Enzymatic methylation of arsenic compounds .3. The marmoset and tamarin, but not the rhesus, monkeys are deficient in methyltransferases that methylate inorganic arsenic

被引:69
作者
Zakharyan, RA
Wildfang, E
Aposhian, HV
机构
[1] UNIV ARIZONA,DEPT MOL & CELLULAR BIOL,TUCSON,AZ 85721
[2] UNIV ARIZONA,DEPT PHARMACOL & TOXICOL,CTR TOXICOL,TUCSON,AZ 85721
基金
美国国家卫生研究院;
关键词
D O I
10.1006/taap.1996.0199
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
The methylation of inorganic arsenic to monomethylarsonic acid (MMA) and dimethylarsinic acid (DMA) have been generally considered to be the major pathway for inorganic arsenic biotransformation and detoxification. Yet, when arsenate/arsenite is injected into the Callithrix jacchus (marmoset) monkey or chimpanzee, monomethylarsonic acid and dimethylarsinic acid are not found in the urine. With the development of a rapid assay for the methyltransferases of arsenic metabolism, we have investigated the methyltransferases of the marmoset monkey liver. We have found that the marmoset, a New World animal, is deficient in liver arsenite and monomethylarsonic acid methyltransferase activities. However, the rhesus monkey, an Old World animal, has ample amounts of such methyltransferase activities. The tamarin, another New World species, is also deficient in these methyltransferases. Polymorphism and deficiency of these methyltransferases may have allowed high levels of arsenite to be maintained in the blood and liver of the marmoset and tamarin. Such high levels of arsenite may have been selective for survival of the species. The rhesus liver methyltransferases for arsenite and MMA have been purified and found to have some properties different from those of the previously reported purified rabbit liver activities. The rhesus and rabbit liver arsenite and MMA methyltransferases are devoid of catechol O-methyltransferase activity. (C) 1996 Academic Press, Inc.
引用
收藏
页码:77 / 84
页数:8
相关论文
共 26 条
  • [1] NEWER DEVELOPMENTS IN ARSENIC TOXICITY
    APOSHIAN, HV
    APOSHIAN, MM
    [J]. JOURNAL OF THE AMERICAN COLLEGE OF TOXICOLOGY, 1989, 8 (07): : 1297 - 1305
  • [2] Aposhian HV., 1989, REV BIOCH TOXICOLOGY, P265
  • [3] ARSENIC BINDING-PROTEINS OF MAMMALIAN SYSTEMS .1. ISOLATION OF 3 ARSENITE-BINDING PROTEINS OF RABBIT LIVER
    BOGDAN, GM
    SAMPAYOREYES, A
    APOSHIAN, HV
    [J]. TOXICOLOGY, 1994, 93 (2-3) : 175 - 193
  • [4] Borchardt R T, 1981, Methods Enzymol, V77, P267
  • [5] BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
  • [6] ROLE OF THIOLS IN THE INVITRO METHYLATION OF INORGANIC ARSENIC BY RAT-LIVER CYTOSOL
    BUCHET, JP
    LAUWERYS, R
    [J]. BIOCHEMICAL PHARMACOLOGY, 1988, 37 (16) : 3149 - 3153
  • [7] CHRONIC ARSENIC POISONING IN THE NORTH OF MEXICO
    CEBRIAN, ME
    ALBORES, A
    AGUILAR, M
    BLAKELY, E
    [J]. HUMAN TOXICOLOGY, 1983, 2 (01): : 121 - 133
  • [8] ARSENIC IN GROUND-WATER IN 6 DISTRICTS OF WEST-BENGAL, INDIA - THE BIGGEST ARSENIC CALAMITY IN THE WORLD .1. ARSENIC SPECIES IN DRINKING-WATER AND URINE OF THE AFFECTED PEOPLE
    CHATTERJEE, A
    DAS, D
    MANDAL, BK
    CHOWDHURY, TR
    SAMANTA, G
    CHAKRABORTI, D
    [J]. ANALYST, 1995, 120 (03) : 643 - 650
  • [9] CHEN CJ, 1985, CANCER RES, V45, P5895
  • [10] IDENTIFICATION OF A NOVEL, THIOL-CONTAINING COFACTOR ESSENTIAL FOR GLUTATHIONE-REDUCTASE ENZYME-ACTIVITY IN TRYPANOSOMATIDS
    FAIRLAMB, AH
    CERAMI, A
    [J]. MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 1985, 14 (02) : 187 - 198