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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Lee, Sung-Eun Campbell, Bruce C. Ok, Yong-Sik Kim, Jeong-Han Park, Byeoung-Soo Liu, Nannan |
| Description | Author Affiliation: Lee SE ( School of Agricultural Biotechnology, Seoul National University, Seoul 151-742, Republic of Korea.) |
| Abstract | In the present study, a permethrin-resistant strain (ALHF) of housefly was used to understand some enzymic changes in normal biosynthetic pathways after insecticide selection. Aflatoxin B(1) (AFB(1)) as a natural substrate was used to verify the changes on the level of cytochrome P450-dependent monooxygenases and oxido-reductase activities in the ALHF strain compared to an insecticide-susceptible strain, aabys. ALHF yielded three major biotransformation products: aflatoxin B(2a) (AFB(2a)), aflatoxin M(1) (AFM(1)), and aflatoxicol (AFL) by larvae. These principal products were also found in aabys. AFL production rate of ALHF larvae was 5-fold lower than that of aabys. Differences between ALHF larvae and aabys in AFM(1) production were found. ALHF did not differ significantly from aabys in AFB(2a) production. The levels of 17 - and ß-hydroxysteroid dehydrogenase (17 - and ß-HSD) were also determined to elucidate which type of dehydrogenase activities could be changed. The cytosolic fraction of ALHF larvae yielded about 2-fold higher 17 -estradiol than that of aabys larvae. In contrast, the microsomal fraction of ALHF larvae produced about 2-fold lower amount of 17 -estradiol than that of aabys larvae. The production rate of microsomal fraction of 17ß-estradiol ALHF larvae yielded 3-fold lower than that of aabys larvae. Inhibition studies on 17 -HSD and 17ß-HSD activities by pyrethroid insecticides showed that there was no inhibition by pyrethroids on the enzyme activity. Therefore, there seems to be no changes on the enzyme structures. Changes on enzyme expression may occur in ALHF larvae in relation to 17 - or ß-HSD. To assess biochemical changes of the cuticle formation phenylalanine 4-hydroxylase and tyrosinase activities were determined. The production rate of tyrosine from phenylalanine in ALHF was about 2-fold higher for larvae than that in aabys. l-(dihydroxylphenyl)alanine (DOPA) content was determined in larvae and ALHF possessed 1.6-fold larger amounts of DOPA than aabys. Tyrosinase activity of ALHF larval preparations showed 1.6-fold higher than aabys. In summary, many enzymic changes were found in ALHF strain compared to aabys strain and these changes may be resulted from the permethrin selection. |
| File Format | HTM / HTML |
| ISSN | 13826689 |
| Issue Number | 2 |
| Journal | Environmental Toxicology and Pharmacology |
| Volume Number | 20 |
| e-ISSN | 18727077 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2005-09-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Environmental Health Discipline Pharmacology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Health, Toxicology and Mutagenesis Medicine Toxicology Pharmacology |
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