{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T10:53:16Z","timestamp":1789901596483,"version":"4.0.1"},"reference-count":58,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2012,3,13]],"date-time":"2012-03-13T00:00:00Z","timestamp":1331596800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100002910","name":"F\u00e9d\u00e9ration Wallonie-Bruxelles","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002910","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000780","name":"European Commission","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000780","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["faseb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FASEB Journal"],"published-print":{"date-parts":[[2012,6]]},"abstract":"<jats:p>\n                    We investigated whether overexpression of AMP\u2010metabolizing enzymes in intact cells would modulate oligomycin\u2010induced AMPK activation. Human embryonic kidney (HEK) 293T cells were transiently transfected with increasing amounts of plasmid vectors to obtain a graded increase in overexpression of AMP\u2010deaminase (AMPD) 1, AMPD2, and soluble 5'\u2010nucleotidase IA (cN\u2010IA) for measurements of AMPK activation and total intracellular adenine nucleotide levels induced by oligomycin treatment. Overexpression of AMPD1 and AMPD2 slightly decreased AMP levels and oligomycin\u2010induced AMPK activation. Increased overexpression of cN\u2010IA led to reductions in the oligomycin\u2010induced increases in AMP and ADP concentrations by ~70 and 50%, respectively, concomitant with a 50% decrease in AMPK activation. The results support the view that a rise in ADP as well as AMP is important for activation of AMPK, which can thus be regulated by the adenylate energy charge. The control coefficient of cN\u2010IA on AMP was 0.3\u20100.7, whereas the values for AMPD1 and AMPD2 were &gt;0.1, suggesting that in this model cN\u2010IA exerts a large proportion of control over intracellular AMP. Therefore, small molecule inhibition of cN\u2010IA could be a strategy for AMPK activation.\u2014Plaideau, C., Liu, J., Hartleib\u2010Geschwindner, J., Bastin\u2010Coyette, L., Bontemps, F., Oscarsson, J., Hue, L., Rider, M. H. Overexpression of AMP\u2010metabolizing enzymes controls adenine nucleotide levels and AMPK activation in HEK293T cells.\n                    <jats:italic>FASEB J.<\/jats:italic>\n                    26, 2685\u20102694 (2012).\n                    <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.fasebj.org\">www.fasebj.org<\/jats:ext-link>\n                  <\/jats:p>","DOI":"10.1096\/fj.11-198168","type":"journal-article","created":{"date-parts":[[2012,3,14]],"date-time":"2012-03-14T20:18:44Z","timestamp":1331756324000},"page":"2685-2694","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":26,"title":["Overexpression of AMP\u2010metabolizing enzymes controls adenine nucleotide levels and AMPK activation in HEK293T cells"],"prefix":"10.1096","volume":"26","author":[{"given":"Catheline","family":"Plaideau","sequence":"first","affiliation":[{"name":"Universit\u00e9 Catholique de Louvain and de Duve Institute Brussels Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jianming","family":"Liu","sequence":"additional","affiliation":[{"name":"AstraZeneca Research and Development M\u00f6lndal Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Judith","family":"Hartleib\u2010Geschwindner","sequence":"additional","affiliation":[{"name":"AstraZeneca Research and Development M\u00f6lndal Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laurent","family":"Bastin\u2010Coyette","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Catholique de Louvain and de Duve Institute Brussels Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fran\u00e7oise","family":"Bontemps","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Catholique de Louvain and de Duve Institute Brussels Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jan","family":"Oscarsson","sequence":"additional","affiliation":[{"name":"AstraZeneca Research and Development M\u00f6lndal Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Louis","family":"Hue","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Catholique de Louvain and de Duve Institute Brussels Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark H.","family":"Rider","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Catholique de Louvain and de Duve Institute Brussels Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2012,3,13]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1152\/physrev.00011.2008"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biochem.67.1.821"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.cmet.2004.12.003"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.tibs.2005.11.009"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1042\/BJ20082055"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(95)01368-7"},{"issue":"3","key":"e_1_2_7_8_1","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1042\/bj3380717","article-title":"AMP\u2010activated protein kinase: an ultrasensitive system for monitoring cellular energy charge","volume":"338","author":"Hardie D. 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