Molecular characterization and tissue distribution of cysteamine dioxygenase (ADO) in common carp Cyprinus carpio
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Jul 22, 2019
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Abstract
The low production of hypotaurine from cysteine but a significantly high taurine deposition in common carp led to the hypothesis that this species utilizes an alternative pathway other than the cysteine sulfinic acid pathway. Cysteamine pathway is common in mammals but not in other animals such as birds, invertebrates, and fishes. The cloned cysteamine dioxygenase (ADO) cDNA in common carp consists of 790 nucleotide bases with 260 deduced amino acid sequence. The conserved domain is the DUF1637 which has a conserved tyrosine and cysteine residues and the presence of three predicted N-glycosylation sites. Phylogenetic analysis using neighbor joint method indicated that ADO in common carp branched after Sinocyclocheilus rhinocerous. ADO was expressed in hepatopancreas, brain, gill, intestine, and muscle of common carp. The hepatopacreas had a significantly higher gene expression level than the other organs examined. The present results suggest that ADO is present in common carp.
How to Cite
Gonzales-Plasus MM, Haga Y, Kondo H, Hirono I, Satoh S. 2019. Molecular characterization and tissue distribution of cysteamine dioxygenase (ADO) in common carp Cyprinus carpio. The Palawan Scientist. 11:17–28. https://doi.org/10.69721/TPS.J.2019.11.1.02.
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Keywords
ADO, tissue distribution, cysteamine pathway
References
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Yokoyama M, Takeuchi T, Park GS and Nakazoe J. 2001. Hepatic cysteinesulphinate decarboxylase activity in fish. Aquaculture Research, 32(Suppl.1): 216-220.
Chang YC, Ding ST, Lee YH, Wang YC, Huang MF and Liu IH. 2013. Taurine homeostasis requires de novo synthesis via cysteine sulfinic acid decarboxylase during zebrafish early embryogenesis. Amino Acids, 44: 615–629.
Goto T, Takagi S, Ichiki T, Sakai T, Endo M, Yoshida T, Ukawa M and Murata H. 2001a. Studies on the green liver in cultured red sea bream fed low level and non-fish meal diets: relationship between hepatic taurine and biliverdin levels. Fisheries Science, 67: 58–63.
Goto T, Matsumoto T and Takagi S. 2001b. Distribution of the hepatic cysteamine dioxygenase activities in fish. Fisheries Science, 67: 1187–1189.
Goto T, Matsumoto T, Murakami S, Takagi S and Hasumi F. 2003. Conversion of cysteate into taurine in liver of fish. Fisheries Science, 69: 216–218.
Griffith OW. 1987. Mammalian sulphuramino acid metabolism: an overview. In: Jakoby WB and Griffith OW (eds). Methods in Enzymology. Vol. 143. Academic Press, New York. pp. 366-376.
Haga Y, Kondo H, Kumagai A, Satoh N, Hirono I and Satoh S. 2015. Isolation, molecular characterization of cysteine sulfinic acid decarboxylase (CSD) of red sea bream Pagrus major and yellowtail Seriola quinqueradiata and expression analysis of CSD from several marine fish species. Aquaculture, 449: 8-17.
Higuchi M, Celino FT, Miura C and Miura T. 2012. The Synthesis and Role of Taurine in the Eel Spermatogenesis. In: Kawaguchi M, Misaki K, Sato H, Yokokawa T, Itai T, Nguyen TM, Ono J and Tanabe S (eds). Interdisciplinary Studies on Environmental Chemistry—Environmental Pollution and Ecotoxicology. Center for Marine Environmental Studies, Ehime University, Japan. © by TERRAPUB, pp. 35-40.
Huxtable RJ. 1992. Physiological actions of taurine. Physiology Review, 72: 101–163.
Jacobsen JG and Smith LH. 1968. Biochemistry and physiology of taurine and taurine derivatives. Physiology Review, 48: 424-511.
Kataoka H, Ohishi K, Imai J and Mukai M. 1988. Distribution of cysteamine dioxygenase in animal tissue. Agricultural and Biological Chemistry, 52(6): 1611-1613.
Larkin MA, Blackshields G, Brown NP, Chenna R, McGettigan PA, McWilliam H, Valentin F, Wallace IM, Wilm A, Lopez R, Thompson JD, Gibson TJ and Higgins DG. 2007. ClustalW and ClustalX version 2. Bioinformatics, 23(21): 2947-2948.
Livak KJ and Schmittgen TD. 2001. Analysis of relative gene expression data using real-time quantitative PCR and the 2−ΔΔCt method. Methods, 25: 402–408.
Marshall RD. 1972. Glycoproteins. Annual Review in Biochemistry, 41: 673-702. DOI: 10.1146/annurev.bi.41.070172.003325
Saitou N and Nei M. 1987. The Neighbor-Joining method—a new method for reconstructing phylogenetic trees. Molecular Biology and Evolution, 4: 406-425.
Stipanuk MH. 2004. Sulfur amino acid metabolism: pathways for production and removal of homocysteine and cysteine. Annual Review in Nutrition, 24: 539-577.
Stipanuk MH and Ueki I. 2011. Dealing with methionine/homocysteine sulfur: cysteine metabolism to taurine and inorganic sulfur. Journal of Inherited Metabolic Disease, 34(1): 17–32.
Tevatia R, Allen J, Rudrappa D, White D, Clemente T, Cerutti H, Demirel Y and Blum P. 2015. The taurine biosynthetic pathway of microalgae. Algal Research, 9: 21–26. DOI: 10.1016/j.algal.2015.02.012
Wang X, He G, Mai K, Xu W and Zhou H. 2015. Ontogenic taurine biosynthesis ability in rainbow trout (Oncorhynchus mykiss). Comparative Biochemistry and Physiology, 185B: 10-15.
Wang X, He G, Mai K, Xu W and Zhou H. 2016. Differential regulation of taurine biosynthesis in rainbow trout and Japanese flounder. Scientific Report, 6: 21231. DOI:10.1038/srep21231.
Watson A, Barrows F and Place A. 2015. The importance of taurine and n-3 fatty acids in Cobia, Rachycentron canadum, Nutrition. Bulletin of Fisheries Research Agency, 40 :51-59.
Worth CK and Blundell TL. 2010. On the evolutionary conservation of hydrogen bonds made by buried polar amino acids: the hidden joists, braces and trusses of protein architecture. BMC Evolutionary Biology, 10: 161. DOI: 10.1186/1471-2148-10-161.
Yokoyama M and Nakazoe J. 1991. Effects of dietary protein levels on free amino acid and glutathione content in the tissue of rainbow trout. Comparative Biochemistry and Physiology, 99B: 203-206.
Yokoyama M, Takeuchi T, Park GS and Nakazoe J. 2001. Hepatic cysteinesulphinate decarboxylase activity in fish. Aquaculture Research, 32(Suppl.1): 216-220.
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