The declined phosphorylation of Heat shock protein 27 in rat cardiac muscle after hindlimb unloading

Details The declined phosphorylation of Heat shock protein 27 in rat cardiac muscle after hindlimb unloading The declined phosphorylation of Heat shock protein 27 in rat cardiac muscle after hindlimb unloading

Jul 2009

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=2009adspr..44..221y&link_type=abstract

Advances in Space Research, Volume 44, Issue 2, p. 221-225.

Physics

Scientific paper

Hindlimb unloading can induce the cardiac atrophy and diminished cardiac function, however, the mechanisms responsible for which remain elusive. The chronic volume unloading of heart, which decreases the local mechanical stress, may lead to cardiac atrophy after hindlimb unloading. Many studies showed that integrin signaling, p38 MAPK, Heat shock protein 27 and cytoskeleton involved in the hypertrophic growth induced by mechanical stress. However, the mechanisms responsible for cardiac atrophy after hindlimb unloading are still unclear. In this study, we used the tail-suspended, hindlimb unloading rat model to simulate the effects of microgravity. Western blot analysis was used to detect the protein expression of Heat shock protein 27, focal adhesion kinase, p38 MAPK and their phosphorylation levels in rat cardiac muscle after 14d hindlimb unloading. The results showed that the phosphorylation levels of both Heat shock protein 27 and p38 MAPK were decreased significantly in rat cardiac muscle after hindlimb unloading. However, the phosphorylation level of focal adhesion kinase was not decreased significantly. The results suggested that Heat shock protein 27, the downstream of p38 MAPK, might play a critical role in the cardiac atrophy in response to simulated microgravity induced by hindlimb unloading.

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