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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 223-232 |
| Number of pages | 10 |
| Journal | Journal of Molecular Neuroscience |
| Volume | 20 |
| Issue number | 3 |
| DOIs | |
| State | Published - Dec 1 2003 |
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Keywords
- Advanced glycation end products
- Amyloid
- Immune response
- Leukocytes
- Neurofilament protein
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience
Cite this
Relationship between the Induction of RAGE Cell-Surface Antigen and the Expression of Amyloid Binding Sites. / Mruthinti, Shyamala; Hill, William D.; Swamy-Mruthinti, Satyanarayana; Buccafusco, Jerry J.
In: Journal of Molecular Neuroscience, Vol. 20, No. 3, 01.12.2003, p. 223-232.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Relationship between the Induction of RAGE Cell-Surface Antigen and the Expression of Amyloid Binding Sites
AU - Mruthinti, Shyamala
AU - Hill, William D.
AU - Swamy-Mruthinti, Satyanarayana
AU - Buccafusco, Jerry J.
PY - 2003/12/1
Y1 - 2003/12/1
N2 - 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.
AB - 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.
KW - Advanced glycation end products
KW - Amyloid
KW - Immune response
KW - Leukocytes
KW - Neurofilament protein
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UR - http://www.scopus.com/inward/citedby.url?scp=0642279880&partnerID=8YFLogxK
U2 - 10.1385/JMN:20:3:223
DO - 10.1385/JMN:20:3:223
M3 - Article
C2 - 14501001
AN - SCOPUS:0642279880
VL - 20
SP - 223
EP - 232
JO - Journal of Molecular Neuroscience
JF - Journal of Molecular Neuroscience
SN - 0895-8696
IS - 3
ER -