{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,13]],"date-time":"2026-02-13T17:10:17Z","timestamp":1771002617879,"version":"3.50.1"},"reference-count":24,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2005,2,4]],"date-time":"2005-02-04T00:00:00Z","timestamp":1107475200000},"content-version":"vor","delay-in-days":8588,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal Cellular Physiology"],"published-print":{"date-parts":[[1981,8]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Cultured rat embryo cells exposed to the L\u2010arginine analogue L\u2010canavanine rapidly accumulated a major 71 kilodalton polypeptide and several minor ones (110, 95, 88, and 78 kilodaltons). Canavanine\u2010treated cultures contained elevated levels of translatable mRNA encoding P<jats:sub>71<\/jats:sub>, and the stimulated synthesis of this protein was blocked by actinomycin D, suggesting that P<jats:sub>71<\/jats:sub> is inducible. Rat embryo cells maintained under routine culture conditions synthesized only trace amounts of P<jats:sub>71<\/jats:sub>; however, they accumulated an abundant 73 kilodalton protein that was closely related to P<jats:sub>71<\/jats:sub>. No kinetic evidence of a precursor\u2010product relationship between P<jats:sub>73<\/jats:sub> and P<jats:sub>71<\/jats:sub> was found. The peptide map of P<jats:sub>71<\/jats:sub> from cultured cells was identical to the map of proteins with the same electrophoretic mobility isolated from incubated slices of rat telencephalon. Previous studies (White, \u203280a, b, c) have shown that the latter proteins are rapidly synthesized by cells associated with cerebral microvessels in incubated brain slices, but are not detectable in vivo. Herein we present evidence that the synthesis of P<jats:sub>71<\/jats:sub> is not unique to brain slices. Incubated slices of heart, lung, thymus, kidney, spleen, and liver all accumulated an abundant 71 kilodalton size class. The peptide maps of P<jats:sub>71<\/jats:sub> obtained from brain, heart, lung, and thymus tissue were similar. The stimulated synthesis of P<jats:sub>71<\/jats:sub> in brain, heart, and lung slices was inhibited strongly by the addition of actinomycin D at the start of incubation. The 71\u201373 kilodalton proteins of canavanine\u2010treated rat embryo cells and incubated slices from seven different organs were compared in detail on two\u2010dimensional poly\u2010acrylamide gels. Eight charge variants were detected in extracts of lung, spleen, and thymus tissue, four in liver and heart, three in kidney, and two different pairs of variants in extracts of brain tissue and cultured cells. The possible significance of the rapid synthesis of a similar small set of proteins in tissue slices and cultured cells in response to a variety of physical, chemical, and biological stimuli is discussed in terms of cellular responses to traumatic injury and metabolic stress.<\/jats:p>","DOI":"10.1002\/jcp.1041080216","type":"journal-article","created":{"date-parts":[[2005,2,26]],"date-time":"2005-02-26T15:46:46Z","timestamp":1109432806000},"page":"261-275","source":"Crossref","is-referenced-by-count":117,"title":["Cellular responses to stress: Comparison of a family of 71\u201373\u2010kilodalton proteins rapidly synthesized in rat tissue slices and canavanine\u2010treated cells in culture"],"prefix":"10.1002","volume":"108","author":[{"given":"Lawrence E.","family":"Hightower","sequence":"first","affiliation":[]},{"given":"Fredric P.","family":"White","sequence":"additional","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\/0092-8674(79)90150-8"},{"key":"e_1_2_1_3_1","doi-asserted-by":"crossref","first-page":"1102","DOI":"10.1016\/S0021-9258(19)75212-0","article-title":"Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis","volume":"253","author":"Cleveland D. 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