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P<jats:sub>110<\/jats:sub>, P<jats:sub>88<\/jats:sub>, P<jats:sub>71,72<\/jats:sub>, and P<jats:sub>23<\/jats:sub> had unique peptide maps. Evidence of a 27,000 dalton precursor to P<jats:sub>23<\/jats:sub> was obtained. The analogue\u2010stimulated proteins were not related to another set of inducible avian polypeptides known as the glucose\u2010regulated proteins. In mammalian cells, the rate of accumulation of several polypeptides, which were similar in size to the avian proteins, sharply increased after canavanine treatment.<\/jats:p><jats:p>Proteins with the same electrophoretic mobilities, isoelectric points, and peptide maps as the analogue\u2010stimulated proteins were expressed at low levels in untreated cultures. To determine the time courses of the canavanine\u2010mediated increases in protein accumulation and the recovery of protein metabolism after analogue treatment, radioactively labeled proteins were extracted from CE cells and analyzed on SDS\u2010polyacrylamide gels. In cultures exposed to canavanine, the rates of accumulation of P<jats:sub>88<\/jats:sub> and P<jats:sub>71,72<\/jats:sub> increased from basal to new plateau levels in about 1.5 hours, while P<jats:sub>23<\/jats:sub> required about 2.5 hours. When added with the analogue, actinomycin D and cordycepin blocked the increases in protein accumulation. These inhibitors also blocked the rapid decline in the rates of accumulation of the enhanced proteins which occurred after removal of canavanine. Studies of the metabolic stability of the enhanced proteins indicated that the changes in their accumulation were caused by alterations in their rates of synthesis. Thus, the analogue\u2010mediated response fulfilled several of the criteria for inducible eucaryotic gene expression.<\/jats:p><jats:p>The amino acid analogue p\u2010fluorophenylalanine and the chain\u2010terminating analogue of amino acyl\u2010tRNA puromycin stimulated the synthesis of the same set of proteins induced by canavanine. The enhanced synthesis of these proteins appeared to be a cellular response to either the presence or catabolism of abnormal proteins and puromycyl peptides.<\/jats:p>","DOI":"10.1002\/jcp.1041020315","type":"journal-article","created":{"date-parts":[[2005,2,26]],"date-time":"2005-02-26T16:23:09Z","timestamp":1109434989000},"page":"407-427","source":"Crossref","is-referenced-by-count":306,"title":["Cultured animal cells exposed to amino acid analogues or puromycin rapidly synthesize several polypeptides"],"prefix":"10.1002","volume":"102","author":[{"given":"Lawrence E.","family":"Hightower","sequence":"first","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2005,2,4]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(72)90397-X"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/0042-6822(77)90217-3"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)91397-9"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00648a026"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj0910340"},{"key":"e_1_2_1_7_1","first-page":"1","article-title":"Intracellular protein degradation","volume":"13","author":"Ballard F. 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