Relationship between the induction of RAGE cell-surface antigen and the expression of amyloid binding sites

• Published in: Journal of molecular neuroscience 2003-01, Vol.20 (3), p.223-232
• Main Authors: Mruthinti, Shyamala, Hill, William D, Swamy-Mruthinti, Satyanarayana, Buccafusco, Jerry J
• Format: Article
• Language: English
• Subjects: Advanced glycosylation end products; Alzheimer Disease - immunology; Alzheimer Disease - metabolism; Amyloid beta-Peptides - immunology; Amyloid beta-Peptides - metabolism; Animals; Antibodies, Monoclonal; Antigens; Binding sites; Binding Sites - immunology; Blood cells; Brain; Brain - immunology; Brain - metabolism; Brain - physiopathology; Cattle; Cell surface; Female; Glycation End Products, Advanced - immunology; Glycation End Products, Advanced - metabolism; Glycosylation; Humans; Immune system; Immunization; Immunogenicity; Immunoglobulin G - blood; Immunoglobulin G - immunology; Leukocytes; Lymphocytes; Lymphocytes - immunology; Medical research; Mice; Mice, Inbred BALB C; Monoclonal antibodies; Neurofilament Proteins - immunology; Neurofilaments; Peptides; Plasma proteins; Proteins; Receptor for Advanced Glycation End Products; Receptors, Immunologic - immunology; Receptors, Immunologic - metabolism; Spleen; Toxicity; Tumor Cells, Cultured; β-Amyloid
• ISSN: 0895-8696; 0895-8696; 1559-1166
• DOI: 10.1385/JMN:20:3:223

Purified human brain neurofilament protein was subjected to glycating conditions to produce an advanced glycation end product (HNF-AGE). Two mice were immunized with this HNF-AGE. Unexpectedly, the animals generated IgGs against a peptide immunogenic fragment of the receptor for advanced glycation end products (RAGE) and against human amyloid beta peptide (Abeta). In leukocyte populations, 30-52% of lymphocytes were positive for cell-surface RAGE, and 20-25% were positive for the Abeta peptide. A monoclonal antibody (MAb) directed against the sequence of human RAGE was reactive against a 35-kDa protein band that was highly expressed in blood cells, plasma proteins, lung, liver, spleen, and brain derived from the immunized mice. A MAb directed against Abeta proteins also identified the same 35-kDa band. Thus, the time-dependent formation of AGEs might play a role within the context of the immune system in the expression of binding sites for amyloid peptides, possibly resulting in enhancing cellular toxicity.