxyl residues, it cannot be assumed any of these adducts is derived uniquely or even fractionally from AG metabolites.
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