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Effect of exercise on in vivo insuli...

Christ-Roberts, Christine Yvonne.

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Effect of exercise on in vivo insulin signaling and action in insulin resistant skeletal muscle.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Effect of exercise on in vivo insulin signaling and action in insulin resistant skeletal muscle./
作者:	Christ-Roberts, Christine Yvonne.
面頁冊數:	163 p.
附註:	Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1170.
Contained By:	Dissertation Abstracts International64-03B.
標題:	Health Sciences, Medicine and Surgery. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3086768

Effect of exercise on in vivo insulin signaling and action in insulin resistant skeletal muscle.
Christ-Roberts, Christine Yvonne.

Effect of exercise on in vivo insulin signaling and action in insulin resistant skeletal muscle. - 163 p.

Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1170.

Thesis (Ph.D.)--The University of Texas Health Science Center at San Antonio, 2003.

Insulin action begins when insulin binds to its receptor, located in the plasma membrane of cells, causing a conformational change in the receptor and activation of its tyrosine kinase activity. This increase in insulin receptor tyrosine kinase activity leads to the autophosphorylates the insulin receptor, increasing its interaction with and phosphorylation of several signaling molecules, including Shc and insulin receptor substrates (primarily IRS-1). Signaling through Shc leads to the activation of the MAP kinase pathway, which is involved in mediating insulin's mitogenic effects. The use of MAP kinase inhibitors <italic> in vitro</italic> suggest that the MAP kinase pathway is not involved in mediating insulin's metabolic effects, however it is unclear if this is the case <italic> in vivo</italic>. Tyrosine phosphorylation of IRS-1 increases its interaction with the regulatory subunit of PI 3-kinase, increasing the catalytic activity of PI 3-kinase. Numerous studies have demonstrated that PI 3-kinase activation is necessary for mediating insulin's metabolic effects. In recent years, Akt/PKB has been shown to be a downstream mediator of PI 3-kinase and involved in insulin-stimulated glucose uptake and activation of glycogen synthase. Studies in our lab and others have determined that insulin resistance and type 2 diabetes are associated with decreased insulin signaling through the PI 3-kinase pathway, while signaling through MAP kinase is not affected.Subjects--Topical Terms:

1017756
Health Sciences, Medicine and Surgery.

Effect of exercise on in vivo insulin signaling and action in insulin resistant skeletal muscle.
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245 1 0 $a Effect of exercise on in vivo insulin signaling and action in insulin resistant skeletal muscle.
300 $a 163 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1170.
500 $a Supervisor: Lawrence J. Mandarino.
502 $a Thesis (Ph.D.)--The University of Texas Health Science Center at San Antonio, 2003.
520 $a Insulin action begins when insulin binds to its receptor, located in the plasma membrane of cells, causing a conformational change in the receptor and activation of its tyrosine kinase activity. This increase in insulin receptor tyrosine kinase activity leads to the autophosphorylates the insulin receptor, increasing its interaction with and phosphorylation of several signaling molecules, including Shc and insulin receptor substrates (primarily IRS-1). Signaling through Shc leads to the activation of the MAP kinase pathway, which is involved in mediating insulin's mitogenic effects. The use of MAP kinase inhibitors <italic> in vitro</italic> suggest that the MAP kinase pathway is not involved in mediating insulin's metabolic effects, however it is unclear if this is the case <italic> in vivo</italic>. Tyrosine phosphorylation of IRS-1 increases its interaction with the regulatory subunit of PI 3-kinase, increasing the catalytic activity of PI 3-kinase. Numerous studies have demonstrated that PI 3-kinase activation is necessary for mediating insulin's metabolic effects. In recent years, Akt/PKB has been shown to be a downstream mediator of PI 3-kinase and involved in insulin-stimulated glucose uptake and activation of glycogen synthase. Studies in our lab and others have determined that insulin resistance and type 2 diabetes are associated with decreased insulin signaling through the PI 3-kinase pathway, while signaling through MAP kinase is not affected.
520 $a Like insulin, exercise is a potent stimulator of glucose metabolism. For instance, exercise increases GLUT4 translocation to the plasma membrane, glucose disposal, glucose phosphorylation to glucose 6-phoshate, and glycogen synthase activity. While exercise acts independent of insulin, acute exercise and exercise training have been shown to increase insulin sensitivity in healthy and insulin resistant human subjects and rodents. This has important implications for the prevention and treatment of insulin resistance and type 2 diabetes. However, most studies investigating this phenomenon have been performed in healthy subjects and have yielded conflicting results. Therefore, the research set forth in this dissertation investigated the effect of exercise on insulin action and signaling in insulin resistance and type 2 diabetes. (Abstract shortened by UMI.)
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