| http://purl.uniprot.org/citations/12963789 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12963789 | http://www.w3.org/2000/01/rdf-schema#comment | "Skeletal muscle that is deficient in creatine kinase (CK-/-) exhibits accelerated glycogenolysis during contraction. Understanding this phenomenon could provide insight into the control of glycogenolysis during contraction. Therefore, glycogen breakdown was investigated in isolated extensor digitorum longus CK-/-muscle. Muscles were stimulated to produce repeated tetani for 20 s in the presence of sodium cyanide to block mitochondrial respiration. Accumulation of lactate after stimulation was similar in wild-type (WT) and CK-/-muscles, whereas accumulation of glucose-6-phosphate was twofold higher in CK-/-muscles, indicating greater glycogenolysis in CK-/-muscles. Total phosphorylase activity was decreased by almost 30 % in CK-/-muscle (P < 0.001). Phosphorylase fractional activity (-/+ 3.3 mM AMP) was similar in both groups in the basal state (about 10 %), but increased to a smaller extent in CK-/- muscles after stimulation (39 +/- 4 % vs. 52 +/-4 % in WT, P < 0.05). Inorganic phosphate, the substrate for phosphorylase, increased marginally in CK-/- muscles after stimulation (basal = 25.3 +/-2.2 micromol (g dry muscle)-1; stimulated = 33.9 +/-2.3 micromol (g dry muscle)-1), but substantially in WT muscles (basal = 11.4 +/- 0.7 micromol (g dry muscle)-1; stimulated = 54.2 +/-4.5 micromol (g dry muscle)-1). Kinetic studies of phosphorylase b (dephosphorylated enzyme) from muscle extracts in vitro demonstrated higher relative activities in CK-/-muscles (60-135 %) in response to low AMP concentrations (up to 50 microM) in both the basal state and after stimulation (P < 0.05), whereas no differences in activity between CK-/- and WT muscles were observed at high AMP concentrations (> 100 microM). These data indicate that allosteric activation of phosphorylase b accounts for the accelerated glycogenolysis in CK-/- muscle during contraction."xsd:string |
| http://purl.uniprot.org/citations/12963789 | http://purl.org/dc/terms/identifier | "doi:10.1113/jphysiol.2003.051078"xsd:string |
| http://purl.uniprot.org/citations/12963789 | http://purl.uniprot.org/core/author | "Yu J."xsd:string |
| http://purl.uniprot.org/citations/12963789 | http://purl.uniprot.org/core/author | "Katz A."xsd:string |
| http://purl.uniprot.org/citations/12963789 | http://purl.uniprot.org/core/author | "Wieringa B."xsd:string |
| http://purl.uniprot.org/citations/12963789 | http://purl.uniprot.org/core/author | "Norman B."xsd:string |
| http://purl.uniprot.org/citations/12963789 | http://purl.uniprot.org/core/author | "Westerblad H."xsd:string |
| http://purl.uniprot.org/citations/12963789 | http://purl.uniprot.org/core/author | "Andersson D.C."xsd:string |
| http://purl.uniprot.org/citations/12963789 | http://purl.uniprot.org/core/author | "Sandstrom M.E."xsd:string |
| http://purl.uniprot.org/citations/12963789 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12963789 | http://purl.uniprot.org/core/name | "J Physiol"xsd:string |
| http://purl.uniprot.org/citations/12963789 | http://purl.uniprot.org/core/pages | "523-531"xsd:string |
| http://purl.uniprot.org/citations/12963789 | http://purl.uniprot.org/core/title | "Contraction-mediated glycogenolysis in mouse skeletal muscle lacking creatine kinase: the role of phosphorylase b activation."xsd:string |
| http://purl.uniprot.org/citations/12963789 | http://purl.uniprot.org/core/volume | "553"xsd:string |
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