Abstract
Mammalian ARTCs are expressed as glycosylphosphatidylinositol (GPI)-anchored ectoenzymes (ARTC1–ARTC4) or secretory proteins (ARTC5) by different cell types. The ARTC2 enzymes catalyze mono-ADP-ribosylation of arginine residues in the extracellular domain of membrane proteins or secretory proteins. In this chapter we provide protocols to monitor the expression and activity of ARTCs on the cell membrane of living cells and in soluble form in biological fluids.
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References
Hottiger MO, Hassa PO, Lüscher B, Schüler H, Koch-Nolte F (2010) Toward a unified nomenclature for mammalian ADP-ribosyltransferases. Trends Biochem Sci 35:208–219
Laing S, Unger M, Koch-Nolte F, Haag F (2010) ADP-ribosylation of arginine. Amino Acids 41:257–269
Koch-Nolte F, Adriouch S, Bannas P, Krebs C, Scheuplein F, Seman M, Haag F (2006) ADP-ribosylation of membrane proteins: unveiling the secrets of a crucial regulatory mechanism in mammalian cells. Ann Med 38:188–199
Glowacki G, Braren R, Firner K, Nissen M, Kühl M, Reche P, Bazan F, Cetkovic-Cvrlje M, Leiter E, Haag F, Koch-Nolte F (2002) The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse. Protein Sci 11:1657–1670
Otto H, Reche PA, Bazan F, Dittmar K, Haag F, Koch-Nolte F (2005) In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs). BMC Genomics 6:139
Koch-Nolte F, Petersen D, Balasubramanian S, Haag F, Kahlke D, Willer T, Kastelein R, Bazan F, Thiele HG (1996) Mouse T cell membrane proteins Rt6-1 and Rt6-2 are arginine/protein mono(ADPribosyl)transferases and share secondary structure motifs with ADP-ribosylating bacterial toxins. J Biol Chem 271:7686–7693
Zolkiewska A, Moss J (1993) Integrin alpha 7 as substrate for a glycosylphosphatidylinositol-anchored ADP-ribosyltransferase on the surface of skeletal muscle cells. J Biol Chem 268:25273–25276
Moss J, Stanley SJ, Watkins PA (1980) Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from Turkey erythrocytes. J Biol Chem 255:5838–5840
Koch-Nolte F, Kernstock S, Mueller-Dieckmann C, Weiss MS, Haag F (2008) Mammalian ADP-ribosyltransferases and ADP-ribosylhydrolases. Front Biosci 13:6716–6729
Kahl S, Nissen M, Girisch R, Duffy T, Leiter EH, Haag F, Koch-Nolte F (2000) Metalloprotease-mediated shedding of enzymatically active mouse ecto-ADP-ribosyltransferase ART2.2 upon T cell activation. J Immunol 165:4463–4469
Menzel S, Rissiek B, Bannas P, Jakoby T, Miksiewicz M, Schwarz N, Nissen M, Haag F, Tholey A, Koch-Nolte F (2015) Nucleotide-induced membrane-proximal proteolysis controls the substrate specificity of T cell ecto-ADP-ribosyltransferase ARTC2.2. J Immunol 195:2057–2066
Adriouch S, Bannas P, Schwarz N, Fliegert R, Guse AH, Seman M, Haag F, Koch-Nolte F (2008) ADP-ribosylation at R125 gates the P2X7 ion channel by presenting a covalent ligand to its nucleotide binding site. FASEB J 22:861–869
Koch-Nolte F, Duffy T, Nissen M, Kahl S, Killeen N, Ablamunits V, Haag F, Leiter EH (1999) A new monoclonal antibody detects a developmentally regulated mouse ecto-ADP-ribosyltransferase on T cells: subset distribution, inbred strain variation, and modulation upon T cell activation. J Immunol 163:6014–6022
Koch-Nolte F, Glowacki G, Bannas P, Braasch F, Dubberke G, Ortolan E, Funaro A, Malavasi F, Haag F (2005) Use of genetic immunization to raise antibodies recognizing toxin-related cell surface ADP-ribosyltransferases in native conformation. Cell Immunol 236:66–71
Parusel I, Kahl S, Braasch F, Glowacki G, Halverson GR, Reid ME, Schawalder A, Ortolan E, Funaro A, Malavasi F, Hardie D, Halder S, Buckley CD, Haag F, Koch-Nolte F (2005) A panel of monoclonal antibodies recognizing GPI-anchored ADP-ribosyltransferase ART4, the carrier of the Dombrock blood group antigens. Cell Immunol 236:59–65
