| pubmed-article:2509465 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2509465 | lifeskim:mentions | umls-concept:C0026845 | lld:lifeskim |
| pubmed-article:2509465 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:2509465 | lifeskim:mentions | umls-concept:C0017082 | lld:lifeskim |
| pubmed-article:2509465 | lifeskim:mentions | umls-concept:C0031713 | lld:lifeskim |
| pubmed-article:2509465 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:2509465 | pubmed:issue | 31 | lld:pubmed |
| pubmed-article:2509465 | pubmed:dateCreated | 1989-11-28 | lld:pubmed |
| pubmed-article:2509465 | pubmed:abstractText | Gangliosides have profound effects on protein phosphorylation in skeletal muscle. Addition of GT1b to guinea pig muscle extract stimulated the phosphorylation of a 98-kDa protein 4-8-fold. In contrast, Ca2+ stimulated the phosphorylation of this protein and two other proteins with apparent Mr of 107,000 and 145,000, respectively. Addition of GT1b in the presence of Ca2+ further enhanced the phosphorylation of the 98-kDa protein but completely inhibited the phosphorylation of both the 107- and the 145-kDa proteins. The nature of the ganglioside-modulated 98-kDa protein has been characterized. Results on the pH activity profiles and the requirements of Ca2+ for phosphorylation suggest that this phosphoprotein may correspond to glycogen phosphorylase. Phosphorylation of purified rabbit muscle phosphorylase b by nonactivated phosphorylase kinase was stimulated by GT1b. This stimulation was in part due to an activation of the kinase activity. Autophosphorylation of highly purified phosphorylase kinase was increased 4-10-fold in the presence of GT1b. Polysialogangliosides were more potent than monosialogangliosides in stimulating the autocatalytic activity, whereas asialo-GM1, colominic acid, N-acetylneuraminic acid, and phosphatidylserine were ineffective. The effects of gangliosides were dose-dependent. At physiological pH, the concentrations of GT1b required for half-maximal stimulation of the autophosphorylation of phosphorylase kinase were 6.4 microM in the absence of Ca2+ and 1.3 microM when the divalent cation was present. These findings suggest that gangliosides may play a role as biomodulators in the regulation of glycogenolysis in muscle. | lld:pubmed |
| pubmed-article:2509465 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2509465 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2509465 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2509465 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2509465 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2509465 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2509465 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2509465 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2509465 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2509465 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2509465 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2509465 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2509465 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2509465 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2509465 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2509465 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:2509465 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:2509465 | pubmed:author | pubmed-author:ChanK FKF | lld:pubmed |
| pubmed-article:2509465 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2509465 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:2509465 | pubmed:volume | 264 | lld:pubmed |
| pubmed-article:2509465 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2509465 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2509465 | pubmed:pagination | 18632-7 | lld:pubmed |
| pubmed-article:2509465 | pubmed:dateRevised | 2008-8-14 | lld:pubmed |
| pubmed-article:2509465 | pubmed:meshHeading | pubmed-meshheading:2509465-... | lld:pubmed |
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| pubmed-article:2509465 | pubmed:meshHeading | pubmed-meshheading:2509465-... | lld:pubmed |
| pubmed-article:2509465 | pubmed:meshHeading | pubmed-meshheading:2509465-... | lld:pubmed |
| pubmed-article:2509465 | pubmed:meshHeading | pubmed-meshheading:2509465-... | lld:pubmed |
| pubmed-article:2509465 | pubmed:meshHeading | pubmed-meshheading:2509465-... | lld:pubmed |
| pubmed-article:2509465 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2509465 | pubmed:articleTitle | Ganglioside-modulated protein phosphorylation in muscle. Activation of phosphorylase b kinase by gangliosides. | lld:pubmed |
| pubmed-article:2509465 | pubmed:affiliation | Laboratory of Experimental Neuropathology, National Institute of Neurological Disorders and Stroke, Bethesda, Maryland 20892. | lld:pubmed |
| pubmed-article:2509465 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2509465 | pubmed:publicationType | Comparative Study | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2509465 | lld:pubmed |
