| Literature DB >> 15633014 |
Sudhir Paul1, Yasuhiro Nishiyama, Stephanie Planque, Sangeeta Karle, Hiroaki Taguchi, Carl Hanson, Marc E Weksler.
Abstract
Antibodies (Abs) and enzymes are structural and functional relatives. Abs with promiscuous peptidase activity are ubiquitous in healthy humans, evidently derived from germline variable domain immunoglobulin genes encoding the serine protease-like nucleophilic function. Exogenous and endogenous electrophilic antigens can bind the nucleophilic sites covalently, and recent evidence suggests that immunization with such antigens can induce proteolytic antibodies. Previously, Ab catalytic activities have been linked to pathogenic autoimmune reactions, but recent studies indicate that proteolytic Abs may also serve beneficial functions. An example is the rapid and selective cleavage of the HIV-1 coat protein gp120 by IgMs found in uninfected humans. The selectivity of this reaction appears to derive from recognition of gp120 as a superantigen. A second example is the cleavage of amyloid beta-peptide by IgM and IgG from aged humans, a phenomenon that may represent a specific proteolytic response to a neurotoxic endogenous peptide implicated in the pathogenesis of Alzheimer's disease.Entities:
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Year: 2005 PMID: 15633014 DOI: 10.1007/s00281-004-0191-1
Source DB: PubMed Journal: Springer Semin Immunopathol ISSN: 0344-4325