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Regulation of cardiac energy metabol...

University of Alberta (Canada).

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Regulation of cardiac energy metabolism and ischemia reperfusion injury by stress-responsive protein kinases.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Regulation of cardiac energy metabolism and ischemia reperfusion injury by stress-responsive protein kinases./
作者:	Jaswal, Jagdip Singh.
面頁冊數:	246 p.
附註:	Source: Dissertation Abstracts International, Volume: 68-07, Section: B, page: 4412.
Contained By:	Dissertation Abstracts International68-07B.
標題:	Health Sciences, Pharmacology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=NR29695
ISBN:	9780494296950

Regulation of cardiac energy metabolism and ischemia reperfusion injury by stress-responsive protein kinases.
Jaswal, Jagdip Singh.

Regulation of cardiac energy metabolism and ischemia reperfusion injury by stress-responsive protein kinases. - 246 p.

Source: Dissertation Abstracts International, Volume: 68-07, Section: B, page: 4412.

Thesis (Ph.D.)--University of Alberta (Canada), 2007.

Optimizing cardiac energy substrate metabolism in the ischemic and reperfused myocardium represents a novel mechanism to limit and/or ameliorate ischemia-reperfusion (IR) injury, and thus enhance the recovery of post-ischemic function. Attenuating the rate of glycolysis improves the coupling between glycolysis and glucose oxidation, and so reduces the rate of proton (H+) production, a facet of myocardial carbohydrate metabolism that is central to the cardioprotective effects of adenosine. Conversely, in select experimental models, the cardioprotective effects of adenosine are lost, and are associated with an uncoupling of glycolysis and glucose oxidation, and an acceleration of the rate of H+ production. The cellular signaling events responsible for IR injury and these metabolic effects of adenosine remain to be characterized. The stress-responsive protein kinases, AMPK and p38 MAPK are implicated in IR injury as well as the regulation of glucose uptake, and may influence myocardial glucose metabolism, and thus represent novel pharmacological targets to attenuate IR injury.

ISBN: 9780494296950Subjects--Topical Terms:

1017717
Health Sciences, Pharmacology.

Regulation of cardiac energy metabolism and ischemia reperfusion injury by stress-responsive protein kinases.
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245 1 0 $a Regulation of cardiac energy metabolism and ischemia reperfusion injury by stress-responsive protein kinases.
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500 $a Source: Dissertation Abstracts International, Volume: 68-07, Section: B, page: 4412.
502 $a Thesis (Ph.D.)--University of Alberta (Canada), 2007.
520 $a Optimizing cardiac energy substrate metabolism in the ischemic and reperfused myocardium represents a novel mechanism to limit and/or ameliorate ischemia-reperfusion (IR) injury, and thus enhance the recovery of post-ischemic function. Attenuating the rate of glycolysis improves the coupling between glycolysis and glucose oxidation, and so reduces the rate of proton (H+) production, a facet of myocardial carbohydrate metabolism that is central to the cardioprotective effects of adenosine. Conversely, in select experimental models, the cardioprotective effects of adenosine are lost, and are associated with an uncoupling of glycolysis and glucose oxidation, and an acceleration of the rate of H+ production. The cellular signaling events responsible for IR injury and these metabolic effects of adenosine remain to be characterized. The stress-responsive protein kinases, AMPK and p38 MAPK are implicated in IR injury as well as the regulation of glucose uptake, and may influence myocardial glucose metabolism, and thus represent novel pharmacological targets to attenuate IR injury.
520 $a This study characterized the role of p38 MAPK in IR injury following hypothermic ischemia, as well as the roles of p38 MAPK and AMPK in the adenosine-induced acceleration of glycolysis and H+ production in hearts stressed by transient ischemia (2 X 10-min I/5-min R). The inhibition of p38 MAPK following hypothermic ischemia was cardioprotective. During aerobic perfusion, the adenosine-induced activation of AMPK was associated with an acceleration of the rate of glycolysis. This was independent of increased glucose uptake, but was accompanied by a suppression of the rate of glycogen synthesis. Inhibition of p38 MAPK prevented the activation of AMPK, and subsequent uncoupling of glycolysis and glucose oxidation by relieving the suppression of glycogen synthesis. In stressed hearts subjected to severe IR, inhibition of p38 MAPK decreased the activity of AMPK, and improved the coupling between glycolysis and glucose oxidation by promoting glycogen synthesis, effects accompanied by enhanced post-ischemic function.
520 $a Thus, data described in these studies indicates that p38 MAPK and AMPK are involved in the regulation of glucose utilization at the level of the balance between glycolysis and glycogen synthesis, and that these kinases may represent novel targets to limit myocardial IR injury.
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