Related Experiment Video
Updated: Aug 8, 2026

Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70
Published on: March 8, 2024
Response and function of skeletal muscle heat shock protein 70
Yuefei Liu1, Larissa Gampert, Katja Nething
1Department of Cardiology, University of Ulm, Ulm, Germany. yuefei.liu@medizin.uni-ulm.de
Abstract:
In response to stress, cells produce a series of heat shock proteins (Hsps). One of the most prominent Hsps, is the 70 kDa Hsp (Hsp70). Hsp70 is a highly conserved and essential protein against stress. The skeletal muscle responds to a diverse group of stress signals namely, muscle contraction linked energy and milieu challenges, ischemia and exercise by producing Hsp70. The extent of this Hsp70 response in skeletal muscle depends on the type and intensity of the signal, and is characterized in a muscle fiber specific manner by a special time course. Hsp70 in the skeletal muscle is regulated at transcriptional, translational and posttranslational levels. Hsp70 serves as an indicator for cellular stress as a molecular chaperone, plays pivotal role in maintaining cellular homeostasis by preventing apoptosis, influences energy metabolism, facilitates cellular processes in terms of muscular adaptation and interacts with other signalling pathways. This review summarizes our current knowledge on the skeletal muscle Hsp70 response.
Related Concept Videos
Other Stress Responses in Bacteria
Regulation of the Unfolded Protein Response
Molecular Chaperones and Protein Folding
The...
Molecular Chaperones and Protein Folding
The...
Bacterial Protein Maturation
The Unfolded Protein Response

