Abstract
Purine metabolism is one mechanism to maintain cellular ATP concentration. The pathway to degrade adenosine nucleotide directly involves in stabilization of the energy charge during ATP consumption. AMP deaminase (E.C.3.5.4.6.; AMPD), which catalyzes the hydrolytic deamination of AMP and converts it to IMP, is thought to play an important role in purine metabolism in all eukaryotic cells. In higher eukaryotes, AMPD has multiple isoforms encoded by a family of AMPD multigenes.1 There are three genes in human: AMPD1, AMPD2, AMPD3, whose products are predominant in muscle (M), liver (L) and erythrocyte (E), respectively.2–4 In rodent, two genes, Ampd1 and Ampd2 that are equivalent to the human AMPD1 and AMPD2, respectively, have been known,2–5 but the gene corresponding to AMPD3 has not been reported. From the analogy of human AMPD, this hypothetical gene has been inferred to code for heart(H)-type AMPD, but molecular studies with rodent heart AMPD has not been done. In this study, mouse cDNA and the gene encoding H-isoform of AMPD have been isolated and characterized for the first time.
The sequence data have been submitted to EMBL/Genbank/DDBJ databases (D85596, D88984-D88994).
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Sabina RL, Swain JL, Holmes EW: Myoadenylate deaminase deficiency. In Metabolic and Molecular Basis of Inherited Diseases. (C. Scriver, L. Beaudet, W.S. Sly, D. Valle, Eds.) Vol. 2. pp 1769–1780, McGraw-Hill, New York, NY, 1995.
Sabina RL, Morisaki T, Clarke P, Eddy R, Show TB, Morton CC, Holmes EW: Characterization of the human and rat myoadenylate deaminase genes. J.Biol.Chem. 265: 9423–9433, 1990.
Bausch-Jurken MT, Mahnke-Zizelman DK, Morisaki T, Sabina RL: Molecular cloning of AMP deaminase isoform L. Sequence and bacterial expression of human AMPD2 cDNA. J.Biol.Chem. 267: 22407–22413, 1992.
Mahnke-Zizelman DK, Sabina RL: Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5′-exons. J.Biol.Chem. 267: 20866–20877, 1992.
Morisaki T, Sabina RL, Holmes EW: Adenylate deaminase. A multigene family in humans and rats. J.Biol.Chem. 265: 11482–11486, 1990.
Wang X, Morisaki H, Sermsuvitayawong K, Mineo I, Toyama K, Ogasawara N, Mukai T, Morisaki T: Cloning and expression of cDNA encoding heart-type isoform of AMP deaminase. Gene 188: 285–290, 1997.
Ogasawara N, Goto H, Yamada Y, Watanabe T: Distribution of AMP-isozymes in rat tissues. Eur.J.Biochem. 87: 297–304, 1978.
Sermsuvitayawong K, Wang X, Nagabukuro A, Matsuda Y, Morisaki H, Toyama K, Mukai T, Morisaki T: Genomic organization of Ampd3, heart-type AMPD gene, located in mouse chromosome 7. Mammal. enom (in press).
Mahnke-Zizelman DK, Eddy R, Show TB, Sabina R: Characterization of the human AMPD3 gene reveals that 5′ exon usage is subject to transcriptional control by three tandem promoters and alternative splicing. Biochem.Biophys.Acta 1306: 75–92, 1996.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1998 Springer Science+Business Media New York
About this chapter
Cite this chapter
Morisaki, T. et al. (1998). Molecular Analysis of Mouse ampd3 Gene Encoding Heart-Type Isoform of Amp Deaminase. In: Griesmacher, A., Müller, M.M., Chiba, P. (eds) Purine and Pyrimidine Metabolism in Man IX. Advances in Experimental Medicine and Biology, vol 431. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5381-6_67
Download citation
DOI: https://doi.org/10.1007/978-1-4615-5381-6_67
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-7456-5
Online ISBN: 978-1-4615-5381-6
eBook Packages: Springer Book Archive