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Role of PKCbeta and IRS1 serine phos...

Zwetsloot, Jennifer Janine.

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Role of PKCbeta and IRS1 serine phosphorylation in skeletal muscle insulin resistance.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Role of PKCbeta and IRS1 serine phosphorylation in skeletal muscle insulin resistance./
Author:	Zwetsloot, Jennifer Janine.
Description:	257 p.
Notes:	Adviser: G. Lynis Dohm.
Contained By:	Dissertation Abstracts International67-09B.
Subject:	Biology, Physiology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3235827
ISBN:	9780542898822

Role of PKCbeta and IRS1 serine phosphorylation in skeletal muscle insulin resistance.
Zwetsloot, Jennifer Janine.

Role of PKCbeta and IRS1 serine phosphorylation in skeletal muscle insulin resistance. - 257 p.

Adviser: G. Lynis Dohm.

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

Insulin resistance in skeletal muscle from obese individuals is marked by a reduction of insulin-stimulated glucose uptake and insulin signal transduction. Insulin receptor substrate-1 (IRS1) serine phosphorylation is a commonly proposed mechanism of decreased IRS1 activity in insulin resistance. IRS1 serine phosphorylation has also been correlated to protein kinase-C (PKC) activity, and we have previously reported that basal and insulin-stimulated PKCbeta are higher in skeletal muscle from obese individuals as compared to lean. The purpose of this study was (i) to determine if basal IRS1 serine phosphorylation is elevated in skeletal muscle from obese individuals in a similar manner to PKCbeta activity; (ii) to determine if insulin-stimulated IRS1 serine phosphorylation in elevated in skeletal muscle in a similar manner to PKCbeta activity; (iii) to investigate the relationship of IRS1 serine phosphorylation and PKCbeta through manipulation of PKC activity. We found that basal IRS1 serine phosphorylation was higher at IRS1 serine 312 similar to PKCbeta activity in skeletal muscle from obese patients as compared to non-obese. We also found that insulin stimulation increased both PKCbeta activity and IRS1 serine phosphorylation at IRS1 serine 312 in skeletal muscle. Incubation with 5-aminoimidazole-4-carboxamide-ribonucleoside (AICAR)/Triacsin C to increase fatty acid oxidation and decrease intramuscular lipid activators of PKC decreased both insulin-stimulated PKCbeta activity and insulin-stimulated IRS1 serine 312 in skeletal muscle from obese patients. We also found that peroxisome proliferators activated receptor-alpha (PPARalpha) treatment, to increase fatty acid oxidation and decrease lipids, improved insulin receptor and IRS1 tyrosine phosphorylation in skeletal muscle from pediatric burn patients. In PKCbeta knockout mice, we found that insulin-stimulated IRS1 serine 307 (312 in human) was completely blocked. Insulin-stimulated IRS1 tyrosine phosphorylation and association with P13K was also higher in the knockout as compared to wild type. Together these data indicate a strong association of PKCbeta and IRS1 serine 307/312 phosphorylation in skeletal muscle.

ISBN: 9780542898822Subjects--Topical Terms:

1017816
Biology, Physiology.

Role of PKCbeta and IRS1 serine phosphorylation in skeletal muscle insulin resistance.
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245 1 0 $a Role of PKCbeta and IRS1 serine phosphorylation in skeletal muscle insulin resistance.
300 $a 257 p.
500 $a Adviser: G. Lynis Dohm.
500 $a Source: Dissertation Abstracts International, Volume: 67-09, Section: B, page: 5028.
502 $a Thesis (Ph.D.)--East Carolina University, 2006.
520 $a Insulin resistance in skeletal muscle from obese individuals is marked by a reduction of insulin-stimulated glucose uptake and insulin signal transduction. Insulin receptor substrate-1 (IRS1) serine phosphorylation is a commonly proposed mechanism of decreased IRS1 activity in insulin resistance. IRS1 serine phosphorylation has also been correlated to protein kinase-C (PKC) activity, and we have previously reported that basal and insulin-stimulated PKCbeta are higher in skeletal muscle from obese individuals as compared to lean. The purpose of this study was (i) to determine if basal IRS1 serine phosphorylation is elevated in skeletal muscle from obese individuals in a similar manner to PKCbeta activity; (ii) to determine if insulin-stimulated IRS1 serine phosphorylation in elevated in skeletal muscle in a similar manner to PKCbeta activity; (iii) to investigate the relationship of IRS1 serine phosphorylation and PKCbeta through manipulation of PKC activity. We found that basal IRS1 serine phosphorylation was higher at IRS1 serine 312 similar to PKCbeta activity in skeletal muscle from obese patients as compared to non-obese. We also found that insulin stimulation increased both PKCbeta activity and IRS1 serine phosphorylation at IRS1 serine 312 in skeletal muscle. Incubation with 5-aminoimidazole-4-carboxamide-ribonucleoside (AICAR)/Triacsin C to increase fatty acid oxidation and decrease intramuscular lipid activators of PKC decreased both insulin-stimulated PKCbeta activity and insulin-stimulated IRS1 serine 312 in skeletal muscle from obese patients. We also found that peroxisome proliferators activated receptor-alpha (PPARalpha) treatment, to increase fatty acid oxidation and decrease lipids, improved insulin receptor and IRS1 tyrosine phosphorylation in skeletal muscle from pediatric burn patients. In PKCbeta knockout mice, we found that insulin-stimulated IRS1 serine 307 (312 in human) was completely blocked. Insulin-stimulated IRS1 tyrosine phosphorylation and association with P13K was also higher in the knockout as compared to wild type. Together these data indicate a strong association of PKCbeta and IRS1 serine 307/312 phosphorylation in skeletal muscle.
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