PMID: 11331419May 2, 2001Paper

Antibodies against c-Jun N-terminal peptide cross-react with neo-epitopes emerging after caspase-mediated proteolysis during apoptosis

Journal of Neurochemistry
C CasasJ E Esquerda

Abstract

In previous studies it has been shown that neural cells undergoing programmed cell death display strongly positive cytoplasmic immunoreactivity to polyclonal antibodies directed against a c-Jun N-terminal peptide. It was later found that c-Jun-like immunoreactivity in apoptosis was due to cross-reactivity with proteins other than c-JUN: We have analysed the biochemical counterpart of this property in neuroblastoma cell lines treated to induce apoptosis. Using the c-Jun/sc-45 antibody, several bands with apparent molecular masses distinct from c-Jun were detected in extracts in parallel with both the degree of apoptosis and the appearance of the cytoplasmic signal after immunostaining. c-Jun/sc-45 immunostaining was prevented by caspase inhibitors and did not require de novo protein synthesis. One of the antigens recognized by the c-Jun/sc-45 antibody was identified as seryl-tRNA synthetase. We provide evidence that seryl-tRNA synthetase is a substrate of caspase-3 in vitro and that the digested form turns highly immunoreactive towards the antibody. A carboxy-terminus epitope of the protein that constitutes a consensus site for caspase-3 is involved in c-Jun/sc-45 recognition. This epitope shares some amino acids with the peptid...Continue Reading

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Citations

Jun 19, 2002·The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society·Joan RiberaJosep E Esquerda
Feb 22, 2002·The Journal of Biological Chemistry·Joseph Austin, Eric A First
Oct 17, 2002·Journal of Neurobiology·Noboru SatoHiroyuki Yaginuma

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