Lymphocyte activation by oxidative modification: avidin-modified T cells activate biotin-modified autologous T cells but not vice versa |
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| Authors: | E Roffman M Wilchek |
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| Affiliation: | 1. Russian Research Center for Molecular Diagnostics and Therapy, 117638 Moscow, Russian Federation;2. Institute of Biochemical Physics, RAS, 119334 Moscow, Russian Federation;3. Federal State Institution “Federal Research Centre ‘Fundamentals of Biotechnology’ of the Russian Academy of Sciences”, 119071 Moscow, Russian Federation;4. Moscow Technological University, 119571 Moscow, Russian Federation;5. Lomonosov Moscow State University, 119991 Moscow, Russian Federation;6. National Research Center “Kurchatov Institute”, 123182 Moscow, Russian Federation;7. Engelhardt Institute of Molecular Biology, RAS, 11999 Moscow, Russian Federation;1. Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York, USA;2. Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York, USA;3. Laboratory of Cellular Physiology and Immunology, Rockefeller University, New York, New York, USA;4. Current address: Department of Medicine, Division of Immunology and Rheumatology, Stanford University School of Medicine, Stanford, California, USA;5. Current address: Laboratory of Immunology, Severance Biomedical Science Institute, Yonsei University College of Medicine, Seoul, Korea;1. School of Chemistry and Chemical Engineering, Key Laboratory of Functional Molecular Engineering of Guangdong Province, South China University of Technology, Guangzhou 510641, China;2. Molecular Diagnosis and Treatment Center for Infectious Diseases, Dermatology Hospital, Southern Medical University, Guangzhou 510091, China;1. Universidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Cátedra de Tecnología Farmacéutica I, Buenos Aires, Argentina;2. Universidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Cátedra de Química Biológica, Buenos Aires, Argentina;3. Universidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Cátedra de Física, Buenos Aires, Argentina;4. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Argentina;1. Department of Respiration, the FirstAffiliated Hospital of Zhengzhou University, Zhengzhou 450052, Henan, China;2. Department of Thoracic Surgery, the FirstAffiliatedHospital of Zhengzhou University, Zhengzhou 450052, Henan, China;1. Department of Experimental Therapeutics, British Columbia Cancer Agency, 675 West 10th Ave., Vancouver, BC V5Z 1L3, Canada;2. College for Interdisciplinary Studies, The University of British Columbia, 1855 West Mall, Vancouver, BC V6T 1Z2, Canada;3. Department of Pathology & Laboratory Medicine, Faculty of Medicine, The University of British Columbia, 2211 Wesbrook Mall, Vancouver, BC V6T 2B5, Canada;4. Faculty of Pharmaceutical Sciences, The University of British Columbia, 2146 East Mall, Vancouver, BC V6T 1Z3, Canada;5. Centre for Drug Research and Development, 2405 Wesbrook Mall, Vancouver, BC V6T 1Z3, Canada |
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| Abstract: | Immunocompetent human thymocytes were oxidized by periodate and conjugated with either biocytin-hydrazide or avidin-hydrazide followed by reduction with borohydride. Without further treatment, the resultant modified cells alone exhibited moderate levels of activation as a function of exogenously added interleukin 2. However, strong interleukin 2-dependent stimulation was observed when avidin-modified cells and biotin-modified cells were mixed. The effect was inhibited by free biotin molecules. By selective inhibition procedures, it was found that the avidin-modified cells induced the stimulation of biotin-modified cells, but not vice versa. It is postulated that the polyvalent avidin-hydrazide molecule covalently crosslinks and "freezes" the movement of oxidized glycoconjugates on the membrane surface. In contrast, the monovalent biocytin hydrazide would enable the modulation of membrane components upon interaction with avidin. The results suggest that crosslinking of mobile sites at the T-cell surface are essential for the transmission of an oxidation-induced mitogenic signal. |
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