Evidence that a rapidly turning over protein, normally degraded by proteasomes, regulates hsp72 gene transcription in HepG2 cells.

@article{Zhou1996EvidenceTA,
  title={Evidence that a rapidly turning over protein, normally degraded by proteasomes, regulates hsp72 gene transcription in HepG2 cells.},
  author={Ming Zhou and Xiaosu Wu and Henry N. Ginsberg},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 40},
  pages={24769-75}
}
Heat shock protein 72/73 (Hsp70) is a cytosolic molecular chaperone that carries out fundamental roles under both normal and stress situations. There is great interest in delineating the mechanisms whereby Hsp70 levels are regulated. We observed that N-acetyl-leucyl-leucyl-norleucinal (ALLN), a synthetic aldehydic tripeptide that inhibits proteasomes, markedly induced Hsp70 levels (up to 30-fold above base line in HepG2 cells and human endothelial cells). Induction of Hsp70 by ALLN was dose… CONTINUE READING