Immunological consequences of methamphetamine protein glycation.
The drug of abuse methamphetamine has been found to participate in the aberrant glycation of proteins. The importance of this chemical process has been shown wherein mouse albumin was readily modified with methamphetamine, and injection of this protein into mice yields a significant immune response, even in the absence of adjuvants. Competition experiments revealed that although methamphetamine binds weakly to the elicited antibodies, the primary epitope is composed of both the methamphetamine moiety and glucose-derived cross-linking region. Implications of this phenonomenon in the context of drug addiction are discussed.
Dickerson
Tobin J
TJ
Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Yamamoto
Noboru
N
Ruiz
Diana I
DI
Janda
Kim D
KD
D000697:Central Nervous System Stimulants / Q000737:chemistry / Q000276:immunology* / Q000378:metabolism* / Q000493:pharmacokinetics; D004797:Enzyme-Linked Immunosorbent Assay; D005947:Glucose / Q000737:chemistry / Q000378:metabolism; D017127:Glycation End Products, Advanced / Q000737:chemistry / Q000276:immunology* / Q000378:metabolism*; D008694:Methamphetamine / Q000737:chemistry / Q000276:immunology* / Q000378:metabolism* / Q000493:pharmacokinetics; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism
D000697:Central Nervous System Stimulants; D017127:Glycation End Products, Advanced; D012710:Serum Albumin, Bovine; D008694:Methamphetamine; D005947:Glucose