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J Mol Neurosci. 2003;20(3):223-32.

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

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  • 1lzheimer's Research Center, Department of Pharmacology and Toxicology, Medical College of Georgia, Augusta, GA 30912, USA.

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 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.

PMID:
14501001
[PubMed - indexed for MEDLINE]
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