Genomic organization and transcription of superoxide dismutase genes (<i>sod1</i>, <i>sod2</i>, and <i>sod3b</i>) and response to diazinon toxicity in platyfish (<i>Xiphophorus maculatus</i>) by using SOD enzyme activity

The aim of this study is to determine the effects of 50% of 96 h LC50 (5.25 ppm) diazinon on the expression of superoxide dismutase (SOD) enzyme genes (sod1, sod2, and sod3b) and SOD enzyme activity at the end of 24, 48, 72, and 96 h in platyfish liver and gill tissues. To this end, we determined the tissue-specific distribution of sod1, sod2, and sod3b genes and performed in silico analyses in platyfish (Xiphophorus maculatus). It was determined that malondialdehyde (MDA) level and SOD enzyme activity were increased in the liver [(43.90 EU mg protein(-1) (control), 62.45 EU mg protein(-1) (24 h), 73.17 EU mg protein(-1) (48 h), 82.18 EU mg protein(-1) (72 h), 92.93 EU mg protein(-1) (96 h)] and gill [(16.44 EU mg protein(-1) (control), 33.47 EU mg protein(-1) (24 h), 50.38 EU mg protein(-1) (48 h), 64.62 EU mg protein(-1) (72 h), 74.04 EU mg protein(-1) (96 h)] tissues of platyfish exposed to diazinon, while the expression of the sod genes was down-regulated. The tissue-specific distribution of the sod genes varied, with the tissues and the sod genes expression were being predominant in the liver (628.32 in sod1, 637.59 in sod2, 888.5 in sod3b). Thus, the liver was considered a suitable tissue for further gene expression studies. Based on the phylogenetic analyses, platyfish sod genes can be reported to be orthologs of sod/SOD genes from other vertebrates. Identity/similarity analyses supported this determination. Conserved gene synteny proved that there are conserved sod genes in platyfish, zebrafish, and humans.

Journal

ANIMAL BIOTECHNOLOGY

Year

2023

Volume

34

Issue

8

Pages

3578-3588

ISSN

1049-5398

eISSN

1532-2378

DOI

10.1080/10495398.2023.2178931

WoS UID

WOS:000935231300001