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Phosphorylation of insulin receptor ...

Zheng, Donghai.

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Phosphorylation of insulin receptor substrate-1 in development of muscle insulin resistance.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Phosphorylation of insulin receptor substrate-1 in development of muscle insulin resistance./
作者:	Zheng, Donghai.
面頁冊數:	126 p.
附註:	Adviser: G. Lynis Dohm.
Contained By:	Dissertation Abstracts International67-08B.
標題:	Biology, Cell. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3229516
ISBN:	9780542832277

Phosphorylation of insulin receptor substrate-1 in development of muscle insulin resistance.
Zheng, Donghai.

Phosphorylation of insulin receptor substrate-1 in development of muscle insulin resistance. - 126 p.

Adviser: G. Lynis Dohm.

Thesis (Ph.D.)--East Carolina University, 2006.

Phosphorylation of the insulin signaling protein insulin substrate-1 (IRS1) on serine residue 307 (312 in human IRS1) has been suggested to play an important role in insulin resistance. Protein kinase C (PKC) and c-Jun N-terminus kinase (JNK) directly and/or indirectly phosphorylate IRS1 at serine307/312 and decrease its signaling function. To study the role of PKC and JNK on insulin resistance in gestational diabetes mellitus (GDM), human rectus abdominus muscle biopsies were taken from elective abdominal surgeries of lean non-pregnant women, non-diabetic pregnant women and women with GDM. Insulin stimulation of IRS1 serine312 phosphorylation and Akt serine473 phosphorylation were used as measures of signal transduction. Skeletal muscle from GDM had significantly greater IRS1 serine312 phosphorylation than non-pregnant and pregnant non-diabetic groups, as well as elevated PKC beta II and JNK activities. An inhibitor of PKC decreased IRS1 serine312 phosphorylation and increased Akt activation in response to insulin. These results demonstrate that gestational diabetes is associated with increased JNK and PKC activities and increased serine312 phosphorylation of IRS1, which is likely to contribute to down-regulated insulin signaling and insulin resistance.

ISBN: 9780542832277Subjects--Topical Terms:

1017686
Biology, Cell.

Phosphorylation of insulin receptor substrate-1 in development of muscle insulin resistance.
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100 1 $a Zheng, Donghai. $3 1293227
245 1 0 $a Phosphorylation of insulin receptor substrate-1 in development of muscle insulin resistance.
300 $a 126 p.
500 $a Adviser: G. Lynis Dohm.
500 $a Source: Dissertation Abstracts International, Volume: 67-08, Section: B, page: 4325.
502 $a Thesis (Ph.D.)--East Carolina University, 2006.
520 $a Phosphorylation of the insulin signaling protein insulin substrate-1 (IRS1) on serine residue 307 (312 in human IRS1) has been suggested to play an important role in insulin resistance. Protein kinase C (PKC) and c-Jun N-terminus kinase (JNK) directly and/or indirectly phosphorylate IRS1 at serine307/312 and decrease its signaling function. To study the role of PKC and JNK on insulin resistance in gestational diabetes mellitus (GDM), human rectus abdominus muscle biopsies were taken from elective abdominal surgeries of lean non-pregnant women, non-diabetic pregnant women and women with GDM. Insulin stimulation of IRS1 serine312 phosphorylation and Akt serine473 phosphorylation were used as measures of signal transduction. Skeletal muscle from GDM had significantly greater IRS1 serine312 phosphorylation than non-pregnant and pregnant non-diabetic groups, as well as elevated PKC beta II and JNK activities. An inhibitor of PKC decreased IRS1 serine312 phosphorylation and increased Akt activation in response to insulin. These results demonstrate that gestational diabetes is associated with increased JNK and PKC activities and increased serine312 phosphorylation of IRS1, which is likely to contribute to down-regulated insulin signaling and insulin resistance.
520 $a To further study the mechanism of insulin resistance, cultured human myotubes were used to determine the direct effect of free fatty acids (FFA) and tumor necrosis factor (TNF) alpha on IRS1 serine312 phosphorylation level and Akt activation. Insulin stimulated Akt serine473 phosphorylation was significantly decreased by FFA and TNF alpha treatment and insulin stimulated IRS1 serine312 phosphorylation levels were increased. A PKC inhibitor significantly decreased IRS1 serine phosphorylation and increased insulin stimulated Akt phosphorylation. Our data support the hypothesis that FFA induces insulin resistance through a mechanism involving the activation of protein kinase C and suggest that IRS1 serine phosphorylation could be involved in the development of insulin resistance in pregnancy and gestational diabetes. The results of these studies provide valuable information about the causes and possible treatments of insulin resistance and gestational diabetes.
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