{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T16:51:38Z","timestamp":1791478298613,"version":"4.3.4"},"reference-count":53,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2002,6,1]],"date-time":"2002-06-01T00:00:00Z","timestamp":1022889600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The Journal of Physiology"],"published-print":{"date-parts":[[2002,6]]},"abstract":"<jats:p>It has been suggested that 5\u2032AMP\u2010activated protein kinase (AMPK) is involved in the regulation of glucose and glycogen metabolism in skeletal muscle. We used patients with chronic high muscle glycogen stores and deficient glycogenolysis (McArdle's disease) as a model to address this issue. Six McArdle patients were compared with control subjects during exercise. Muscle \u03b12AMPK activity increased in McArdle patients (from 1.3 \u00b1 0.2 to 1.9 \u00b1 0.2 pmol min<jats:sup>\u22121<\/jats:sup> mg<jats:sup>\u22121<\/jats:sup>, <jats:styled-content><jats:italic>P<\/jats:italic>= 0.05<\/jats:styled-content>) but not in control subjects (from 1.0 \u00b1 0.1 to 1.3 \u00b1 0.3 pmol min<jats:sup>\u22121<\/jats:sup> mg<jats:sup>\u22121<\/jats:sup>). Exercise\u2010induced phosphorylation of the <jats:italic>in vivo<\/jats:italic> AMPK substrate acetyl CoA carboxylase (ACC\u03b2; Ser<jats:sup>221<\/jats:sup>) was higher (<jats:styled-content><jats:italic>P<\/jats:italic> &lt; 0.01<\/jats:styled-content>) in McArdle patients than in control subjects (18 \u00b1 3 <jats:italic>vs.<\/jats:italic> 10 \u00b1 1 arbitrary units). Exercise\u2010induced whole\u2010body glucose utilization was also higher in McArdle patients than in control subjects (<jats:styled-content><jats:italic>P<\/jats:italic> &lt; 0.05<\/jats:styled-content>). No correlation between individual AMPK or ACC\u03b2 values and glucose utilization was observed. Glycogen synthase (GS) activity was decreased in McArdle patients from 11 \u00b1 1.3 to 5 \u00b1 1.2 % (<jats:styled-content><jats:italic>P<\/jats:italic> &lt; 0.05<\/jats:styled-content>) and increased in control subjects from 19 \u00b1 1.6 to 23 \u00b1 2.3 % (<jats:styled-content><jats:italic>P<\/jats:italic> &lt; 0.05<\/jats:styled-content>) in response to exercise. This was not associated with activity changes of GS kinase 3 or protein phosphatase 1, but the changes in GS activity could be due to changes in activity of AMPK or protein kinase A (PKA) as a negative correlation between either ACC\u03b2 phosphorylation (Ser<jats:sup>221<\/jats:sup>) or plasma adrenaline and GS activity was observed. These findings suggest that GS activity is increased by glycogen breakdown and decreased by AMPK and possibly PKA activation and that the resultant GS activity depends on the relative strengths of the various stimuli. Furthermore, AMPK may be involved in the regulation of glucose utilization during exercise in humans, although the lack of correlation between individual AMPK activity or ACC\u03b2 phosphorylation (Ser<jats:sup>221<\/jats:sup>) values and individual glucose utilization during exercise implies that AMPK may not be an essential regulator.<\/jats:p>","DOI":"10.1113\/jphysiol.2002.018044","type":"journal-article","created":{"date-parts":[[2002,7,28]],"date-time":"2002-07-28T23:15:15Z","timestamp":1027898115000},"page":"979-989","source":"Crossref","is-referenced-by-count":77,"title":["Role of 5\u2032AMP\u2010activated protein kinase in glycogen synthase activity and glucose utilization: insights from patients with McArdle's disease"],"prefix":"10.1113","volume":"541","author":[{"given":"Jakob N.","family":"Nielsen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J\u00f8rgen F. 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