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Myocardial Hsp70 Phosphorylation And Pkc-Mediated Cardioprotection Following Exercise, C.W. Melling, David Thorp, Kevin Milne, Earl Noble
Myocardial Hsp70 Phosphorylation And Pkc-Mediated Cardioprotection Following Exercise, C.W. Melling, David Thorp, Kevin Milne, Earl Noble
Jamie Melling
Both protein kinase C (PKC) activation and Hsp70 expression have been shown to be key components for exercise-mediated myocardial protection during ischemia–reperfusion injury. Given that Hsp70 has been shown to undergo inducible phosphorylation in striated muscle and liver, we hypothesized that PKC may regulate myocardial Hsp70 function and subsequent exercise-conferred cardioprotection through this phosphorylation. Hence, acute exercise of male Sprague–Dawley rats (30 m/min for 60 min at 2% grade) was employed to assess the role of PKC and its selected isoforms in phosphorylation of Hsp70 and protection of the myocardium during ischemia-reperfusion injury. It was observed that administration of the …
Invited Review: Heat Shock Proteins And Exercise: A Primer, Earl Noble, Kevin Milne, C.W. Melling
Invited Review: Heat Shock Proteins And Exercise: A Primer, Earl Noble, Kevin Milne, C.W. Melling
Jamie Melling
Heat shock proteins (HSPs) are, in general, prosurvival molecules within the cellular environment, and the overexpression of even just 1 family of HSPs can lead to protection against and improvements after a variety of stressors. Not surprisingly, a fertile area of study has grown out of effors to exploit the innate biologic behaviour of HSPs. Exercise, because of the inherent physiologic stresses associated with it, is but 1 stimulus that can result in a robust increase in various HSPs in several tissues, not the least of which happen to be the heart and skeletal muscle. The purpose of this review …
Heat Shock Proteins And Whole Body Physiology, Earl Nobe, C.W. James Melling, Kevin Milne
Heat Shock Proteins And Whole Body Physiology, Earl Nobe, C.W. James Melling, Kevin Milne
Jamie Melling
No abstract provided.
Exercise-Mediated Regulation Of Hsp70 Gene Expression Following Exercise Training, C.W. Melling, David Thorp, Kevin Milne, Matthew Krause, Earl Noble
Exercise-Mediated Regulation Of Hsp70 Gene Expression Following Exercise Training, C.W. Melling, David Thorp, Kevin Milne, Matthew Krause, Earl Noble
Jamie Melling
An issue central to understanding the biological benefits associated with regular exercise training is to elucidate the intracellular mechanisms governing exercise-conferred cardioprotection. Heat shock proteins (HSPs), most notably the inducible 70-kDa HSP family member Hsp70, are believed to participate in the protection of the myocardium during cardiovascular stress. Following acute exercise, activation of PKA mediates the suppression of an intermediary protein kinase, ERK1/2, which phosphorylates and suppresses the activation of the heat shock transcription factor 1 (HSF1). However, following exercise training, ERK1/2 has been reported to regulate the transcriptional activation of several genes involved in cell growth and proliferation and …
Pka-Mediated Erk1/2 Inactivation And Hsp70 Gene Expression Following Exercise, C.W. Melling, Matthew Krause, Earl Noble
Pka-Mediated Erk1/2 Inactivation And Hsp70 Gene Expression Following Exercise, C.W. Melling, Matthew Krause, Earl Noble
Jamie Melling
Exercise induces the expression of the cardioprotective protein, Hsp70, through the activation of its transcription factor HSF1. Recently, we reported that administration of a protein kinase A (PKA) inhibitor suppressed exercise-induced hsp70 gene expression, suggesting a role for PKA in the regulation of HSF1 activation in vivo. While the mechanism by which PKA regulates HSF1 is unclear, studies in vitro have reported that HSF1 is phosphorylated on two serine residues by mitogen activated protein kinases (MAPKs); ERK1/2 (ser307) and JNK/SAPK (ser363). As PKA is a regulator of these protein kinases, the current study examined the role of PKA in their …
Castration Inhibits The Exercise-Induced Accumulation Of Hsp70 In Male Rodent Cardiac Muscle Tissue, Kevin Milne, David Thorp, C.W. Melling, Earl Noble
Castration Inhibits The Exercise-Induced Accumulation Of Hsp70 In Male Rodent Cardiac Muscle Tissue, Kevin Milne, David Thorp, C.W. Melling, Earl Noble
Jamie Melling
Intense exercise leads to accumulation of the inducible member of the 70-kDa family of heat shock proteins, Hsp70, in male, but not female, hearts. Estrogen is at least partially responsible for this difference. Because androgen receptors are expressed in the heart and castration leads to decreases in calcium regulatory proteins and altered cardiac function, testosterone (T) or its metabolites could also be involved. We hypothesized that removal of endogenous T production through castration would reduce cardiac Hsp70 accumulation after an acute exercise bout, whereas castrated animals supplemented with 5α-dihydrotestosterone (DHT) would show the intact male response. Fifty-four 8-wk-old male Sprague-Dawley …
Regulation Of Myocardial Hsp70 Gene Expression Following Exercise, C.W. Melling, David Thorp, Earl Noble
Regulation Of Myocardial Hsp70 Gene Expression Following Exercise, C.W. Melling, David Thorp, Earl Noble
Jamie Melling
No abstract provided.