PUBLICATION
Hsp27 associates with the titin filament system in heat-shocked zebrafish cardiomyocytes
- Authors
- Tucker, N.R., and Shelden, E.A.
- ID
- ZDB-PUB-090714-12
- Date
- 2009
- Source
- Experimental cell research 315(8): 3176-3186 (Journal)
- Registered Authors
- Shelden, Eric
- Keywords
- Hsp27, titin, myocardium
- MeSH Terms
-
- Actin Cytoskeleton/metabolism
- Actins/metabolism*
- Animals
- Connectin
- Desmin/metabolism
- HSP27 Heat-Shock Proteins/metabolism*
- Heat-Shock Response/physiology
- Muscle Proteins/metabolism*
- Muscles/cytology
- Muscles/metabolism
- Myocardium/cytology
- Myocardium/metabolism*
- Myocytes, Cardiac/cytology
- Myocytes, Cardiac/metabolism*
- Myofibrils/metabolism
- Myosins/metabolism
- Protein Kinases/metabolism*
- Zebrafish/metabolism*
- Zebrafish Proteins/metabolism*
- PubMed
- 19580808 Full text @ Exp. Cell Res.
Citation
Tucker, N.R., and Shelden, E.A. (2009) Hsp27 associates with the titin filament system in heat-shocked zebrafish cardiomyocytes. Experimental cell research. 315(8):3176-3186.
Abstract
Injury to muscle tissue plays a central role in various cardiovascular pathologies. Overexpression of the small heat shock protein Hsp27 protects muscle cells against thermal, oxidative and ischemic stress. However, underlying mechanisms of this protection have not been resolved. A distinctive feature of muscle cells is the stress-induced association of Hsp27 with the sarcomere. The association of Hsp27 with the cytoskeleton, in both muscle and non-muscle cells, is thought to represent interaction with Z-line components or filamentous actin. Here, we examined the association of Hsp27 with myofibrils in adult zebrafish myocardium subjected to hyperthermia and mechanical stretching. Consistent with previously published results, Hsp27 in resting length myofibrils localized to narrowly defined regions, or bands, which colocalized with Z-line markers. However, analysis of stretched myofibrils revealed that the association of Hsp27 with myofibrils was independent of desmin, alpha-actinin, myosin, and filamentous actin. Instead, Hsp27 maintained a consistent relationship with a marker for the titin A/I border over various sarcomeric lengths. Finally, extraction of actin filaments revealed that Hsp27 binds to a component of the remaining sarcomere. Together, these novel data supports a mechanism of Hsp27 function where interactions with the titin filament system protect myofibrils from stress-induced degradation.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping