Abstract
Among a number of tissues and peripheral blood cells in chicken, leukocytes, bone marrow cells, liver and spleen showed high ADP-ribosyltransferase activity, with leukocytes having the highest. Density gradient centrifugation of the leukocytes revealed that the leukocyte ADP-ribosyltransferase originates in the polymorphonuclear cells, so called heterophils. Subcellular distribution of the cells showed the localization of the enzyme in the granule fraction. Based on the obtained amino acid sequences of arginine-specific ADP-ribosyltransferase purified from chicken peripheral heterophils, two arginine-specific ADP-ribosyltransferase cDNAs (designated ATI and AT2) were obtained from chicken bone marrow cells. Each cDNA encodes a different peptide of 312 amino acid residues. Homology of the deduced amino acid sequences between AT1 and AT2 was 78.3%. Arginine-specific ADP-ribosyltransferase activity was detected in culture medium of COS 7 cells transiently transfected with ATI cDNA, while activity from the cells transfected with AT2 cDNA was found in both culture medium and cell lysate. ATI transferase required 2-mercaptoethanol (MSH) for the activity and in the presence of NaCl, the activity was inhibited while the AT2 enzyme was activated by either agent. Highly conserved regions were observed among the deduced amino acid sequences of AT1, AT2, chicken erythroblast and rabbit and human skeletal muscle ADP-ribosyltransferases, and rodent Tcell surface antigen RT6. Two forms of the transferase with much the same properties as AT1 and AT2 proteins, regarding the effect of NaCl and MSH, were detected in bone marrow cells. Based on these results it seems that ATI and AT2 cDNAs encode the two forms of arginine-specific ADP-ribosyltransferase detected in chicken bone marrow cells.
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
Peterson, J. E., Jacquiline, S.-A. L. & Graves, D. J. 1990. Purification and partial characterization of arginine-specific ADP-ribosyltransferase from skeletal muscle microsomal membranes. J. Biol. Chem. 265: 17602–17609.
Zolkiewska, A., Nightingale, M. S. & Moss, J. 1992. Molecular characterization of NAD:arginine ADP-ribosyltransferase from rabbit skeletal muscle. Proc. Natl. Acad. Sci. USA. 89: 11352–11356.
Okazaki, I. J., Zolkiewska, A., Nightingale, M. S. & Moss, J. 1994. Immunological and structural conservation of mammalian skeletal muscle glycosylphosphatidylinositol-linked ADP-ribosyltransferase. Biochemistry. 33: 12828–12836.
Mishima, K., Terashima, M., Obara, S., Yamada, K., lmai, K. & Shimoyama, M. 1991. Arginine-specific ADP-ribosyltransferase and its acceptor protein p33 in chicken polymorphonuclear cells: co-localization in the cell granules, partial characterization, and In Situ mono(ADP-ribosyl)ation. J. Biochem. 110: 388–394.
Terashima, M., Mishima, K., Yamada, K., Tsuchiya, M., Wakutani, T. & Shimoyama, M. 1992. ADP-ribosylation of acins by arginine-specific ADP-ribosyltransferase purified from chicken heterophils. Eur. J. Biochem. 204: 305–311.
Terashima, M., Yamamori, C. & Shimoyama, M. 1995. ADP-ribosylation of Arg28 and Arg206 on the actin molecule by chicken arginine-specific ADP-ribosyltransferase. Eur. J. Biochem. 231: 242–249.
Yamada, K., Tsuchiya, M., Nishikori, Y & Shimoyama, M. 1994. Automodification of arginine-specific ADP-ribosyltransferase purified from chicken peripheral heterophils and alteration of the transferase ativity. Arch. Biochem. Biophys. 308: 31–36.
Tsuchiya, M., Hara, N., Yamada, K., Osago, H. & Shimoyama, M. 1994. Cloning and expression of cDNA for arginine-specific ADP-ribosyltransferase from chicken bone marrow cells. J. Biol. Chem. 269: 27451–27457.
Borregaard, N., Heiple, J. M, Simons, E. R. & Clark, R. A. 1983. Subcellular localization of the b-cytochrome component of the human neutrophil microbicidal oxidase. J. Cell Biol. 97: 52–61.
von Heijne, G. 1985. Signal sequences. J. Mol. biol. 184: 99–105.
Tsuchiya, M., Tanigawa, Y, Mishima, K. & Shimoyama, M. 1986. Determination of ADP-ribosylarginine anomers by reverse-phase high-performance liquid chromatography. Anal. Biochem. 157: 381–384.
Davis, T. & Shall, S. 1995. Sequence of a chicken erythroblast mono(ADP-ribosyl)transferase-encoding gene and its upstream region. Gene. 164: 371–372.
Koch, R, Haag, R, Kashan, A. & Thiele, H.-G. 1990. Primary structure of rat RT6.2, a nonglycosylated phosphatidylinositol-linked surface marker of postthymic T cells. Proc. Natl. Acad. Sci. USA. 87: 964–967.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1997 Springer Science+Business Media New York
About this chapter
Cite this chapter
Shimoyama, M., Tsuchiya, M., Hara, N., Yamada, K., Osago, H. (1997). Molecular Cloning and Characterization of Arginine-Specific ADP-Ribosyltransferases from Chicken Bone Marrow Cells. In: Haag, F., Koch-Nolte, F. (eds) ADP-Ribosylation in Animal Tissues. Advances in Experimental Medicine and Biology, vol 419. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-8632-0_16
Download citation
DOI: https://doi.org/10.1007/978-1-4419-8632-0_16
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-4652-4
Online ISBN: 978-1-4419-8632-0
eBook Packages: Springer Book Archive