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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 

Ischemia-induced increase of stiffness of alphaB-crystallin/ HSPB2-deficient myocardium.

The two small heat shock proteins (sHSPs), alphaB-crystallin and HSPB2, have been shown to translocate within a few minutes of cardiac ischemia from the cytosol to myofibrils; and it has been suggested that their chaperone-like properties might protect myofibrillar proteins from unfolding or aggregation during stress conditions. Further evidence of an important role for HSPs in muscle function is provided by the fact that mutations of the alphaB-crystallin gene cause myopathy and cardiomyopathy. In the present study, we subjected isolated papillary muscles of alphaB-crystallin/ HSPB2-deficient mice to simulated ischemia and reperfusion. During ischemia in alphaB-crystallin/ HSPB2-deficient muscles, the development of contracture started earlier and reached a higher value compared to the wildtype mice. The recovery of contracture of alphaB-crystallin/ HSPB2-deficient muscles was also attenuated during the simulated reperfusion period. However, twitch force was not significantly altered at any time of the experiment. This suggests that during ischemic insults, alphaB-crystallin/ HSPB2 may not be important for the contraction process itself, but rather serve to maintain muscular elasticity.[1]

References

  1. Ischemia-induced increase of stiffness of alphaB-crystallin/HSPB2-deficient myocardium. Golenhofen, N., Redel, A., Wawrousek, E.F., Drenckhahn, D. Pflugers Arch. (2006)
 
 
 
 
 
 
 
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