Relationship between the Induction of RAGE Cell-Surface Antigen and the Expression of Amyloid Binding Sites

Shyamala Mruthinti, William D. Hill, Satyanarayana Swamy-Mruthinti, Jerry J. Buccafusco

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


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 β peptide (Aβ). In leukocyte populations, 30-52% of lymphocytes were positive for cell-surface RAGE, and 20-25% were positive for the Aβ 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 Aβ 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.

Original languageEnglish (US)
Pages (from-to)223-232
Number of pages10
JournalJournal of Molecular Neuroscience
Issue number3
StatePublished - 2003
Externally publishedYes


  • Advanced glycation end products
  • Amyloid
  • Immune response
  • Leukocytes
  • Neurofilament protein

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience


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