{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,12]],"date-time":"2026-09-12T09:02:36Z","timestamp":1789203756019,"version":"build-2803163510"},"reference-count":28,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2006,6,9]],"date-time":"2006-06-09T00:00:00Z","timestamp":1149811200000},"content-version":"vor","delay-in-days":4391,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J. Biochem. Toxicol."],"published-print":{"date-parts":[[1994,6]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The chemical TCDD (2,3,7,8\u2010tetrachlorodibenzo\u2010<jats:italic>p<\/jats:italic>\u2010dioxin) at very low concentrations has been found to cause a rapid rise in protein phosphorylation activities in the extranuclear fraction (i.e., cytosol and cellular membranes) of the adipose tissue from male guinea pigs. The effect occurred both <jats:italic>in vivo<\/jats:italic> and when TCDD was added to adipose in tissue culture (<jats:italic>in situ<\/jats:italic>). To study the cause for such a TCDD\u2010induced biochemical change, isolated adipose tissues were treated with TCDD in conjunction with various diagnostic agents known to affect protein synthesis (actinomycin D and cycloheximide) and protein phosphorylation activities (genistein). The stimulatory effect of TCDD on protein phosphorylation was not totally abolished by actinomycin D; however, cycloheximide and genistein partially suppressed the effect of TCDD. Such an action of TCDD was accompanied by a quick rise in <jats:italic>ras<\/jats:italic> GTP binding activity as well as a rise in phosphorylation of nuclear c\u2010myc protein product within 10 minutes after TCDD addition, indicating that TCDD is likely to activate the signal transduction pathway for growth factors. In view of the absence of an inhibitory action of actinomycin D and the short time required for TCDD to induce these changes, we have formulated a working hypothesis that stimulation of protein phosphorylation activities by TCDD may not be mediated by a transcriptional process. To test this possibility, an extranuclear fraction was obtained from the homogenate of adipose tissue, and the effect of TCDD was studied <jats:italic>in vitro cell\u2010and nucleus\u2010free<\/jats:italic> conditions. It was found that TCDD was capable of activating protein phosphorylation activity under <jats:italic>cell free<\/jats:italic> conditions even in the absence of nuclei. Such an action of TCDD is dependent on the action of the Ah receptor.<\/jats:p>","DOI":"10.1002\/jbt.2570090308","type":"journal-article","created":{"date-parts":[[2006,10,18]],"date-time":"2006-10-18T02:04:40Z","timestamp":1161137080000},"page":"159-170","source":"Crossref","is-referenced-by-count":30,"title":["Significance of TCDD\u2010induced changes in protein phosphorylation in the adipocyte of male guinea pigs"],"prefix":"10.1002","volume":"9","author":[{"given":"Essam","family":"Enan","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fumio","family":"Matsumura","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2006,6,9]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.pa.22.040182.002505"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.pa.30.040190.001343"},{"key":"e_1_2_1_4_2","first-page":"500","volume-title":"Biological Mechanisms of Dioxin Actions, Banbury Report","author":"Poland A.","year":"1984"},{"key":"e_1_2_1_5_2","doi-asserted-by":"publisher","DOI":"10.1080\/03601238809372617"},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.256.5060.1193"},{"key":"e_1_2_1_7_2","first-page":"3436","article-title":"Doseresponse relationships for chronic exposure to 2,3,7,8\u2010tetrachlorodibenzo\u2010p\u2010dioxin in a rat tumor promotion model: quantification and immunolocalization of CYP1A1 and CYP1A2 in the liver","volume":"52","author":"Tritscher A. 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