Phage-displayed antibodies for the detection of glycated proteasome in aging cells

Regina Gonzalez-Dosal, Morten Dræby Sørensen, Brian F.C. Clark, Suresh I.S. Rattan, Peter Kristensen*

*Kontaktforfatter

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

17 Citationer (Scopus)

Abstract

Accumulation of posttranslationally damaged proteins during aging could explain the decline of cell performance with age. Nε- 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).

OriginalsprogEngelsk
TidsskriftAnnals of the New York Academy of Sciences
Vol/bind1067
Udgave nummer1
Sider (fra-til)474-478
Antal sider5
ISSN0077-8923
DOI
StatusUdgivet - 1 jan. 2006
Udgivet eksterntJa

Fingeraftryk

Dyk ned i forskningsemnerne om 'Phage-displayed antibodies for the detection of glycated proteasome in aging cells'. Sammen danner de et unikt fingeraftryk.

Citationsformater