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

Abstract

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.

Keywords:

• Bioinformatics
• mRNA expression
• platyfish
• superoxide dismutase

Disclosure statement

No potential conflict of interest was reported by the author(s).

Additional information

Funding

The present research was financially supported by Ataturk University Scientific Research Project Unit [FBA-2019-7379].