Biopolym. Cell. 2003; 19(2):185-189.
Molecular Biomedicine
Phosphotransferase activity of IgG preparations from blood serum of humans with lupus erythromatosis pathology
1Kit Yu. Ya., 1Kovaleva V. A., 2Richter V. A.
  1. Institute of Cell Biology, NAS of Ukraine
    14/16, Drahomanov Str., Lviv, Ukraine, 79005
  2. Institute of Bioorganic Chemistry, Siberian Branch of the Academy of Sciences of the USSR
    8, Akademika Lavrentieva Ave., Novosibirsk, Russian Federation, 630090

Abstract

This article evidences that phosphotransferase activity is associated with IgG fraction from blood serum of humans with lupus erythromatosis pathology. Polyclonal IgG (f. 1) was purified by sequential chromatography on protein-A-sepharose and DEAE-Fractogel. The IgG fraction (f. 2) possessing affinity to ATP was obtained by chromatography of f. 1 on ATP-sepharose. Phosphorylation of f. 1 and f. 2 in the presence of [γ-32P]ATP caused the formation of 32P-labeled low-molecular-weight non-protein products detected by SDS-electrophoresis. These products contained 32P-labeled phospholipids which formed 6 fractions upon separation by the two-dimensional TLC. The IgG polypeptides phosphorylation was not observed. After removal of the lipids by gel-filtration in the buffer containing 5 % dioxan, the phosphorylation of H- and L-chains of IgG has been detected. Addition of 1 μM ATP to the reaction medium containing 0,018 μM [γ-32P] ATP, increased inclusion of 32P in the H-chain of IgG. We assume, that IgG-abzymes having phosphotranspherase activity may be present in blood of humans with lupus erythromatosis patology.

References

[1] Avrameas S. Natural autoantibodies: from 'horror autotoxicus' to 'gnothi seauton'. Immunol Today. 1991;12(5):154-9.
[2] Mackay IR. Burnet oration. Autoimmunity: paradigms of Burnet and complexities of today. Immunol Cell Biol. 1992;70 ( Pt 3):159-71.
[3] Dawson KH, Bell DA. Production and pathogenic effects of anti-DNA antibodies: relevance to antisense research. Antisense Res Dev. 1991 Winter;1(4):351-60.
[4] Nevinsky GA, Kanyshkova TG, Buneva VN. Natural catalytic antibodies (abzymes) in normalcy and pathology. Biochemistry (Mosc). 2000;65(11):1245-55.
[5] Paul S. Mechanism and functional role of antibody catalysis. Appl Biochem Biotechnol. 1998;75(1):13-24.
[6] Kozyr AV, Kolesnikov AV, Aleksandrova ES, Sashchenko LP, Gnuchev NV, Favorov PV, Kotelnikov MA, Iakhnina EI, Astsaturov IA, Prokaeva TB, Alekberova ZS, Suchkov SV, Gabibov AG. Novel functional activities of anti-DNA autoantibodies from sera of patients with lymphoproliferative and autoimmune diseases. Appl Biochem Biotechnol. 1998;75(1):45-61.
[7] Kanyshkova TG, Semenov DV, Vlasov AV, Khlimankov DIu, BaranovskiÄ­ AG, Shipitsyn MV, IamkovoÄ­ VI, Buneva BN, NevinskiÄ­ GA. DNA- and RNA- hydrolysed antibodies from human milk and its biological role. Mol Biol (Mosk). 1997;31(6):1082-91.
[8] Kit Y, Mitrofanova EE, Shestova OE, Kuligina EV, Romannikova IV, Richter VA. Human anti-DNA secretory immunglobulins A possess endonuclease activity and they are able to cause the destruction of nuclear chromatin in vitro. Ukr Biokhim Zh. 2000;72(3):73-6.
[9] Semenov DV, Kanyshkova TG, Kit YY, Khlimankov DY, Akimzhanov AM, Gorbunov DA, Buneva VN, Nevinsky GA. Human breast milk immunoglobulins G hydrolyze nucleotides. Biochemistry (Mosc). 1998;63(8):935-43.
[10] Kit IuIa, Semenov DV, NevinskiÄ­ GA. [Do catalytically active antibodies exist in healthy people? (Protein kinase activity of sIgA antibodies from human milk)]. Mol Biol (Mosk). 1995;29(4):893-906.
[11] Kit YY, Shipitsin MV, Semenov DV, Richter VA, Nevinsky GA. Phosphorylation of lipids tightly bound to secretory immunoglobulin A in antibody fractions from human breast milk possessing protein kinase activity. Biochemistry (Mosc). 1998;63(6):719-24.
[12] Gorbunov DV, Semenov DV, Shipitsin MV, Kit YY, Kanyshkova TG, Buneva VN, Nevinsky GA. Phosphorylation of Minor Lipids of Human Milk Tightly Bound to Secretory Immunoglobulin A. Russ J Immunol. 2000;5(3):267-278.
[13] Kit YYa, Semenov DV, Nevinsky GA. Phosphorylation of different human milk proteins by human catalytic secretory immunoglobulin A. Biochem Mol Biol Int. 1996;39(3):521-7.
[14] Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(5259):680-5.
[15] Kit YY, Semenov DV, Kuligina EV, Richter VA. Influence of nucleic acids and polysaccharides on phosphotransferase activity of preparations of secretory immunoglobulin A from human milk. Biochemistry (Mosc). 2000;65(2):237-43.
[16] Levy BD, Petasis NA, Serhan CN. Polyisoprenyl phosphates in intracellular signalling. Nature. 1997;389(6654):985-90.