Cloning of the cDNA encoding adenosine 5′-monophosphate deaminase 1 and its mRNA expression in Japanese flounder Paralichthys olivaceus

Keyong Jiang; Shujuan Sun; Mei Liu; Baojie Wang; Xiaolin Meng; Lei Wang

doi:10.1007/s00343-013-2055-9

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Cloning of the cDNA encoding adenosine 5′-monophosphate deaminase 1 and its mRNA expression in Japanese flounder Paralichthys olivaceus

Updated：2023-05-16

- Cloning of the cDNA encoding adenosine 5′-monophosphate deaminase 1 and its mRNA expression in Japanese flounder Paralichthys olivaceus
- Journal of Oceanology and Limnology Vol. 31, Issue 1, Pages: 118-127(2013)
- Affiliations：
  
  1. R&D Center of Marine Biotechnology Institute of Oceanology Chinese Academy of Sciences
  2. Graduate University of Chinese Academy of Sciences
- Author bio：
- Funds：
- DOI：10.1007/s00343-013-2055-9
  CLC：
- Online First：16 January 2013，
  
  Published：2013
- Accepted：
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Jiang, K., Sun, S., Liu, M. et al. Cloning of the cDNA encoding adenosine 5′-monophosphate deaminase 1 and its mRNA expression in Japanese flounder Paralichthys olivaceus, ., Chin. J. Ocean. Limnol. 31, 118–127 (2013). https://doi.org/10.1007/s00343-013-2055-9
DOI：

Jiang, K., Sun, S., Liu, M. et al. Cloning of the cDNA encoding adenosine 5′-monophosphate deaminase 1 and its mRNA expression in Japanese flounder Paralichthys olivaceus, ., Chin. J. Ocean. Limnol. 31, 118–127 (2013). https://doi.org/10.1007/s00343-013-2055-9 DOI：

摘要

Abstract

AMP deaminase catalyzes the conversion of AMP into IMP and ammonia. In the present study

a full-length cDNA of AMPD1 from skeletal muscle of Japanese flounder Paralichthys olivaceus was cloned and characterized. The 2 526 bp cDNA contains a 5′-UTR of 78 bp

a 3′-UTR of 237 bp and an open reading frame (ORF) of 2 211 bp

which encodes a protein of 736 amino acids. The predicted protein contains a highly conserved AMP deaminase motif (SLSTDDP) and an ATP-binding site sequence (EPLMEEYAIAAQVFK). Phylogenetic analysis showed that the AMPD1 and AMPD3 genes originate from the same branch

but are evolutionarily distant from the AMPD2 gene. RT-PCR showed that the flounder AMPD1 gene was expressed only in skeletal muscle. QRT-PCR analysis revealed a statistically significant 2.54 fold higher level of AMPD1 mRNA in adult muscle (750±40 g) compared with juvenile muscle (7.5±2 g) (P<0.05). HPLC analysis showed that the IMP content in adult muscle (3.35±0.21 mg/g) was also statistically significantly higher than in juvenile muscle (1.08±0.04 mg/g) (P<0.05). There is a direct relationship between the AMPD1 gene expression level and IMP content in the skeletal muscle of juvenile and adult flounders. These results may provide useful information for quality improvement and molecular breeding of aquatic animals.

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references

Chai L J, Chu M X, Wen J et al. 2005. Study on polymorphism of AMPD1 gene and its association with inosine monophosphate content in Beijing fatty chickens. Acta Veterinaria et Zootechnica Sinica, 36: 1 117–1 120. (in Chinese with English abstract)

Gross M, Morisaki H, Morisaki T et al. 1994. Identification of functional domains in AMPD1 by mutational analysis. Biochem. Biophys. Res. Commun., 205: 1 010–1 017.

Kaletha K, Thebault M T, Raffin J P. 1991. Comparative studies on heart and skeletal muscle AMP-deaminase from rainbow trout (Salmo gairdneri). Comp. Biochem. Physiol., 99B: 751–754.

Kuninaka A. 1960. Studies on taste of ribonucleic acid derivatives. Agric. Chem. Soc. Jpn., 34: 487–492.

Lahbib-Mansais Y, Mellink C, Yerle M et al. 1994. A new marker (NGFB) on pig chromosome 4, isolated by using a consensus sequence conserved among species. Cytogenet Cell Genet., 67: 120–125.

Li J S, Chen M L. 1998. Determination of inosinic acid in muscles by RP-HPLC. Journal of Zhejiang Agriculture University, 24: 295–296. (in Chinese with English abstract)

Loh E, Rebbeck T R, Mahoney P D. 1999. Common variant in AMPD1 gene predicts improved clinical outcome in patients with heart failure. Circulation, 11: 1 422–1 425.

