Asian-Australasian Journal of Animal Sciences

  • 제22권5호
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  • Pages.712-720
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  • 2009
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  • 1011-2367(pISSN)
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  • 1976-5517(eISSN)
아세아태평양축산학회 (Asian Australasian Association of Animal Production Societies)
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Molecular Cloning, Segmental Distribution and Ontogenetic Regulation of Cationic Amino Acid Transporter 2 in Pigs

  • Zou, Shi-geng (College of Animal Science, South China Agricultural University,Guangdong Vocatioanal College of Science and Trade) ;
  • Zhi, Ai-min (College of Animal Science, South China Agricultural University) ;
  • Zhou, Xiang-yan (College of Animal Science, South China Agricultural University) ;
  • Zuo, Jian-jun (College of Animal Science, South China Agricultural University) ;
  • Zhang, Yan (College of Animal Science, South China Agricultural University) ;
  • Huang, Zhi-yi (College of Animal Science, South China Agricultural University) ;
  • Xu, Ping-Wen (College of Animal Science, South China Agricultural University) ;
  • Feng, Ding-yuan (College of Animal Science, South China Agricultural University)
  • 투고 : 2008.08.25
  • 심사 : 2008.12.16
  • 발행 : 2009.05.01
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초록

The goal of this study was to elucidate the expression and segmental distribution of the glomerular cationic amino acid metabolism transporter-2 (CAT-2) and thus to improve our understanding of porcine cationic amino acid transporters and amino acid absorption. Porcine CAT-2 was cloned, sequenced and characterized. The predicted amino acid sequence of porcine CAT-2 shared 86.1% and 92.1% identity with human and mouse CAT-2A, respectively. The tissue distribution patterns and ontogenic changes of CAT-2 mRNAs were determined by real-time Q-PCR. The results showed that porcine CAT-2 was highly expressed in the heart and intestinal tract (duodenum, ileum and jejunum). In addition, the mRNA of CAT-2 was found in liver, lung, kidney, brain and muscle. Within the intestinal tract, CAT-2 mRNA was most abundant in the ileum and rarely expressed in the duodenum. In the duodenum, the levels of CAT-2 mRNA reached their peak on day 7 (p<0.05) while in the jejunum, levels were low on day 1 and 7 and increased rapidly after day 26 before peaking on days 30 and 60 (p<0.05). The levels then dramatically decreased by day 90 (p<0.05). In the ileum, levels achieved their maximum on day 30 and then decreased significantly on day 60 (p<0.05).

