High-level, heat-regulated synthesis of proteins in eukaryotic cells |
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| Authors: | M Dreano J Brochot A Myers C Cheng-Meyer D Rungger R Voellmy P Bromley |
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| Institution: | 1. Department of Radiology, Wake Forest School of Medicine, Winston-Salem 27157, USA;2. Comprehensive Cancer Center, Brain Tumor Center of Excellence, Wake Forest School of Medicine, Winston-Salem 27157, USA;3. Department of Biomedical Engineering, Wake Forest School of Medicine, Winston-Salem 27157, USA;4. Department of Biostatistics Sciences, Wake Forest School of Medicine, Winston-Salem 27157, USA;1. Department of Dermatology, Hubei Maternity and Child Health Hospital, Wuhan, China;2. Department of Gynecology, Hubei Maternity and Child Health Hospital, Wuhan, China;3. Department of Pathology, Renmin Hospital of Wuhan University, Wuhan, China;4. Department of Dermatology, The Third Affiliated Hospital of Soochow University, Changzhou, China;5. Key Lab of the Ministry of Education for Plant Developmental Biology, College of Life Sciences, Wuhan University, Wuhan, China;6. Department of Dermatology, The Second Affiliated Hospital, Xi''an Jiaotong University, Xi’an, China |
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| Abstract: | Plasmids have been constructed in which promoters of 70-kDa heat-shock protein genes (hsp70) of human and Drosophila origin were linked to three different eukaryotic genes encoding human growth hormone (hGH), chicken lysozyme (cL) and a human influenza haemagglutinin (HA). Following transfection into widely divergent eukaryotic cells, the hybrid genes direct the transient, heat-regulated synthesis of the three proteins. hGH and cL are secreted into the medium. A human hsp70-hGH construct was used to establish stable mouse fibroblast lines that are capable of producing and secreting hGH at high levels following heat induction: hGH is secreted at a 500-1200-fold higher rate by heat-treated than by untreated cells. |
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