Literature DB >> 16581027

Suppression of receptor-mediated apoptosis by death effecter domain recruiting domain binding peptide aptamer.

Gab Seok Kim1, Young Ae Park, Yong Seok Choi, Yun-Hee Choi, Hyun Woo Choi, Yong-Keun Jung, Sunjoo Jeong.   

Abstract

FLASH protein is a component of death-inducing signaling complex and might be involved in death receptor-mediated extrinsic apoptosis. Here we developed the peptide aptamer against death effecter domain recruiting domain (DRD) of FLASH protein and showed that the peptide bound to FLASH protein in vitro. Intracellular expression of the DRD-binding peptide aptamer specifically suppressed receptor-mediated extrinsic apoptosis but not intrinsic pathway, which was recapitulated by the antisense oligonucleotides for FLASH. These data suggest that DRD-binding peptide is not only a novel inhibitor modulating receptor-mediated apoptosis but also a tool for elucidating the roles of FLASH in apoptosis.

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Year:  2006        PMID: 16581027     DOI: 10.1016/j.bbrc.2006.03.029

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Fluorescent peptides highlight peripheral nerves during surgery in mice.

Authors:  Michael A Whitney; Jessica L Crisp; Linda T Nguyen; Beth Friedman; Larry A Gross; Paul Steinbach; Roger Y Tsien; Quyen T Nguyen
Journal:  Nat Biotechnol       Date:  2011-02-06       Impact factor: 54.908

2.  Systems-wide RNAi analysis of CASP8AP2/FLASH shows transcriptional deregulation of the replication-dependent histone genes and extensive effects on the transcriptome of colorectal cancer cells.

Authors:  Amanda B Hummon; Jason J Pitt; Jordi Camps; Georg Emons; Susan B Skube; Konrad Huppi; Tamara L Jones; Tim Beissbarth; Frank Kramer; Marian Grade; Michael J Difilippantonio; Thomas Ried; Natasha J Caplen
Journal:  Mol Cancer       Date:  2012-01-04       Impact factor: 27.401

  2 in total

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