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.
N1 - Funding Information:
This work was supported by a Merit Review award sponsored by the Office of Research and Development, Medical Research Service, Department of Veterans Affairs (J.J.B.), and by a VISN 7 career development award (to S.M.). The work also was supported by NIH NS32835 and an intramural (CIGP) small grant from the Medical College of Georgia (W.D.H.). The authors would like to thank Dr. David Stern, Dean, School of Medicine, Medical College of Georgia, for his kind suggestions and insights with regard to the development of this manuscript.
Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2003
Y1 - 2003
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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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 - Molecular and Chemical Neuropathology
JF - Molecular and Chemical Neuropathology
SN - 0895-8696
IS - 3
ER -