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참고문헌

  1. Albritton, L. M., A. M. Bowcock, R. L. Eddy, C. C. Morton, L. Tseng, L. A. Farrer, L. L. Cavalli-Sforza, T. B. Shows and J. M. Cunningham. 1992. Intestinal apical amino acid absorption during development of the pig. Am. J. Physiol. Regul. Integr. Comp. Physiol. 280:R241-247
  2. Buddington, R. K., J. Elnif, A. A. Puchal-Gardiner and P. T. Sangild. 2001. Intestinal apical amino acid absorption during development of the pig. Am. J. Physiol. Regul. Integr. Comp. Physiol. 280:R241-247
  3. Closs, E. I., L. M. Albritton, J. W. Kim and J. M. Cunningham. 1993. Identification of a low affinity, high capacity transporter of cationic amino acids in mouse liver. J. Biol. Chem. 268: 7538-7544
  4. Closs, E. I., P. Graf, A. Habermeier, J. M. Cunningham and U. Forstermann. 1997. Human cationic amino acid transporters hCAT-1, hCAT-2A, and hCAT-2B: Three related carriers with distinct transport properties. Biochem. 36:6462-6468 https://doi.org/10.1021/bi962829p
  5. Closs, E. I., C. R. Lyons, C. Kelly and J. M. Cunningham. 1993. Characterization of the third member of the MCAT family of cationic amino acid transporters identification of a domain that determines the transport properties of the MCAT proteins. J. Biol. Chem. 268:20796-20800
  6. Cui, Z., S. Zharikov, S-L., Xia, S. I. Anderson, A. S. Law, A. L. Archibald and E. R. Block. 2005. Molecular cloning, characterization, and chromosomal assignment of porcine cationic amino acid transporter-1. Genomics 85:352-359 https://doi.org/10.1016/j.ygeno.2004.11.006
  7. de Castro, E., C. J. A. Sigrist, A. Gattiker, V. Bulliard, P. S. Langendijk-Genevaux, E. Gasteiger, A. Bairoch and N. Hulo. 2006. ScanProsite: detection of PROSITE signature matches and ProRule-associated functional and structural residues in proteins. Nucl. Acids 34:362-365 https://doi.org/10.1093/nar/gkl124
  8. Deves, R. and C. A. Boyd. 1998. Transporters for cationic amino acids in animal cells: Discovery, structure, and function. Physiol. Rev. 78:487-545 https://doi.org/10.1161/hy0202.102700
  9. Deves, R., P. Chavez and C. A. Boyd. 1992. Identification of a new transport system (y+L) in human erythrocytes that recognizes lysine and leucine with high affinity. J. Physiol. 454:491-501 https://doi.org/10.1093/emboj/18.1.49
  10. Kavanaugh, M. P., H. Wang, Z. Zhang, W. Zhang, Y. N. Wu, E. Dechant, R. A. North and D. Kabat. 1994. Control of cationic amino acid transport and retroviral receptor functions in a membrane protein family. J. Biol. Chem. 269:15445-15450
  11. Krogh, A., B. Larsson, G. V. Heijne and E. L. L. Sonnhammer. 2001. Predicting transmembrane protein topology with a hidden markov model: application to complete genomes. Journal of Molecular Biology 305:567-580 https://doi.org/10.1006/jmbi.2000.4315
  12. Lee, K.-H., D. Bunick, G. Lamprecht, I. Choi and J. M. Bahr. 2008. Differential expression of genes important to efferent ductules ion homeostasis across postnatal development in estrogen receptor-α knockout and wildtype mice. Asian-Aust. J. Anim. Sci. 21:510-522
  13. Livak, K. J. and T. D. Schmittgen. 2001. Analysis of relative gene expression data using real-time quantitative PCR and the $2^{-\Delta\Delta}CT$ Method. Methods 25:402-408 https://doi.org/10.1006/meth.2001.1262
  14. Palacin, M., R. Estevez, J. Bertran and A. Zorzano. 1998. Molecular biology of mammalian plasma membrane amino acid transporters. Physiol. Rev. 78:969-1054
  15. Sperandeo, M. P. and G. Borsani. 1998. The gene encoding a cationic amino acid transporter (SLC7A4) maps to the region deleted in the velocardiofacial syndrome. Genomics 49:230-236 https://doi.org/10.1006/geno.1998.5252
  16. Van Winkle, L. J., A. L. Campione and J. M. Gorman. 1988. Na+- independent transport of basic and zwitterionic amino acids in mouse blastocysts by a shared system and by processes which distinguish between these substrates. J. Biol. Chem. 263:3150-3163
  17. Van Winkle, L. J., H. N. Christensen and A. L. Campione. 1985. Na+-dependent transport of basic, zwitterionic, and bicyclic amino acids by a broad-scope system in mouse blastocysts. J. Biol. Chem. 260:12118-12123
  18. Vekony, N., S. Wolf, J. P. Boissel, K. Gnauert and E. I. Closs. 2001. Human cationic amino acid transporter hCAT-3 is preferentially expressed in peripheral tissues. Biochemistry 40:12387-12394 https://doi.org/10.1021/bi011345c
  19. Verrey, F., C. Meier, G. Rossier and L. C. Kuhn. 2000. Glycoprotein-associated amino acid exchangers: broadening the range of transport specificity. Pflugers Arch 440:503-512
  20. Wolf, S., A. Janzen, N. VÉkony, U. MartinÉ, D. Strand, E. I. Closs. 2002. Expression of solute carrier 7A4 (SLC7A4) in the plasma membrane is not sufficient to mediate amino acid transport activity. Biochem. J. 364:767-775 https://doi.org/10.1042/BJ20020084
  21. Yoshimoto, T., E. Yoshimoto and D. Meruelo. 1991. Molecular cloning and characterization of a novel human gene homologous to the murine ecotropic retroviral receptor. Virology 185:10-17 https://doi.org/10.1016/0042-6822(91)90748-Z
  22. Zhi, Ai-min, Ding-yuan Feng, Xiang-yan Zhou, Shi-geng Zou, Zhi-yi Huang, Jian-jun Zuo, Hui Ye, Chang-ming Zhang, Zemin Dong and Zhun Liu. 2008. Molecular cloning, tissue distribution and segmental ontogenetic regulation of $b^{o}^{+}$amino acid transporter in lantang pigs. Asian-Aust. J. Anim. Sci. 21:1134-1143

피인용 문헌

  1. Expression of cationic amino acid transporters in pig skeletal muscles during postnatal development vol.49, pp.11, 2017, https://doi.org/10.1007/s00726-017-2478-2
  2. Molecular Cloning, Tissue Distribution and Expression of Porcine y+L Amino Acid Transporter-1 vol.23, pp.2, 2009, https://doi.org/10.5713/ajas.2010.90275