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Journal of Lipid Research, Vol 25, 1109-1116, Copyright © 1984 by Lipid Research, Inc.
UP Steinbrecher, M Fisher, JL Witztum and LK Curtiss
We previously showed that immunization of guinea pigs with reductively
glucosylated guinea pig low density lipoprotein (LDL) or albumin resulted
in the formation of antibodies specific for the glucosylated protein. The
present studies were done to determine if modifications of homologous LDL
or albumin, other than addition of carbohydrate, would also render these
proteins immunogenic. We found that derivatization of lysine residues of
guinea pig LDL or albumin by carbamylation, acetylation, ethylation, or
even methylation rendered them immunogenic in guinea pigs. In addition, the
specificity of the antibodies was strikingly influenced by whether modified
homologous LDL or modified homologous albumin was used as the immunogen.
Antibodies generated against modified LDL were directed almost exclusively
against the derivatized lysine residues (i.e., carbamyllysine,
acetyllysine, or methyllysine) and hence reacted equivalently with other
modified proteins that contained the same lysine derivative. However,
antibodies generated against guinea pig albumin (or fibrinogen) modified in
the same ways reacted primarily with the modified protein used as
immunogen, and not with the free lysine derivative, or with other similarly
modified proteins. Each of the modifications referred to above could
potentially occur in vivo. Therefore, the findings presented may be
relevant to autoantibody formation and immunopathogenetic mechanisms in
certain diseases.
ARTICLES
Immunogenicity of homologous low density lipoprotein after methylation, ethylation, acetylation, or carbamylation: generation of antibodies specific for derivatized lysine
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