| pubmed-article:8178978 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8178978 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8178978 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:8178978 | lifeskim:mentions | umls-concept:C0026845 | lld:lifeskim |
| pubmed-article:8178978 | lifeskim:mentions | umls-concept:C0031686 | lld:lifeskim |
| pubmed-article:8178978 | lifeskim:mentions | umls-concept:C0332325 | lld:lifeskim |
| pubmed-article:8178978 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:8178978 | pubmed:issue | 4 Pt 1 | lld:pubmed |
| pubmed-article:8178978 | pubmed:dateCreated | 1994-6-9 | lld:pubmed |
| pubmed-article:8178978 | pubmed:abstractText | Reduced type 1 protein phosphatase (PP-1) activity in human muscle extracts may contribute to the reduced insulin-stimulated glycogen synthase activity associated with insulin resistance for glucose disposal in humans. Because inactive forms of PP-1 can be activated with trypsin plus Mn2+, these reagents were used to compare the PP-1 activities in skeletal muscle extracts before and after separation into cytosolic and glycogen microsomal (GM) fractions. PP-1 activities were reduced in the GM fraction from insulin-resistant subjects (54 +/- 2 vs. 61 +/- 1, P < 0.01) but, in contrast to our previously published results, were elevated in the extract (33 +/- 6 vs. 18 +/- 3, P < 0.05). Recombination of the cytosol and GM fractions (reconstituted extract) demonstrated that the low extract PP-1 activities could only be regenerated when the GM fraction from insulin-sensitive subjects was recombined with cytosol from either group. The results indicate that the elevated PP-1 activity observed in extracts of insulin-resistant compared with insulin-sensitive subjects is caused by an inhibitor of extract PP-1 activity that sediments with the GM pellet and is more active in the insulin-sensitive subjects. | lld:pubmed |
| pubmed-article:8178978 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8178978 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8178978 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8178978 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8178978 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8178978 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8178978 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8178978 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8178978 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8178978 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8178978 | pubmed:issn | 0002-9513 | lld:pubmed |
| pubmed-article:8178978 | pubmed:author | pubmed-author:MoriHH | lld:pubmed |
| pubmed-article:8178978 | pubmed:author | pubmed-author:MenzM JMJ | lld:pubmed |
| pubmed-article:8178978 | pubmed:author | pubmed-author:StoneKK | lld:pubmed |
| pubmed-article:8178978 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8178978 | pubmed:volume | 266 | lld:pubmed |
| pubmed-article:8178978 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8178978 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8178978 | pubmed:pagination | E574-82 | lld:pubmed |
| pubmed-article:8178978 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:8178978 | pubmed:meshHeading | pubmed-meshheading:8178978-... | lld:pubmed |
| pubmed-article:8178978 | pubmed:meshHeading | pubmed-meshheading:8178978-... | lld:pubmed |
| pubmed-article:8178978 | pubmed:meshHeading | pubmed-meshheading:8178978-... | lld:pubmed |
| pubmed-article:8178978 | pubmed:meshHeading | pubmed-meshheading:8178978-... | lld:pubmed |
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| pubmed-article:8178978 | pubmed:meshHeading | pubmed-meshheading:8178978-... | lld:pubmed |
| pubmed-article:8178978 | pubmed:meshHeading | pubmed-meshheading:8178978-... | lld:pubmed |
| pubmed-article:8178978 | pubmed:meshHeading | pubmed-meshheading:8178978-... | lld:pubmed |
| pubmed-article:8178978 | pubmed:meshHeading | pubmed-meshheading:8178978-... | lld:pubmed |
| pubmed-article:8178978 | pubmed:meshHeading | pubmed-meshheading:8178978-... | lld:pubmed |
| pubmed-article:8178978 | pubmed:meshHeading | pubmed-meshheading:8178978-... | lld:pubmed |
| pubmed-article:8178978 | pubmed:meshHeading | pubmed-meshheading:8178978-... | lld:pubmed |
| pubmed-article:8178978 | pubmed:meshHeading | pubmed-meshheading:8178978-... | lld:pubmed |
| pubmed-article:8178978 | pubmed:meshHeading | pubmed-meshheading:8178978-... | lld:pubmed |
| pubmed-article:8178978 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8178978 | pubmed:articleTitle | Trypsin-Mn(2+)-resistant form of type 1 protein phosphatase in human muscle. | lld:pubmed |
| pubmed-article:8178978 | pubmed:affiliation | Clinical Diabetes and Nutrition Section, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Phoenix, Arizona 85016. | lld:pubmed |
| pubmed-article:8178978 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8178978 | lld:pubmed |
