Title : Evidence for cytochrome P4501A2-mediated protein covalent binding of thiabendazole and for its passive intestinal transport: use of human and rabbit derived cells.

Pub. Date : 2000 Jul 3

PMID : 10936227






5 Functional Relationships(s)
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1 Evidence for cytochrome P4501A2-mediated protein covalent binding of thiabendazole and for its passive intestinal transport: use of human and rabbit derived cells. Thiabendazole cytochrome P450 family 1 subfamily A member 2 Homo sapiens
2 Thiabendazole (TBZ), an anthelmintic and fungicide benzimidazole, was recently demonstrated to be extensively metabolized by cytochrome P450 (CYP) 1A2 in man and rabbit, yielding 5-hydroxythiabendazole (5OH-TBZ), the major metabolite furtherly conjugated, and two minor unidentified metabolites (M1 and M2). Thiabendazole cytochrome P450 family 1 subfamily A member 2 Homo sapiens
3 Thiabendazole (TBZ), an anthelmintic and fungicide benzimidazole, was recently demonstrated to be extensively metabolized by cytochrome P450 (CYP) 1A2 in man and rabbit, yielding 5-hydroxythiabendazole (5OH-TBZ), the major metabolite furtherly conjugated, and two minor unidentified metabolites (M1 and M2). Thiabendazole cytochrome P450 family 1 subfamily A member 2 Homo sapiens
4 Thus, CYP1A2 is a major isoenzyme involved in the formation of TBZ-derived residues bound to protein. Thiabendazole cytochrome P450 family 1 subfamily A member 2 Homo sapiens
5 Nevertheless, caution is necessary in the use of TBZ concurrently with other drugs able to regulate CYP1A2, particularly in respect to liver and lung tissues, recognised as sites of covalent-binding. Thiabendazole cytochrome P450 family 1 subfamily A member 2 Homo sapiens