Details

Autor(en) / Beteiligte

• Shorofsky, Matthew
• Maguy, Ange
• Nattel, Stanley

Titel

Consequences of Atrial or Ventricular Tachypacing on the Heat Shock Proteins (HSP) level of Expression and Phosphorylation

Ist Teil von

• McGill journal of medicine, 2009-11, Vol.12 (2), p.34-34

Ort / Verlag

Canada: McGill University

Erscheinungsjahr

2009

Quelle

EZB-FREE-00999 freely available EZB journals

Beschreibungen/Notizen

• Uncontrolled atrial fibrillation (AF) results in complex changes in the cardiomyocyte electrical and contractile functioning that promote atrial remodeling and the continuation of AF. Recently there has been a growing interest in understanding the role of heat shock proteins (HSPs), which are cytoprotective molecular chaperones, in the pathophysiology of AF. Several groups have examined HSP expression in patients with AF but have yielded mixed results. To allow for better consistency and reproducibility between subjects, we utilized canine models to reproduce AFpromoting conditions to better investigate the role of HSPs in the pathophysiology of AF. AF promoting conditions were simulated in canine models with fifteen adult mongrel dogs (20.6 to 36.0 kg) divided into three groups: (1) Control (n=5), (2) two week ventricular tachypacing (VTP) induced congestive heart failure (CHF) (n=5), and (3) one week atrial tachypacying (ATP) (n=5). Quick frozen right atrial free wall tissue samples were used for protein isolation and were analyzed via Western blotting with data was expressed as a relative ratio and were analyzed using a two-tailed, unpaired ttest and significance was set at p < 0.05. The expression levels of HSP 90, 70, and 25 were studied along with the phosphorylation status of HSP27 at serine-78. We first examined the effects of the ATP and CHF heart models on the expression of a select group of HSPs via Western Blot. We found that there was no significant difference in levels of expression of HSP 90, 70, or 25 when either ATP or CHF models were compared to control canines. The phosphorylation status of HSP27 was significantly decreased in the CHF canine model when compared to control (p < 0.0111) and it tended towards a decrease in the ATP canine model when compared to control (p=0.0923). This study showed that even though the expression levels of HSPs may remain constant, there are protein phosphorylation and dephosphorylation events that occur in AF that may have important consequences in its pathophysiology. It is therefore necessary to investigate the full scale of HSP modifications during AF and AF-promoting conditions.