Mahnke-Zizelman D K, Sabina R L. 1992. Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 50-exons. J. Biol. Chem., 267: 20 866–20 877.

Manoba T, Hasegawa K. 1991. Sensory changes in umami taste of inosine 5’-monophosphate solution after heating. Journal of Food Science, 56: 1 429–1 432.

Mardanyan S, Sharoyan S, Antonyan A et al. 2001. Tryptophan environment in adenosine deaminase: I. Enzyme modification with N-bromosuccinimide in the presence of adenosine and EHNA analogues. Biochimica et Biophysica Acta, 1 546: 185–195.

Morisaki T, Gross M, Morisaki H et al. 1992. Molecular basis of AMP deaminase deficiency in skeletal muscle. PNAS, 89: 6 457–6 461.

Morisaki T, Sabina R L, Holmes E W. 1990. Adenylate deaminase. A multi gene family in humans and rats. J. Biol. Chem., 265:11 482–11 486.

Ogasawara N, Goto H, Yamada Y et al. 1978. Distribution of AMP deaminase isozymes in rat tissues. Eur. J. Biochem., 87: 297–304.

Ogasawara N, Goto H, Yamada Y et al. 1982. AMP deaminase isozymes in human tissues. Biochim. Biophys. Acta, 714: 298–306.

Purzycka J. 1962. AMP and adenosine aminohydrolases in rat tissues. Acta Biochim. Pol., 9: 83–93.

Rico-Sanz J, Rankinen T, Joanisse D R. 2003. Associations between cardiorespiratory responses to exercise and the C34T AMPD1 gene polymorphism in the HERITAGE family study. Physiol. Genomics, 14: 161–166.

Rubio J C, Martin M A, Del-Hoyo P et al. 2000. Molecular analysis of Spanish patients with AMP deaminase deficiency. Muscle & Nerve, 23: 1 175–1 178.

Sabina R L, Mahnke-Zizelman D K. 2000. Towards an understanding of the functional significance of N-terminal domain divergence in human AMP deaminase isoforms. Pharm. Ther., 87: 279–283.

Sabina R L, Morisaki T, Clarke P et al. 1990. Characterization of the human and ratmyoadenylate deaminase genes. J. Biol. Chem., 265: 9 423–9 433.

Sabina R L, Ogasawara N, Holmes E W. 1989. Expression of three stage-specific transcripts of AMP deaminase during myogenesis. Mol. Cell. Biol., 9: 2 244–2 246.

Saitou N, Nei M. 1987. The neighbor-joining method: a new method for reconstructing phylogenic trees. Mol. Biol. Evol., 4: 406–425.

Seiko M, Minoru S, Yoshihiro S et al. 2011. Molecular characterization of adenosine 5′-monophosphate deaminase-the key enzyme responsible for the umani taste of Nori (Porphyra yezoensisi Ueda, Rhodophyta). Mar. Biotechnol., 13: 1 140–1 147.

Stankiewicz A, Spychala J, Makarewicz W. 1980. Comparative studies on muscle AMP deaminase-III. Substrate specificity of the enzyme from man, rabbit, rat, hen, frog and pikeperch. Comp. Biochem. Physiol., 66B: 529–533.

Strail A, Knoll A, Moser G et al. 2000. The porcine adenosine monophosphate deaminase 1(AMPD1) gene maps to chromosome 4. Anim Genet., 31: 147–148.

Tamura K, Dudley J, Nei M et al. 2007. MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol. Bio. Evol., 24: 1 596–1 599.

Thebault M T, Izem L, Leroy J P et al. 2005. AMP-deaminase in elasmobranch fish: a comparative histochemical and enzymatic study. Comp. Biochem. Physiol., 141B: 472–479.

Thebault M T, Tanguy A, Meistertzheim A L et al. 2010. Partial characterization of the gene encoding myoadenylate deaminase from the teleost fish Platichthys flesus. Fish Physiol. Biochem., 36: 819–825.

Wang L J, Mo X Y, Xu Y J et al. 2008. Molecular characterization and expression patterns of AMP deaminase1(AMPD1) in porcine skeletal muscle. Comp. Biochem. Physiol., 151B: 159–166.

Wessels J A, Kooloos W M, DeJonge R. 2006. Relationship between genetic variants in the adenosine pathway and outcome of methotrexate treatment in patients with recent-onset rheumatoid arthritis. Arthritis Rheum., 54: 2 830–2 839.

Yamaguchi S. 1967. The synergistic taste effect of monosodium glutamate and disodium 5′-inosinate. Food Sci., 32: 473–478.

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