Transcript profiles of mitochondrial and cytoplasmic manganese superoxide dismutases in Exopalaemon carinicauda under ammonia stress

Hai Ren; Jian Li; Jitao Li; Ping Liu; Zhongxiu Liang; Jianhua Wu

doi:10.1007/s00343-015-4143-5

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Transcript profiles of mitochondrial and cytoplasmic manganese superoxide dismutases in Exopalaemon carinicauda under ammonia stress

Updated：2023-05-16

- Transcript profiles of mitochondrial and cytoplasmic manganese superoxide dismutases in Exopalaemon carinicauda under ammonia stress
- Journal of Oceanology and Limnology Vol. 33, Issue 3, Pages: 714-724(2015)
- Affiliations：
  
  1. Hebei Normal University of Science and Technology
  2. Key Laboratory of Sustainable Development of Marine Fisheries Ministry of Agriculture Yellow Sea Fisheries Research Institute Chinese Academy of Fishery Sciences
- Author bio：
- Funds：
- DOI：10.1007/s00343-015-4143-5
  CLC：
- Online First：16 January 2015，
  
  Published：2015
- Accepted：
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Ren, H., Li, J., Li, J. et al. Transcript profiles of mitochondrial and cytoplasmic manganese superoxide dismutases in Exopalaemon carinicauda under ammonia stress., Chin. J. Ocean. Limnol. 33, 714–724 (2015). https://doi.org/10.1007/s00343-015-4143-5
DOI：

Ren, H., Li, J., Li, J. et al. Transcript profiles of mitochondrial and cytoplasmic manganese superoxide dismutases in Exopalaemon carinicauda under ammonia stress., Chin. J. Ocean. Limnol. 33, 714–724 (2015). https://doi.org/10.1007/s00343-015-4143-5 DOI：

摘要

Abstract

Superoxide dismutase (SOD) is one of the most important antioxidant defense enzymes

and is considered as the first line against oxidative stress. In this study

we cloned a mitochondrial manganese (Mn) SOD (mMnSOD) cDNA from the ridgetail white prawn Exopalaemon carinicauda by using rapid amplification of cDNA ends (RACE) methods. The full-length cDNA for mMnSOD was 1 014-bp long

containing a 5′-untranslated region (UTR) of 37-bp

a 3′-UTR of 321-bp with a poly (A) tail

and included a 657-bp open reading frame encoding a protein of 218 amino acids with a 16-amino-acid signal peptide. The protein had a calculated molecular weight of 23.87 kDa and a theoretical isoelectric point of 6.75. The mMnSOD sequence included two putative N-glycosylation sites (NHT and NLS)

the MnSOD signature sequence 180DVWEHAYY187

and four putative Mn binding sites (H48

H96

D180

and H184). Sequence comparison showed that the mMnSOD deduced amino acid sequence of E. carinicauda shared 97%

95%

89%

84%

82%

72%

and 69% identity with that of Macrobrachium rosenbergii

Macrobrachium nipponense

Fenneropeneaus chinensis

Callinectes sapidus

Perisesarma bidens

Danio rerio

and Homo sapiens

resectively. Quantitative real-time RT-PCR analysis showed that mMnSOD transcripts were present in all E. carinicauda tissues examined

with the highest levels in the hepatopancreas. During an ammonia stress treatment

the transcript levels of mMnSOD and cMnSOD were up-regulated at 12 h in hemocytes and at 24 h in the hepatopancreas. As the duration of the ammonia stress treatment extended to 72 h

the transcript levels of mMnSOD and cMnSOD significantly decreased both in hemocytes and hepatopancreas. These findings indicate that the SOD system is induced to respond to acute ammonia stress

and may be involved in environmental stress responses in E. carinicauda.

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references

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