{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T16:09:59Z","timestamp":1781107799578,"version":"3.54.1"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"2","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1972,2]]},"abstract":"<jats:p>\n                    Cyclic AMP-phosphodiesterase is present in various mouse fibroblasts. Contact-inhibited 3T3 cells contain two forms of the enzyme, one with a\n                    <jats:italic>\n                      K\n                      <jats:sub>m<\/jats:sub>\n                    <\/jats:italic>\n                    of 2.5 \u03bcM and the second with a\n                    <jats:italic>\n                      K\n                      <jats:sub>m<\/jats:sub>\n                    <\/jats:italic>\n                    of 71 \u03bcM. As 3T3 cells grow to confluency and cAMP concentrations rise, the activity of the first enzyme increases, whereas that of the second is unchanged. A line of SV40-transformed 3T3 cells with low cAMP concentration also has low levels of the cAMP-phosphodiesterase with a\n                    <jats:italic>\n                      K\n                      <jats:sub>m<\/jats:sub>\n                    <\/jats:italic>\n                    of 2.5 \u03bcM. Treatment of 3T3 and SV40-transformed 3T3 cells with dibutyryl cAMP and theophylline increases cAMP-phosphodiesterase accumulation. This accumulation is blocked by cycloheximide and actinomycin D. The newly formed enzyme resembles the higher affinity enzyme present in unstimulated cells, since it has a\n                    <jats:italic>\n                      K\n                      <jats:sub>m<\/jats:sub>\n                    <\/jats:italic>\n                    of 1.2-2.0 \u03bcM, and is stimulated by snake venom. In L cells in which cAMP concentrations are elevated by treatment with prostaglandin E\n                    <jats:sub>1<\/jats:sub>\n                    , cAMP phosphodiesterase also accumulates. We conclude that intracellular concentrations of cAMP regulate the synthesis of cAMP-phosphodiesterase, and that cAMP functions as an inducer of the enzyme.\n                  <\/jats:p>","DOI":"10.1073\/pnas.69.2.459","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T02:32:44Z","timestamp":1149042764000},"page":"459-462","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":88,"title":["Regulation of Adenosine 3\u2032:5\u2032-Cyclic Monophosphate Phosphodiesterase Activity in Fibroblasts by Intracellular Concentrations of Cyclic Adenosine Monophosphate"],"prefix":"10.1073","volume":"69","author":[{"given":"Massimo","family":"D'Armiento","sequence":"first","affiliation":[{"name":"Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20014"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"George S.","family":"Johnson","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20014"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ira","family":"Pastan","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20014"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1972,2]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.69.2.459","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T10:28:40Z","timestamp":1649845720000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.69.2.459"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1972,2]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1972,2]]}},"alternative-id":["10.1073\/pnas.69.2.459"],"URL":"https:\/\/doi.org\/10.1073\/pnas.69.2.459","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1972,2]]},"assertion":[{"value":"1972-02-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}