{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,7]],"date-time":"2026-02-07T22:43:14Z","timestamp":1770504194673,"version":"3.49.0"},"reference-count":0,"publisher":"Canadian Science Publishing","issue":"11-12","license":[{"start":{"date-parts":[[1994,11,1]],"date-time":"1994-11-01T00:00:00Z","timestamp":783648000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.nrcresearchpress.com\/page\/about\/CorporateTextAndDataMining"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochem. Cell Biol."],"published-print":{"date-parts":[[1994,11,1]]},"abstract":"<jats:p> The antiapoptosis potential of bcl-2 has now been well established. But the biochemical mechanism of bcl-2 action is still poorly understood. Using the phosphatase inhibitor okadaic acid (OA) or chemotherapeutic agents such as Taxol and 5\u2032-fluorouracil, we found that bcl-2 can be phosphorylated. Since OA or Taxol treatment leads to apoptosis, it seems that phosphorylation of bcl-2 leads to its inactivation. Exposure of several lymphoid cell lines expressing differential amounts of bcl-2 protein to OA resulted in apoptosis of the cells and hyperphosphorylation of bcl-2. Interestingly, the lymphoblastoid cell lines that did not phosphorylate bcl-2 following OA exposure did not undergo apoptosis. Moreover, pro-B cells isolated from patients with acute lymphoblastic leukemias exhibited endogenous phosphorylated forms of bcl-2 and a large number of apoptotic cells, even without OA treatment. Treatment with the phosphatase inhibitor or with chemotherapeutic agents (Taxol, 5\u2032-fluorouracil) led to severe apoptosis of these cells, along with hyperphosphorylation of bcl-2. Phosphoamino acid analysis reveals that bcl-2 is phosphorylated at a serine residue. In summary, our investigation indicates that the phosphorylation pathway involving bcl-2 can be the determinant of cell death in lymphocytes.Key words: bcl-2, oncogene, apoptosis, phosphorylation, dephosphorylation. <\/jats:p>","DOI":"10.1139\/o94-061","type":"journal-article","created":{"date-parts":[[2009,12,23]],"date-time":"2009-12-23T19:50:41Z","timestamp":1261597841000},"page":"455-462","source":"Crossref","is-referenced-by-count":39,"title":["Antiapoptosis potential of <i>bcl-2<\/i> oncogene by dephosphorylation"],"prefix":"10.1139","volume":"72","author":[{"given":"Subrata","family":"Haldar","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nilamani","family":"Jena","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Carlo M.","family":"Croce","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"155","container-title":["Biochemistry and Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/cdnsciencepub.com\/doi\/pdf\/10.1139\/o94-061","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,7,2]],"date-time":"2025-07-02T18:33:53Z","timestamp":1751481233000},"score":1,"resource":{"primary":{"URL":"https:\/\/cdnsciencepub.com\/doi\/10.1139\/o94-061"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1994,11,1]]},"references-count":0,"journal-issue":{"issue":"11-12","published-print":{"date-parts":[[1994,11,1]]}},"alternative-id":["10.1139\/o94-061"],"URL":"https:\/\/doi.org\/10.1139\/o94-061","relation":{},"ISSN":["0829-8211","1208-6002"],"issn-type":[{"value":"0829-8211","type":"print"},{"value":"1208-6002","type":"electronic"}],"subject":[],"published":{"date-parts":[[1994,11,1]]}}}