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Phage‐Displayed Antibodies for the Detection of Glycated Proteasome in Aging Cells
Author(s) -
GONZALEZDOSAL REGINA,
SØRENSEN MORTEN DRÆBY,
CLARK BRIAN F.C.,
RATTAN SURESH I. S.,
KRISTENSEN PETER
Publication year - 2006
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1354.068
Subject(s) - proteasome , glycation , protein subunit , ubiquitin , telomerase , microbiology and biotechnology , antibody , chemistry , biology , biochemistry , immunology , receptor , gene
Accumulation of posttranslationally damaged proteins during aging could explain the decline of cell performance with age. N ɛ ‐carboxymethyllysine (CML) is the major glycation product on damaged proteins, causing dysfunction and cross‐linking. The proteasome, a multicatalytic degradation complex, is one of the pathways for eliminating damaged proteins, and thus regulating their accumulation within the cell. However, the proteinase activities of the proteasome decline during aging. This may be due to posttranslational modifications of the subunits forming the proteasome complex. Using phage display technology, we have selected 16 single‐chain variable fragments (scFv) recognizing the CML‐modified α7 subunit of the proteasome. Using one of them, Ab3, we have observed a five‐fold increase of CML‐α7 in old human skin fibroblasts in comparison with young fibroblasts and telomerase‐immortalized bone marrow cells (hTERT‐BMCs).