Krebs C, Koestner W, Nissen M, Welge V, Parusel I, Malavasi F, Leiter EH, Santella RM, Haag F, Koch-Nolte F (2003) Flow cytometric and immunoblot assays for cell surface ADP-ribosylation using a monoclonal antibody specific for ethenoadenosine. Anal Biochem 314:108–115
Möller S, Jung C, Adriouch S, Dubberke G, Seyfried F, Seman M, Haag F, Koch-Nolte F (2007) Monitoring the expression of purinoceptors and nucleotide-metabolizing ecto-enzymes with antibodies directed against proteins in native conformation. Purinergic Signal 3:359–366
Koch-Nolte F, Reyelt J, Schossow B, Schwarz N, Scheuplein F, Rothenburg S, Haag F, Alzogaray V, Cauerhff A, Goldbaum FA (2007) Single domain antibodies from llama effectively and specifically block T cell ecto-ADP-ribosyltransferase ART2.2 in vivo. FASEB J 21:3490–3498
Haag F, Koch-Nolte F, Kühl M, Lorenzen S, Thiele HG (1994) Premature stop codons inactivate the RT6 genes of the human and chimpanzee species. J Mol Biol 243:537–546
Koch-Nolte F, Klein J, Hollmann C, Kühl M, Haag F, Gaskins HR, Leiter E, Thiele HG (1995) Defects in the structure and expression of the genes for the T cell marker Rt6 in NZW and (NZB x NZW)F1 mice. Int Immunol 7:883–890
Teege S, Hann A, Miksiewicz M, MacMillan C, Rissiek B, Buck F, Menzel S, Nissen M, Bannas P, Haag F, Boyer O, Seman M, Adriouch S, Koch-Nolte F (2015) Tuning IL-2 signaling by ADP-ribosylation of CD25. Sci Rep 5:8959
Lischke T, Schumacher V, Wesolowski J, Hurwitz R, Haag F, Koch-Nolte F, Mittrücker H-W (2013) CD8-β ADP-ribosylation affects CD8(+) T-cell function. Eur J Immunol 43:1828–1838
Seman M, Adriouch S, Scheuplein F, Krebs C, Freese D, Glowacki G, Deterre P, Haag F, Koch-Nolte F (2003) NAD-induced T cell death: ADP-ribosylation of cell surface proteins by ART2 activates the cytolytic P2X7 purinoceptor. Immunity 19:571–582
Rissiek B, Danquah W, Haag F, Koch-Nolte F (2014) Technical advance: a new cell preparation strategy that greatly improves the yield of vital and functional Tregs and NKT cells. J Leukoc Biol 95:543–549
Scheuplein F, Schwarz N, Adriouch S, Krebs C, Bannas P, Rissiek B, Seman M, Haag F, Koch-Nolte F (2009) NAD+ and ATP released from injured cells induce P2X7-dependent shedding of CD62L and externalization of phosphatidylserine by murine T cells. J Immunol 182:2898–2908
Bannas P, Adriouch S, Kahl S, Braasch F, Haag F, Koch-Nolte F (2005) Activity and specificity of toxin-related mouse T cell ecto-ADP-ribosyltransferase ART2.2 depends on its association with lipid rafts. Blood 105:3663–3670
Bannas P, Well L, Lenz A, Rissiek B, Haag F, Schmid J, Hochgräfe K, Trepel M, Adam G, Ittrich H, Koch-Nolte F (2014) In vivo near-infrared fluorescence targeting of T cells: comparison of nanobodies and conventional monoclonal antibodies. Contrast Media Mol Imaging 9:135–142
Bannas P, Lenz A, Kunick V, Fumey W, Rissiek B, Schmid J, Haag F, Leingärtner A, Trepel M, Adam G, Koch-Nolte F (2015) Validation of nanobody and antibody based in vivo tumor xenograft NIRF-imaging experiments in mice using ex vivo flow cytometry and microscopy. J Vis Exp 98:52462
Bannas P, Lenz A, Kunick V, Well L, Fumey W, Rissiek B, Haag F, Schmid J, Schütze K, Eichhoff A, Trepel M, Adam G, Ittrich H, Koch-Nolte F (2015) Molecular imaging of tumors with nanobodies and antibodies: timing and dosage are crucial factors for improved in vivo detection. Contrast Media Mol Imaging 10:367–378
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Menzel, S., Adriouch, S., Bannas, P., Haag, F., Koch-Nolte, F. (2018). Monitoring Expression and Enzyme Activity of Ecto-ARTCs. In: Chang, P. (eds) ADP-ribosylation and NAD+ Utilizing Enzymes. Methods in Molecular Biology, vol 1813. Humana, New York, NY. https://doi.org/10.1007/978-1-4939-8588-3_11
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DOI: https://doi.org/10.1007/978-1-4939-8588-3_11
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