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| (especial para SIIC © Derechos reservados) |
| María Belén Prados* Autora invitada por SIIC |
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![]() Profundizar Referencias bibliográficas |
| 1. Coloma MJ, Clift A, Wims L, Morrison S J. The role of carbohydrate in the assembly and function of polymeric IgG. Mol Immunol 2000; 37(18):1081-1090. 2. Jefferis R, Lund J, and Pound JD. IgG-Fc-mediated effector functions: molecular definition of interaction sites for effector ligands and the role of glycosylation. Immunol Rev, 1998; 163:59-76. 3. Mullinax F, Mullinax G. Abnormality of IgG structure in rheumatoid arthritis and systemic lupus erythematosus. Arthritis Rheum 1975; 18:417-418. 4. Tao and Morrison. Studies of aglycosylated mouse-human IgG. Role of carbohydrate in the structure and effector functions mediated by the human IgG constant region. J Immunol 1989; 143:2595-2601. 5. Tomana M, Schrohenloher R, Koopman W, Alarcon G, Paul W. Abnormal glycosylation of serum IgG from patients with chronic inflammatory diseases. Arthritis Reum 1988; 31:333-338. 6. Wright A, Tao MH, Kabat EA and Morrisson SL. Antibody variable region glycosylation: position effects on antigen binding and carbohydrate structure. EMBO J 1991; 10:2717-2723. 7. Co MS, Scheimberg N, Avdalovic NM, Mc Graw K, Vásquez M, Caron P and Queen C. Genetically engineered deglycosylation of the variable domain increases the affinity of an anti-CD33 monoclonal antibody. Mol Immuno. 1993; 30:1361-1371. 8. Margni R and Binaghi R. Non-precipitating asymmetric antibodies. Annu Rev Immunol 1988; 6:535-554. 9. Morelli L, Plotkin L, Leoni J, Fossati C and Margni R. Analysis of oligosaccharides involved in the asymmetrical glycosylation of IgG monoclonal antibodies. Mol Immunol 1993; 30:695-700. 10. Margni R. Are the non-precipitating asymmetric antibodies autoprotective and regulatory antibodies? Res Immunol (Inst. Pasteur) 1989; 140:725-729. 11. Margni R and Malan Borel I. Paradoxical behavior of asymmmetric IgG antibodies. Immunol Reviews 1998; 163:77-87. 12. Jacquemin M, Radcliffe CM, Lavend’homme R, Wormald MR, Vanderelst L, Wallays G, Dewaele J, Collen D, Vermylen J, Dwek RA, Saint-Remy JM, Rudd PM and Dewerchin M. Variable region heavy chain glycosylation determines the anticoagulant activity of a factor VIII antibody. Journal of Thrombosis and Haemostasis 2006; 4:1047–1055 13. Omtvedt LA, Bailey D, Renouf DV, Davies MJ, Paramonov NA, Haavik S, Husby G, Sletten K, Hounsell EF. Glycosylation of immunoglobulin light chains associated with amyloidosis. Amyloid 2000; (7) 4:227-244. 14. Canellada A, Blois S, Gentile T, Margni R. In vitro modulation of protective antibody responses by estrogen, progesterone and interleukin-6. Am J Reprod Immunol 2002; 47:8735-8920. 15. Gutierrez G, Malan Borel I, Margni RA. The regulatory placental factor involved in asymmetric IgG antibody synthesis responds to IL-6 features. J Reprod Immunol 2001; 49:21-32. 16. Miranda S, Canellada A, Gentile T and Margni R. Interleukin-6 and dexamethasone modulate in vitro asymmetric antibodies synthesis and UDP-Glc glycoprotein glucosyltransferase activity. J Reprod Immunol 2005; 66:141-150. 17. Szereday L, Varga P, and Szekeres-Bartho J. Cytokine production in pregnancy. Am J Reprod Immunol 1997; 38:418–422. 18. Kelemen K, Bognar I, Paal M, Szekeres-Bartho J. A progesterone-induced protein increases the synthesis of asymmetric antibodies. Cell Immunol 1996; 167(1):129-34. 19. Lachmann M, Gelbmann D, Kalman E, Polgar B, Buschle M, Gabain A, Szekeres-Bartho J, and Nagy E. PIBF (progesterone induced blocking factor) is overexpressed in highly proliferating cells and associated with the centrosome. Int J Cancer 2004; 112:51–60. 20. Kornfeld R and Kornfeld S. Assembly of asparagine linked oligosaccharides. Ann Rev Biochem 1985; 54:631-64. 21. Kelleher D, Karaoglu D, Mandon E and Gilmore R. Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol Cell 2003; 19:101-111. 22. Ruiz-Canada C, Kelleher DJ, Gilmore R. Cotranslational and Posttranslational N-Glycosylation of Polypeptides by Distinct Mammalian OST Isoforms. Cell 2009; 136:272–283. |
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Acerca del trabajo completo |
| MECANISMOS REGULATORIOS DE LA N-GLICOSILACIÓN DE LA IGG MEDIADOS POR PROGESTERONA |
| Título original en castellano PROGESTERONA INDUCE CAMBIOS EN LA EXPRESIÓN DE LAS ISOFORMAS DE LA ENZIMA OLIGOSACARILTRANSFERASA: CONSECUENCIAS EN LA N-GLICOSILACIÓN DE LA IGG |
| Autores María Belén Prados1, Julia Lablunda2, Julia Szekeres-Bartho3, Julio Caramelo4, Silvia Miranda5 |
| 1 Dra. Cs. Biológicas, Laboratorio de Glicoinmunobiología, Instituto de Investigaciones Cardiológicas "Prof. Dr. Alberto C. Taquini" (ININCA), CONICET-Universidad de Buenos Aires, Investigador 2, Laboratorio de Glicoinmunobiología, Instituto de Investigaciones Cardiológicas "prof. Dr. Alberto C. Taquini" (ininca), Conicet-universidad de Buenos Aires, Argentina. 3, Department Of Medical Microbiology And Immunology, Medical School, Pecs University 4, Instituto de Investigaciones Bioquímicas de Buenos Aires (iibba), Conicet And Fundación Instituto Leloir, Departamento de Química Biológica, Facultad de Ciencias Exactas Y Naturales, Universidad de Buenos Aires, 5, Laboratorio de Glicoinmunobiología, Instituto de Investigaciones Cardiológicas "prof. Dr. Alberto C. Taquini" (ininca), Conicet-universidad de Buenos Aires, Argentina. |
| Acceso a la fuente original Immunology Letters |
| http://www.sciencedirect.com/science/journal/01652478 |
Acceso al texto original completo (full text) |
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| El artículo se relaciona estrictamente con las especialidades de siicsalud | |
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