| pubmed-article:3087652 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3087652 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:3087652 | lifeskim:mentions | umls-concept:C0017911 | lld:lifeskim |
| pubmed-article:3087652 | lifeskim:mentions | umls-concept:C0017932 | lld:lifeskim |
| pubmed-article:3087652 | lifeskim:mentions | umls-concept:C1152161 | lld:lifeskim |
| pubmed-article:3087652 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:3087652 | pubmed:dateCreated | 1986-7-31 | lld:pubmed |
| pubmed-article:3087652 | pubmed:abstractText | The activities of glycogen synthase and glycogen phosphorylase were quantitated in liver and skeletal muscle removed following glucose infusion in hemodynamically stable endotoxin-treated rats. Four hours after the IV injection of endotoxin or saline, rats were infused with 235 mumole/min/kg of glucose or saline for up to 4 additional hr. Saline-infused endotoxemic rats had lower basal glycogen content in muscle and liver, which was associated with an increased phosphorylase a activity in both tissues compared to controls. During the glucose infusion, the rate of glycogen repletion in muscle was similar in the two groups. Skeletal muscle phosphorylase a and glycogen synthase I & D activities were elevated above control values in endotoxemia, while glycogen synthase I activity remain unchanged. These changes in the activity of muscle phosphorylase and synthase are consistent with an increased flux of carbon into and out of glycogen and a normal rate of net glycogen synthesis during glucose infusion in endotoxin-treated rats. In contrast to muscle, hepatic glycogen synthesis by endotoxemic animals was reduced compared to glucose-infused controls. Hepatic glycogen repletion in control animals appeared to be mediated primarily by a glucose-induced suppression of phosphorylase a activity rather than an increased glycogen synthase activity. Glucose infusion failed to decrease phosphorylase a activity in endotoxin-treated rats, which may be causally related to the impaired ability of these animals to replete liver glycogen. | lld:pubmed |
| pubmed-article:3087652 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3087652 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3087652 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3087652 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3087652 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3087652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3087652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3087652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3087652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3087652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3087652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3087652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3087652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3087652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3087652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3087652 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3087652 | pubmed:issn | 0092-6213 | lld:pubmed |
| pubmed-article:3087652 | pubmed:author | pubmed-author:SpitzerJ JJJ | lld:pubmed |
| pubmed-article:3087652 | pubmed:author | pubmed-author:BagbyG JGJ | lld:pubmed |
| pubmed-article:3087652 | pubmed:author | pubmed-author:LangC HCH | lld:pubmed |
| pubmed-article:3087652 | pubmed:author | pubmed-author:BudayA ZAZ | lld:pubmed |
| pubmed-article:3087652 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3087652 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:3087652 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3087652 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3087652 | pubmed:pagination | 149-63 | lld:pubmed |
| pubmed-article:3087652 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:3087652 | pubmed:meshHeading | pubmed-meshheading:3087652-... | lld:pubmed |
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| pubmed-article:3087652 | pubmed:meshHeading | pubmed-meshheading:3087652-... | lld:pubmed |
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| pubmed-article:3087652 | pubmed:meshHeading | pubmed-meshheading:3087652-... | lld:pubmed |
| pubmed-article:3087652 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:3087652 | pubmed:articleTitle | Glycogen synthase and phosphorylase activities during glycogen repletion in endotoxemic rats. | lld:pubmed |
| pubmed-article:3087652 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3087652 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3087652 | lld:pubmed |
