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Published on: December 16, 2011
Is Desmin Propensity to Aggregate Part of its Protective Function?
Sonia R Singh1,2, Hikmet Kadioglu3, Krishna Patel3
1Institute of Experimental Pharmacology and Toxicology, University Medical Center Hamburg-Eppendorf, 20246 Hamburg, Germany.
Insights
Desmin protein aggregates in heart failure (HF) may protect against acute stress but contribute to disease long-term. Understanding desmin
Area of Science:
- Muscle cell biology
- Cardiovascular research
- Protein biochemistry
Background:
- Desmin is a key intermediate filament (IF) protein in muscle cytoskeletons.
- Accumulation of misfolded desmin is a hallmark of heart failure (HF).
- Therapeutic reversal of desmin alterations suggests a causal role in HF development.
Purpose of the Study:
- To review the function of IFs, particularly desmin.
- To propose a model for desmin's role in stress protection.
- To explore desmin's contribution to heart failure.
Main Methods:
- Literature review of intermediate filament function.
- Analysis of desmin's role in cardiac stress.
- Proposal of an evolutionary model for desmin aggregation.
Main Results:
- IFs are known to protect cells from stress, but mechanisms are unclear.
- The heart's cyclic contraction makes it a model for IF function under mechanical stress.
- Desmin aggregation may dissipate mechanical and redox stress.
Conclusions:
- Desmin misfolding might protect against acute injury.
- Sustained desmin aggregate accumulation can impair proteostasis.
- This aggregation may contribute to heart failure pathogenesis.
Abstract:
Desmin is the major protein component of the intermediate filaments (IFs) cytoskeleton in muscle cells, including cardiac. The accumulation of cleaved and misfolded desmin is a cellular hallmark of heart failure (HF). These desmin alterations are reversed by therapy, suggesting a causal role for the IFs in the development of HF. Though IFs are known to play a role in the protection from stress, a mechanistic model of how that occurs is currently lacking. On the other hand, the heart is uniquely suited to study the function of the IFs, due to its inherent, cyclic contraction. That is, HF can be used as a model to address how IFs afford protection from mechanical, and possibly redox, stress. In this review we provide a brief summary of the current views on the function of the IFs, focusing on desmin. We also propose a new model according to which the propensity of desmin to aggregate may have been selected during evolution as a way to dissipate excessive mechanical and possibly redox stress. According to this model, though desmin misfolding may afford protection from acute injury, the sustained or excessive accumulation of desmin aggregates could impair proteostasis and contribute to disease.
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