pubmed-article:10334307 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10334307 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
pubmed-article:10334307 | lifeskim:mentions | umls-concept:C0242692 | lld:lifeskim |
pubmed-article:10334307 | lifeskim:mentions | umls-concept:C0021641 | lld:lifeskim |
pubmed-article:10334307 | lifeskim:mentions | umls-concept:C0017718 | lld:lifeskim |
pubmed-article:10334307 | lifeskim:mentions | umls-concept:C0031621 | lld:lifeskim |
pubmed-article:10334307 | lifeskim:mentions | umls-concept:C0164786 | lld:lifeskim |
pubmed-article:10334307 | lifeskim:mentions | umls-concept:C0574032 | lld:lifeskim |
pubmed-article:10334307 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
pubmed-article:10334307 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:10334307 | lifeskim:mentions | umls-concept:C1637379 | lld:lifeskim |
pubmed-article:10334307 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:10334307 | pubmed:dateCreated | 1999-6-10 | lld:pubmed |
pubmed-article:10334307 | pubmed:abstractText | Glucosamine, a metabolite of glucose via the hexosamine biosynthetic pathway, potently induces insulin resistance in skeletal muscle by impairing insulin-induced GLUT4 translocation to the plasma membrane. Activation of phosphoinositide (PI) 3-kinase is necessary for insulin-stimulated GLUT4 translocation, and the serine/threonine kinase Akt/protein kinase B (PKB) is a downstream mediator of some actions of PI 3-kinase. To determine whether glucosamine-induced insulin resistance could be due to impaired signaling, we measured insulin receptor substrate (IRS)-1 and insulin receptor tyrosine phosphorylation; PI 3-kinase activity associated with IRS-1, IRS-2, and phosphotyrosine; and Akt activity and phosphorylation in skeletal muscle of rats infused for 2 h with glucosamine (6.0 mg x kg(-1) x min(-1)) or saline. Euglycemic-hyperinsulinemic clamp studies (12 mU x kg(-1) x min(-1) insulin) in awake rats showed that glucosamine infusion resulted in rapid induction of insulin resistance, with a 33% decrease in glucose infusion rate (P < 0.01). Tissues were harvested after saline alone (basal), 1 min after an insulin bolus (10 U/kg), or after 2 h of insulin clamp in saline- and glucosamine-infused rats. After 1 min of insulin stimulation, phosphorylation of IRS-1 and insulin receptor increased 6- to 8-fold in saline-infused rats and 7- to 10-fold in glucosamine-infused rats. In saline-infused rats, 1 min of insulin stimulation increased PI 3-kinase activity associated with IRS-1, IRS-2, or phosphotyrosine 7.6-, 6.4-, and 10-fold, respectively. In glucosamine-infused rats treated for 1 min with insulin, PI 3-kinase activity associated with IRS-1 was reduced 28% (P < 0.01) and that associated with phosphotyrosine was reduced 43% (P < 0.01). Insulin for 1 min stimulated Akt/PKB activity approximately 5-fold in both saline- and glucosamine-infused rats; insulin-induced hyperphosphorylation of Akt/PKB was not different between groups. Glucosamine infusion alone had no effect on tyrosine phosphorylation of the insulin receptor or IRS-1 or on stimulation of PI 3-kinase or Akt/PKB activity. However, 2 h of insulin clamp reduced PI 3-kinase activity associated with IRS-1, IRS-2, or phosphotyrosine to <30% of that seen with 1 min of insulin. No effect of glucosamine was seen on these signaling events when compared with 2 h of insulin clamp without glucosamine. Our data show that 1) glucosamine infusion in rats is associated with an impairment in the early activation of PI 3-kinase by insulin in skeletal muscle, 2) this insulin-resistant state does not involve alterations in the activation of Akt/PKB, and 3) prolonged insulin infusion under clamp conditions results in a blunting of the PI 3-kinase response to insulin. | lld:pubmed |
pubmed-article:10334307 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10334307 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10334307 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10334307 | pubmed:language | eng | lld:pubmed |
pubmed-article:10334307 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10334307 | pubmed:citationSubset | AIM | lld:pubmed |
pubmed-article:10334307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10334307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10334307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10334307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10334307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10334307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10334307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10334307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10334307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10334307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10334307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10334307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10334307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10334307 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10334307 | pubmed:month | Feb | lld:pubmed |
pubmed-article:10334307 | pubmed:issn | 0012-1797 | lld:pubmed |
pubmed-article:10334307 | pubmed:author | pubmed-author:KimY BYB | lld:pubmed |
pubmed-article:10334307 | pubmed:author | pubmed-author:FuhY JYJ | lld:pubmed |
pubmed-article:10334307 | pubmed:author | pubmed-author:ZierathJ RJR | lld:pubmed |
pubmed-article:10334307 | pubmed:author | pubmed-author:BaronA DAD | lld:pubmed |
pubmed-article:10334307 | pubmed:author | pubmed-author:KahnB BBB | lld:pubmed |
pubmed-article:10334307 | pubmed:author | pubmed-author:ShenH QHQ | lld:pubmed |
pubmed-article:10334307 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10334307 | pubmed:volume | 48 | lld:pubmed |
pubmed-article:10334307 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10334307 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10334307 | pubmed:pagination | 310-20 | lld:pubmed |
pubmed-article:10334307 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:meshHeading | pubmed-meshheading:10334307... | lld:pubmed |
pubmed-article:10334307 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10334307 | pubmed:articleTitle | Glucosamine infusion in rats rapidly impairs insulin stimulation of phosphoinositide 3-kinase but does not alter activation of Akt/protein kinase B in skeletal muscle. | lld:pubmed |
pubmed-article:10334307 | pubmed:affiliation | Department of Medicine, Beth Israel-Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts 02215, USA. | lld:pubmed |
pubmed-article:10334307 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10334307 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:10334307 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10334307 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10334307 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10334307 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10334307 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10334307 | lld:pubmed |