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Cloning of Pig Kidney cDNA Encoding an Angiotensin I Converting Enzyme  

Yoon, Jang-Ho (Department of Food Science and Technology, Dongguk University)
Yoon, Joo-Ok (Department of Food Science and Technology, Dongguk University)
Hong, Kwang-Won (Department of Food Science and Technology, Dongguk University)
Publication Information
Applied Biological Chemistry / v.49, no.4, 2006 , pp. 293-297 More about this Journal
Abstract
Angiotensin converting enzyme(ACE) is a zinc-containing dipeptidase widely distributed in mammalian tissues and is thought to play a significant role in blood pressure regulation by hydrolyzing angiotensin I to the potent vasoconstrictor, angiotensin II. Recently, the presence of ACE in pig ovary was reported and the ACE from pig kidney was isolated and characterized. However no nucleotide sequence of the ACE gene from pig is yet known. We report here the cloning of the ACE cDNA from pig kidney by using the reverse transcriptase-polymerase chain reaction. The complete amino acid sequence deduced from the cDNA contains 1309 residues with a molecular mass of 150 kDa, beginning with a signal peptide of 33 amino acids. Amino acid sequence analysis showed that pig kidney ACE is also probably anchored by a short transmembrane domain located near the C-terminus. This protein contains a tandem duplication of the two homologous amino acid peptidase domain. Each of these two domains bears a putative metal-binding site (His-Glu-Met-Gly-His) identified in mammalian somatic ACE. The alignment of pig ACE amino acid sequence with human, rabbit, and mouse reveals that both two domains have been highly conserved during evolution.
Keywords
pig kidney; cDNA cloning; angiotensin-converting enzyme(ACE); dipeptidyl carboxypeptidase;
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1 Cushman, D. W. and Cheung, H. S. (1971) Concentration of angiotensin I converting enzyme on tissues of rat. Biochem. Biophys. Acta 250, 261-265   DOI   ScienceOn
2 Erdos, E. G., (1990) Angiotensin I converting enzyme and the changes in our concepts through the year: Lewis K. Dahl memorial lecture. Hypertension. 16, 363-370   DOI
3 Lattion, A. L., Soubrier, F., Allegrini, J., Hubert, C., Corvol, P. and Alhenc-Gelas, F. (1989) The testicular transcript of the angiotensin converting enzyme encodes for the ancestral, nonduplicated form of the enzyme. FEBS Lett. 252, 99-104   DOI   ScienceOn
4 Kumar, R. S., Kusari, J., Roy, S. N., Soffer, R. L. and Sen, G. C. (1989) Structure of testicular angiotensin converting enzyme. A segmental mosaic isozyme. J. biol. Chem. 264, 16754- 16758
5 Thompson, J. D., Higgins, D. G. and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positionsspecific gap penalties and weight matrix choice. Nucleic Acids Research. 22, 4673-4680   DOI
6 Vallotton, M. B. (1987) The renin-angiotensin system. Trends Pharmac. Sci. 8, 69-74   DOI   ScienceOn
7 Costerousse, O., Allegrini, J., Lopez, M., and Alheng-Gelas, F. (1993) Angiotensin I converting enzyme in human circulating mononuclear cells. Genetic polymorphism of expression in Tlymphocytes. Biochem. J. 290, 33-40   DOI
8 Conell, M. J., Williams, T. A., Lamango, N. S., Dacid, C., Corvool, P., Soubrier, F., Hoheisel, J., Lehrachm H., and Isaac, R. E. (1995) Cloning and Expression of an Evolutionary Conserved Single-domain Angiotensin Converting Enzyme from Drosophila melanogaster. J. Biol. Chem. 270, 13613- 13619   DOI   ScienceOn
9 Lanzillo, J. J., Stevens, J., Dasarsthy, Y., Yotsumoto, H. and Fanburg, B. L., (1985) Angiotensin converting enzyme from human tissues. Physicochemical, catalytic, and immunological properties. J. Biol. Chem. 260, 14938-14944
10 Kumar, R. S., Thekkumkara, T. J. and Sen, C. G. (1991) The mRNA encoding the two angiotensin converting isozymes are transcribed from the same gene by a tissue-specific choice of alternative transcription initation sites. J. Biol. Chem. 266, 3854-3862
11 Matsui H. and Takahashi T. (2002) Presence of angiotensinconverting enzyme in follicular fluids of porcine ovaries and its possible involvement in the intrafollicular breakdown of bradykinin. Mol Reprod Dev. 62, 99-105   DOI   ScienceOn
12 Koike, G., Krieger, J. E., Jacob, H. J., Mukoyama, M., Pratt, R. E. and Dzau, V. J. (1994) Angiotensin converting enzyme and genetic hypertension: cloning of rat cDNAs and characterization of the enzyme. Biochem. Biophys. Res. Commun. 198, 380-386   DOI   ScienceOn
13 Kenny, A. J. and Hooper, N. M. (1991) In Degradation of Bioactive Substances: Peptidases involved in the metabolism of inactive peptides. CRC Press. Florida
14 Patchett, A. A. and Cordes, E. H. (1985) The design and properties of N-carboxyalkyldipeptide inhibitors of angiotensin converting enzyme. Adv. Enzym. 57, 1-84
15 Soubrier, F., Wei, L., Hubert, C., Clauser, E., Alhenc-Gelas, F., and Corvol, P. (1993) Molecular biology of the angiotensin converting enzyme: Structure-function. Gene polymorphism and clinical implications. J. Hypertens. 11, 599-604   DOI
16 Soffer, R. L. (1981) In Biochemical Regulation of Blood Pressure. John Wiley and Sons, New York
17 Skegges, L. T., Dorer, F. E., Kahn, J. R., Lentz, K. E. and Levine, M. (1976) The Biochemistry of the Renin-Angiotensin System and Its Role in Hypertension. Am. J. Med. 60, 737-748   DOI   ScienceOn
18 Erdos, E. G. and Skidgel, R. A. (1987) The angiotensin I converting enzyme. Lab. Invest. 56, 345-348
19 Ehlers, M. R. W., Chen, Y. N-P., and Riordan, J. F. (1989) Molecular cloning of human testicular angiotensin converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial ACE. Proc. Natl. Acad. Sci. USA 86, 7741-7745
20 Baudin, B. (2002) New aspects on angiotensin-converting enzyme: from gene to disease. Clin. Chem. Lab. Med. 40, 256- 265   DOI   ScienceOn
21 Chomczynski, P. and Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidium thiocyanate-phenolchloroform extraction. Anal. Biochem. 18, 5294-5299
22 Ehlers, M. R. and Riordan, J. F. (1989) Angiotensin converting enzyme: new concepts concerning its biological role. Proc. Biochemistry. 28, 5311-5318