Journal of Molecular Neuroscience

, Volume 20, Issue 3, pp 223–232

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
Target Identification And Validation

Abstract

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.

Index Entries

Advanced glycation end products neurofilament protein amyloid immune response leukocytes 

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Copyright information

© Humana Press Inc 2003

Authors and Affiliations

  • Shyamala Mruthinti
    • 1
    • 2
    • 4
  • William D. Hill
    • 1
    • 3
    • 4
  • Satyanarayana Swamy-Mruthinti
    • 5
  • Jerry J. Buccafusco
    • 1
    • 2
    • 4
  1. 1.Alzheimer’s Research CenterMedical College of GeorgiaAugusta
  2. 2.Department of Pharmacology and ToxicologyMedical College of GeorgiaAugusta
  3. 3.Department of Cellular Biology and AnatomyMedical College of GeorgiaAugusta
  4. 4.Veterans Administration Medical CenterAugusta
  5. 5.State University of West GeorgiaCarrollton

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